Full text data of TMED10
TMED10
(TMP21)
[Confidence: high (present in two of the MS resources)]
Transmembrane emp24 domain-containing protein 10 (21 kDa transmembrane-trafficking protein; S31III125; S31I125; Tmp-21-I; Transmembrane protein Tmp21; p23; p24 family protein delta-1; p24delta1; p24delta; Flags: Precursor)
Transmembrane emp24 domain-containing protein 10 (21 kDa transmembrane-trafficking protein; S31III125; S31I125; Tmp-21-I; Transmembrane protein Tmp21; p23; p24 family protein delta-1; p24delta1; p24delta; Flags: Precursor)
hRBCD
IPI00028055
IPI00028055 Transmembrane protein Tmp21 precursor Transmembrane protein Tmp21 precursor membrane n/a 1 2 1 2 n/a 1 n/a n/a n/a 1 n/a 1 n/a n/a n/a n/a n/a 1 n/a Type I membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00028055 Transmembrane protein Tmp21 precursor Transmembrane protein Tmp21 precursor membrane n/a 1 2 1 2 n/a 1 n/a n/a n/a 1 n/a 1 n/a n/a n/a n/a n/a 1 n/a Type I membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
P49755
ID TMEDA_HUMAN Reviewed; 219 AA.
AC P49755; B2R605; Q15602; Q16536; Q86TC2; Q86TS5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-DEC-1998, sequence version 2.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Transmembrane emp24 domain-containing protein 10;
DE AltName: Full=21 kDa transmembrane-trafficking protein;
DE AltName: Full=S31III125;
DE Short=S31I125;
DE AltName: Full=Tmp-21-I;
DE AltName: Full=Transmembrane protein Tmp21;
DE AltName: Full=p23;
DE AltName: Full=p24 family protein delta-1;
DE Short=p24delta1;
DE AltName: Full=p24delta;
DE Flags: Precursor;
GN Name=TMED10; Synonyms=TMP21;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8663407; DOI=10.1074/jbc.271.29.17183;
RA Blum R., Feick P., Puype M., Vandekerckhove J., Klengel R.,
RA Nastainczyk W., Schulz I.;
RT "Tmp21 and p24A, two type I proteins enriched in pancreatic microsomal
RT membranes, are members of a protein family involved in vesicular
RT trafficking.";
RL J. Biol. Chem. 271:17183-17189(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sanseau P., Sherington R., Trower M.K., St George-Hyslop P.H.,
RA Dykes C.W.;
RT "New human gene, member of a large family implicated in protein
RT trafficking.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7596406; DOI=10.1038/375754a0;
RA Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G.,
RA Ikeda M., Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L.,
RA Foncin J.-F., Bruni A.C., Montesi M.P., Sorbi S., Rainero I.,
RA Pinessi L., Nee L., Chumakov I., Pollen D., Brookes A., Sanseau P.,
RA Polinsky R.J., Wasco W., da Silva H.A.R., Haines J.L.,
RA Pericak-Vance M.A., Tanzi R.E., Roses A.D., Fraser P.E., Rommens J.M.,
RA St George-Hyslop P.H.;
RT "Cloning of a gene bearing missense mutations in early-onset familial
RT Alzheimer's disease.";
RL Nature 375:754-760(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=10376215;
RA Hoerer J., Blum R., Feick P., Nastainczyk W., Schulz I.;
RT "A comparative study of rat and human Tmp21 (p23) reveals the
RT pseudogene-like features of human Tmp21-II.";
RL DNA Seq. 10:121-126(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 32-42.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective
RT labeling of protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [12]
RP SUBCELLULAR LOCATION, ASSOCIATION WITH COPI AND COPII VESICLE COAT,
RP AND MUTAGENESIS OF 211-PHE-PHE-212 AND 215-LYS-LYS-216.
RX PubMed=9472029; DOI=10.1083/jcb.140.4.751;
RA Dominguez M., Dejgaard K., Fullekrug J., Dahan S., Fazel A.,
RA Paccaud J.P., Thomas D.Y., Bergeron J.J., Nilsson T.;
RT "gp25L/emp24/p24 protein family members of the cis-Golgi network bind
RT both COP I and II coatomer.";
RL J. Cell Biol. 140:751-765(1998).
RN [13]
RP FUNCTION.
RX PubMed=10052452; DOI=10.1016/S0092-8674(00)80654-6;
RA Bremser M., Nickel W., Schweikert M., Ravazzola M., Amherdt M.,
RA Hughes C.A., Sollner T.H., Rothman J.E., Wieland F.T.;
RT "Coupling of coat assembly and vesicle budding to packaging of
RT putative cargo receptors.";
RL Cell 96:495-506(1999).
RN [14]
RP SUBUNIT.
RX PubMed=10359607; DOI=10.1091/mbc.10.6.1939;
RA Fullekrug J., Suganuma T., Tang B.L., Hong W., Storrie B., Nilsson T.;
RT "Localization and recycling of gp27 (hp24gamma3): complex formation
RT with other p24 family members.";
RL Mol. Biol. Cell 10:1939-1955(1999).
RN [15]
RP MUTAGENESIS OF 211-PHE-PHE-212 AND 215-LYS-LYS-216.
RX PubMed=10761932; DOI=10.1016/S0092-8674(00)80703-5;
RA Goldberg J.;
RT "Decoding of sorting signals by coatomer through a GTPase switch in
RT the COPI coat complex.";
RL Cell 100:671-679(2000).
RN [16]
RP INTERACTION WITH COPG1, AND MUTAGENESIS OF 211-PHE-PHE-212 AND
RP 215-LYS-LYS-216.
RX PubMed=11056392;
RA Futatsumori M., Kasai K., Takatsu H., Shin H.-W., Nakayama K.;
RT "Identification and characterization of novel isoforms of COP I
RT subunits.";
RL J. Biochem. 128:793-801(2000).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=10852829;
RA Emery G., Rojo M., Gruenberg J.;
RT "Coupled transport of p24 family members.";
RL J. Cell Sci. 113:2507-2516(2000).
RN [18]
RP FUNCTION, AND INTERACTION WITH ARF1.
RX PubMed=11726511; DOI=10.1093/emboj/20.23.6751;
RA Gommel D.U., Memon A.R., Heiss A., Lottspeich F., Pfannstiel J.,
RA Lechner J., Reinhard C., Helms J.B., Nickel W., Wieland F.T.;
RT "Recruitment to Golgi membranes of ADP-ribosylation factor 1 is
RT mediated by the cytoplasmic domain of p23.";
RL EMBO J. 20:6751-6760(2001).
RN [19]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=12237308; DOI=10.1074/jbc.M206989200;
RA Jenne N., Frey K., Brugger B., Wieland F.T.;
RT "Oligomeric state and stoichiometry of p24 proteins in the early
RT secretory pathway.";
RL J. Biol. Chem. 277:46504-46511(2002).
RN [20]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [21]
RP INTERACTION WITH COPG1.
RX PubMed=16940185; DOI=10.1128/MCB.01055-06;
RA Bethune J., Kol M., Hoffmann J., Reckmann I., Brugger B., Wieland F.;
RT "Coatomer, the coat protein of COPI transport vesicles, discriminates
RT endoplasmic reticulum residents from p24 proteins.";
RL Mol. Cell. Biol. 26:8011-8021(2006).
RN [22]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16641999; DOI=10.1038/nature04667;
RA Chen F., Hasegawa H., Schmitt-Ulms G., Kawarai T., Bohm C.,
RA Katayama T., Gu Y., Sanjo N., Glista M., Rogaeva E., Wakutani Y.,
RA Pardossi-Piquard R., Ruan X., Tandon A., Checler F., Marambaud P.,
RA Hansen K., Westaway D., St George-Hyslop P., Fraser P.;
RT "TMP21 is a presenilin complex component that modulates gamma-
RT secretase but not epsilon-secretase activity.";
RL Nature 440:1208-1212(2006).
RN [23]
RP FUNCTION.
RX PubMed=17288597; DOI=10.1186/1750-1326-2-4;
RA Vetrivel K.S., Gong P., Bowen J.W., Cheng H., Chen Y., Carter M.,
RA Nguyen P.D., Placanica L., Wieland F.T., Li Y.M., Kounnas M.Z.,
RA Thinakaran G.;
RT "Dual roles of the transmembrane protein p23/TMP21 in the modulation
RT of amyloid precursor protein metabolism.";
RL Mol. Neurodegener. 2:4-4(2007).
RN [24]
RP IDENTIFICATION IN A COMPLEX WITH SURF4 AND TMED2.
RX PubMed=18287528; DOI=10.1091/mbc.E07-10-0989;
RA Mitrovic S., Ben-Tekaya H., Koegler E., Gruenberg J., Hauri H.-P.;
RT "The cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate
RT compartment (ERGIC)-53, and p25 are required to maintain the
RT architecture of ERGIC and Golgi.";
RL Mol. Biol. Cell 19:1976-1990(2008).
RN [25]
RP INTERACTION WITH MPPE1.
RX PubMed=19837036; DOI=10.1016/j.cell.2009.08.040;
RA Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T.;
RT "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored
RT proteins from the ER to the Golgi.";
RL Cell 139:352-365(2009).
RN [26]
RP FUNCTION.
RX PubMed=19296914; DOI=10.1016/j.cellsig.2009.03.006;
RA Luo R., Ha V.L., Hayashi R., Randazzo P.A.;
RT "Arf GAP2 is positively regulated by coatomer and cargo.";
RL Cell. Signal. 21:1169-1179(2009).
RN [27]
RP FUNCTION.
RX PubMed=20427317; DOI=10.1242/jcs.062950;
RA Bonnon C., Wendeler M.W., Paccaud J.P., Hauri H.P.;
RT "Selective export of human GPI-anchored proteins from the endoplasmic
RT reticulum.";
RL J. Cell Sci. 123:1705-1715(2010).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [29]
RP INTERACTION WITH STX17.
RX PubMed=21545355; DOI=10.1042/BC20110006;
RA Muppirala M., Gupta V., Swarup G.;
RT "Syntaxin 17 cycles between the ER and ERGIC and is required to
RT maintain the architecture of ERGIC and Golgi.";
RL Biol. Cell 103:333-350(2011).
RN [30]
RP FUNCTION, AND INTERACTION WITH F2RL1.
RX PubMed=21219331; DOI=10.1111/j.1471-4159.2011.07173.x;
RA Luo W., Wang Y., Reiser G.;
RT "Proteinase-activated receptors, nucleotide P2Y receptors, and mu-
RT opioid receptor-1B are under the control of the type I transmembrane
RT proteins p23 and p24A in post-Golgi trafficking.";
RL J. Neurochem. 117:71-81(2011).
CC -!- FUNCTION: Involved in vesicular protein trafficking. Mainly
CC functions in the early secretory pathway. Thought to act as cargo
CC receptor at the lumenal side for incorporation of secretory cargo
CC molecules into transport vesicles and to be involved in vesicle
CC coat formation at the cytoplasmic side. In COPII vesicle-mediated
CC anterograde transport involved in the transport of GPI-anchored
CC proteins and proposed to act together with TMED2 as their cargo
CC receptor; the function specifically implies SEC24C and SEC24D of
CC the COPII vesicle coat and lipid raft-like microdomains of the ER.
CC Recognizes GPI anchors structural remodeled in the ER by PGAP1 and
CC MPPE1 (By similarity). In COPI vesicle-mediated retrograde
CC transport involved in the biogenesis of COPI vesicles and vesicle
CC coat recruitment. On Golgi membranes, acts as primary receptor for
CC ARF1-GDP which is involved in COPI-vesicle formation. Increases
CC coatomer-dependent GTPase-activating activity of ARFGAP2. Involved
CC in trafficking of G protein-coupled receptors (GPCRs). Regulates
CC F2LR1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the
CC plasma membrane thus contributing to receptor resensitization.
CC Involved in trafficking of amyloid beta A4 protein and soluble
CC APP-beta release (independent of modulation of gamma-secretase
CC activity). As part of the presenilin-dependent gamma-secretase
CC complex regulates gamma-cleavages of the amyloid beta A4 protein
CC to yield amyloid-beta 40 (Abeta40). Involved in organization of
CC the Golgi apparatus.
CC -!- SUBUNIT: Predominantly homodimeric and to lesser extent monomeric
CC in endoplasmic reticulum. Homodimer and monomer in endoplasmic
CC reticulum-Golgi intermediate compartment and cis-Golgi network.
CC Probably oligomerizes with other members of the EMP24/GP25L family
CC such as TMED2, TMED7 and TMED9. Interacts with TMED2. Associates
CC with the COPI vesicle coat (coatomer); TMED10:TMED2
CC heterotetramers are proposed to be involved in coatomer
CC association. Interacts (via C-terminus) with COPG1; the
CC interaction involves dimeric TMED10. Interacts with ARF1 (GDP-
CC bound); the interaction probably involves a TMED10 oligomer.
CC Interacts with SEC23A; indicative for an association of TMED10
CC with the COPII vesicle coat. Interacts with CD59, SEC24B, SEC24C
CC and SEC24D (By similarity). Interacts with MPPE1/PGAP5. Interacts
CC with F2LR1. Interacts with KDELR2; the interaction is disrupted by
CC KDELR2 ligand (By similarity). Found in a complex composed at
CC least of SURF4, TMED2 and TMED10. Associates with the presenilin-
CC dependent gamma-secretase complex. Interacts with STX17; the
CC interaction is direct.
CC -!- INTERACTION:
CC Q92542:NCSTN; NbExp=5; IntAct=EBI-998422, EBI-998440;
CC P49768:PSEN1; NbExp=3; IntAct=EBI-998422, EBI-297277;
CC Q9NZ42:PSENEN; NbExp=3; IntAct=EBI-998422, EBI-998468;
CC P17706-1:PTPN2; NbExp=5; IntAct=EBI-998422, EBI-4409481;
CC Q15363:TMED2; NbExp=7; IntAct=EBI-998422, EBI-998485;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane;
CC Single-pass type I membrane protein. Melanosome. Endoplasmic
CC reticulum membrane; Single-pass type I membrane protein.
CC Endoplasmic reticulum-Golgi intermediate compartment membrane;
CC Single-pass type I membrane protein. Cytoplasmic vesicle,
CC secretory vesicle membrane; Single-pass type I membrane protein
CC (By similarity). Cell membrane (By similarity). Golgi apparatus,
CC trans-Golgi network membrane; Single-pass type I membrane protein
CC (By similarity). Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV. Cycles between
CC compartments of the early secretatory pathway.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The lumenal domain mediates localization to the plasma
CC membrane by partially overriding the ER retention by the
CC cytoplasmic domain (By similarity).
CC -!- MISCELLANEOUS: Ectopic expression of TMED10 alone does not result
CC in its proper cis-Golgi network localization. Coexpression of
CC TMED2 is necessary, and coexpression of TMED3 and /or TMED9 is
CC facilitating localization.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family.
CC -!- SIMILARITY: Contains 1 GOLD domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC42003.1; Type=Frameshift; Positions=Several;
CC Sequence=CAD66561.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; X97442; CAA66071.1; -; mRNA.
DR EMBL; X97444; CAA66073.1; -; mRNA.
DR EMBL; U61734; AAB03625.1; -; Genomic_DNA.
DR EMBL; L40397; AAC42003.1; ALT_FRAME; mRNA.
DR EMBL; AJ004913; CAA06213.1; -; mRNA.
DR EMBL; BX248754; CAD66561.1; ALT_INIT; mRNA.
DR EMBL; AK312384; BAG35302.1; -; mRNA.
DR EMBL; AL832012; CAD89913.1; -; mRNA.
DR EMBL; AC007055; AAD31941.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81223.1; -; Genomic_DNA.
DR EMBL; BC001496; AAH01496.1; -; mRNA.
DR EMBL; BC001825; AAH01825.1; -; mRNA.
DR PIR; G01159; G01159.
DR RefSeq; NP_006818.3; NM_006827.5.
DR UniGene; Hs.74137; -.
DR ProteinModelPortal; P49755; -.
DR IntAct; P49755; 23.
DR MINT; MINT-3017717; -.
DR STRING; 9606.ENSP00000303145; -.
DR PhosphoSite; P49755; -.
DR DMDM; 3915893; -.
DR PaxDb; P49755; -.
DR PeptideAtlas; P49755; -.
DR PRIDE; P49755; -.
DR DNASU; 10972; -.
DR Ensembl; ENST00000303575; ENSP00000303145; ENSG00000170348.
DR GeneID; 10972; -.
DR KEGG; hsa:10972; -.
DR UCSC; uc001xrm.1; human.
DR CTD; 10972; -.
DR GeneCards; GC14M075598; -.
DR HGNC; HGNC:16998; TMED10.
DR HPA; CAB037251; -.
DR MIM; 605406; gene.
DR neXtProt; NX_P49755; -.
DR PharmGKB; PA128394579; -.
DR eggNOG; NOG323830; -.
DR HOVERGEN; HBG107275; -.
DR InParanoid; P49755; -.
DR OMA; VCFESKS; -.
DR OrthoDB; EOG7PZRZM; -.
DR PhylomeDB; P49755; -.
DR ChiTaRS; TMED10; human.
DR GeneWiki; TMED10; -.
DR GenomeRNAi; 10972; -.
DR NextBio; 41690; -.
DR PRO; PR:P49755; -.
DR ArrayExpress; P49755; -.
DR Bgee; P49755; -.
DR CleanEx; HS_TMED10; -.
DR Genevestigator; P49755; -.
DR GO; GO:0005801; C:cis-Golgi network; ISS:HGNC.
DR GO; GO:0030137; C:COPI-coated vesicle; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070765; C:gamma-secretase complex; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; ISS:HGNC.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISS:UniProtKB.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042589; C:zymogen granule membrane; ISS:HGNC.
DR GO; GO:0034205; P:beta-amyloid formation; IMP:UniProtKB.
DR GO; GO:0035459; P:cargo loading into vesicle; TAS:UniProtKB.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; TAS:UniProtKB.
DR GO; GO:0048208; P:COPII vesicle coating; TAS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IDA:UniProtKB.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0051259; P:protein oligomerization; IEA:Ensembl.
DR GO; GO:0045055; P:regulated secretory pathway; ISS:HGNC.
DR GO; GO:0001101; P:response to acid; IEA:Ensembl.
DR GO; GO:0043279; P:response to alkaloid; IEA:Ensembl.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; ISS:UniProtKB.
DR InterPro; IPR009038; GOLD.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Complete proteome; Cytoplasmic vesicle;
KW Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW Glycoprotein; Golgi apparatus; Membrane; Methylation; Polymorphism;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1 31
FT CHAIN 32 219 Transmembrane emp24 domain-containing
FT protein 10.
FT /FTId=PRO_0000010399.
FT TOPO_DOM 32 185 Lumenal (Potential).
FT TRANSMEM 186 206 Helical; (Potential).
FT TOPO_DOM 207 219 Cytoplasmic (Potential).
FT DOMAIN 41 193 GOLD.
FT REGION 1 142 Required for interaction with STX17.
FT REGION 147 178 Required for TMED10 and TMED2 cis-Golgi
FT network localization.
FT REGION 204 219 Interaction with COPG1.
FT REGION 207 219 Interaction with ARF1.
FT MOTIF 211 219 COPI vesicle coat-binding.
FT MOTIF 211 212 COPII vesicle coat-binding.
FT MOD_RES 171 171 Omega-N-methylated arginine (By
FT similarity).
FT MOD_RES 176 176 Omega-N-methylated arginine (By
FT similarity).
FT CARBOHYD 179 179 N-linked (GlcNAc...) (Potential).
FT VARIANT 64 64 S -> Y (in dbSNP:rs4929).
FT /FTId=VAR_012051.
FT VARIANT 152 152 R -> G (in dbSNP:rs17103066).
FT /FTId=VAR_049111.
FT MUTAGEN 211 212 FF->AA: Disrupts interaction with COPG1
FT and association with coatomer; when
FT associated with 215-A-A-216.
FT MUTAGEN 211 212 FF->AA: No decrease in binding to COPG1.
FT Disrupts interaction with SEC23A.
FT MUTAGEN 215 216 KK->AA: Disrupts interaction with COPG1
FT and association with coatomer; when
FT associated with 211-A-A-212.
FT MUTAGEN 215 216 KK->AA: Significant reduction in binding
FT to COPG1.
FT CONFLICT 75 75 K -> R (in Ref. 7; CAD89913).
SQ SEQUENCE 219 AA; 24976 MW; 0A0486BE65C4DBBB CRC64;
MSGLSGPPAR RGPFPLALLL LFLLGPRLVL AISFHLPINS RKCLREEIHK DLLVTGAYEI
SDQSGGAGGL RSHLKITDSA GHILYSKEDA TKGKFAFTTE DYDMFEVCFE SKGTGRIPDQ
LVILDMKHGV EAKNYEEIAK VEKLKPLEVE LRRLEDLSES IVNDFAYMKK REEEMRDTNE
STNTRVLYFS IFSMFCLIGL ATWQVFYLRR FFKAKKLIE
//
ID TMEDA_HUMAN Reviewed; 219 AA.
AC P49755; B2R605; Q15602; Q16536; Q86TC2; Q86TS5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-DEC-1998, sequence version 2.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=Transmembrane emp24 domain-containing protein 10;
DE AltName: Full=21 kDa transmembrane-trafficking protein;
DE AltName: Full=S31III125;
DE Short=S31I125;
DE AltName: Full=Tmp-21-I;
DE AltName: Full=Transmembrane protein Tmp21;
DE AltName: Full=p23;
DE AltName: Full=p24 family protein delta-1;
DE Short=p24delta1;
DE AltName: Full=p24delta;
DE Flags: Precursor;
GN Name=TMED10; Synonyms=TMP21;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8663407; DOI=10.1074/jbc.271.29.17183;
RA Blum R., Feick P., Puype M., Vandekerckhove J., Klengel R.,
RA Nastainczyk W., Schulz I.;
RT "Tmp21 and p24A, two type I proteins enriched in pancreatic microsomal
RT membranes, are members of a protein family involved in vesicular
RT trafficking.";
RL J. Biol. Chem. 271:17183-17189(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sanseau P., Sherington R., Trower M.K., St George-Hyslop P.H.,
RA Dykes C.W.;
RT "New human gene, member of a large family implicated in protein
RT trafficking.";
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7596406; DOI=10.1038/375754a0;
RA Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G.,
RA Ikeda M., Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L.,
RA Foncin J.-F., Bruni A.C., Montesi M.P., Sorbi S., Rainero I.,
RA Pinessi L., Nee L., Chumakov I., Pollen D., Brookes A., Sanseau P.,
RA Polinsky R.J., Wasco W., da Silva H.A.R., Haines J.L.,
RA Pericak-Vance M.A., Tanzi R.E., Roses A.D., Fraser P.E., Rommens J.M.,
RA St George-Hyslop P.H.;
RT "Cloning of a gene bearing missense mutations in early-onset familial
RT Alzheimer's disease.";
RL Nature 375:754-760(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=10376215;
RA Hoerer J., Blum R., Feick P., Nastainczyk W., Schulz I.;
RT "A comparative study of rat and human Tmp21 (p23) reveals the
RT pseudogene-like features of human Tmp21-II.";
RL DNA Seq. 10:121-126(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 32-42.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective
RT labeling of protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [12]
RP SUBCELLULAR LOCATION, ASSOCIATION WITH COPI AND COPII VESICLE COAT,
RP AND MUTAGENESIS OF 211-PHE-PHE-212 AND 215-LYS-LYS-216.
RX PubMed=9472029; DOI=10.1083/jcb.140.4.751;
RA Dominguez M., Dejgaard K., Fullekrug J., Dahan S., Fazel A.,
RA Paccaud J.P., Thomas D.Y., Bergeron J.J., Nilsson T.;
RT "gp25L/emp24/p24 protein family members of the cis-Golgi network bind
RT both COP I and II coatomer.";
RL J. Cell Biol. 140:751-765(1998).
RN [13]
RP FUNCTION.
RX PubMed=10052452; DOI=10.1016/S0092-8674(00)80654-6;
RA Bremser M., Nickel W., Schweikert M., Ravazzola M., Amherdt M.,
RA Hughes C.A., Sollner T.H., Rothman J.E., Wieland F.T.;
RT "Coupling of coat assembly and vesicle budding to packaging of
RT putative cargo receptors.";
RL Cell 96:495-506(1999).
RN [14]
RP SUBUNIT.
RX PubMed=10359607; DOI=10.1091/mbc.10.6.1939;
RA Fullekrug J., Suganuma T., Tang B.L., Hong W., Storrie B., Nilsson T.;
RT "Localization and recycling of gp27 (hp24gamma3): complex formation
RT with other p24 family members.";
RL Mol. Biol. Cell 10:1939-1955(1999).
RN [15]
RP MUTAGENESIS OF 211-PHE-PHE-212 AND 215-LYS-LYS-216.
RX PubMed=10761932; DOI=10.1016/S0092-8674(00)80703-5;
RA Goldberg J.;
RT "Decoding of sorting signals by coatomer through a GTPase switch in
RT the COPI coat complex.";
RL Cell 100:671-679(2000).
RN [16]
RP INTERACTION WITH COPG1, AND MUTAGENESIS OF 211-PHE-PHE-212 AND
RP 215-LYS-LYS-216.
RX PubMed=11056392;
RA Futatsumori M., Kasai K., Takatsu H., Shin H.-W., Nakayama K.;
RT "Identification and characterization of novel isoforms of COP I
RT subunits.";
RL J. Biochem. 128:793-801(2000).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=10852829;
RA Emery G., Rojo M., Gruenberg J.;
RT "Coupled transport of p24 family members.";
RL J. Cell Sci. 113:2507-2516(2000).
RN [18]
RP FUNCTION, AND INTERACTION WITH ARF1.
RX PubMed=11726511; DOI=10.1093/emboj/20.23.6751;
RA Gommel D.U., Memon A.R., Heiss A., Lottspeich F., Pfannstiel J.,
RA Lechner J., Reinhard C., Helms J.B., Nickel W., Wieland F.T.;
RT "Recruitment to Golgi membranes of ADP-ribosylation factor 1 is
RT mediated by the cytoplasmic domain of p23.";
RL EMBO J. 20:6751-6760(2001).
RN [19]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=12237308; DOI=10.1074/jbc.M206989200;
RA Jenne N., Frey K., Brugger B., Wieland F.T.;
RT "Oligomeric state and stoichiometry of p24 proteins in the early
RT secretory pathway.";
RL J. Biol. Chem. 277:46504-46511(2002).
RN [20]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
RA Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
RA Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
RA Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [21]
RP INTERACTION WITH COPG1.
RX PubMed=16940185; DOI=10.1128/MCB.01055-06;
RA Bethune J., Kol M., Hoffmann J., Reckmann I., Brugger B., Wieland F.;
RT "Coatomer, the coat protein of COPI transport vesicles, discriminates
RT endoplasmic reticulum residents from p24 proteins.";
RL Mol. Cell. Biol. 26:8011-8021(2006).
RN [22]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16641999; DOI=10.1038/nature04667;
RA Chen F., Hasegawa H., Schmitt-Ulms G., Kawarai T., Bohm C.,
RA Katayama T., Gu Y., Sanjo N., Glista M., Rogaeva E., Wakutani Y.,
RA Pardossi-Piquard R., Ruan X., Tandon A., Checler F., Marambaud P.,
RA Hansen K., Westaway D., St George-Hyslop P., Fraser P.;
RT "TMP21 is a presenilin complex component that modulates gamma-
RT secretase but not epsilon-secretase activity.";
RL Nature 440:1208-1212(2006).
RN [23]
RP FUNCTION.
RX PubMed=17288597; DOI=10.1186/1750-1326-2-4;
RA Vetrivel K.S., Gong P., Bowen J.W., Cheng H., Chen Y., Carter M.,
RA Nguyen P.D., Placanica L., Wieland F.T., Li Y.M., Kounnas M.Z.,
RA Thinakaran G.;
RT "Dual roles of the transmembrane protein p23/TMP21 in the modulation
RT of amyloid precursor protein metabolism.";
RL Mol. Neurodegener. 2:4-4(2007).
RN [24]
RP IDENTIFICATION IN A COMPLEX WITH SURF4 AND TMED2.
RX PubMed=18287528; DOI=10.1091/mbc.E07-10-0989;
RA Mitrovic S., Ben-Tekaya H., Koegler E., Gruenberg J., Hauri H.-P.;
RT "The cargo receptors Surf4, endoplasmic reticulum-Golgi intermediate
RT compartment (ERGIC)-53, and p25 are required to maintain the
RT architecture of ERGIC and Golgi.";
RL Mol. Biol. Cell 19:1976-1990(2008).
RN [25]
RP INTERACTION WITH MPPE1.
RX PubMed=19837036; DOI=10.1016/j.cell.2009.08.040;
RA Fujita M., Maeda Y., Ra M., Yamaguchi Y., Taguchi R., Kinoshita T.;
RT "GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored
RT proteins from the ER to the Golgi.";
RL Cell 139:352-365(2009).
RN [26]
RP FUNCTION.
RX PubMed=19296914; DOI=10.1016/j.cellsig.2009.03.006;
RA Luo R., Ha V.L., Hayashi R., Randazzo P.A.;
RT "Arf GAP2 is positively regulated by coatomer and cargo.";
RL Cell. Signal. 21:1169-1179(2009).
RN [27]
RP FUNCTION.
RX PubMed=20427317; DOI=10.1242/jcs.062950;
RA Bonnon C., Wendeler M.W., Paccaud J.P., Hauri H.P.;
RT "Selective export of human GPI-anchored proteins from the endoplasmic
RT reticulum.";
RL J. Cell Sci. 123:1705-1715(2010).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [29]
RP INTERACTION WITH STX17.
RX PubMed=21545355; DOI=10.1042/BC20110006;
RA Muppirala M., Gupta V., Swarup G.;
RT "Syntaxin 17 cycles between the ER and ERGIC and is required to
RT maintain the architecture of ERGIC and Golgi.";
RL Biol. Cell 103:333-350(2011).
RN [30]
RP FUNCTION, AND INTERACTION WITH F2RL1.
RX PubMed=21219331; DOI=10.1111/j.1471-4159.2011.07173.x;
RA Luo W., Wang Y., Reiser G.;
RT "Proteinase-activated receptors, nucleotide P2Y receptors, and mu-
RT opioid receptor-1B are under the control of the type I transmembrane
RT proteins p23 and p24A in post-Golgi trafficking.";
RL J. Neurochem. 117:71-81(2011).
CC -!- FUNCTION: Involved in vesicular protein trafficking. Mainly
CC functions in the early secretory pathway. Thought to act as cargo
CC receptor at the lumenal side for incorporation of secretory cargo
CC molecules into transport vesicles and to be involved in vesicle
CC coat formation at the cytoplasmic side. In COPII vesicle-mediated
CC anterograde transport involved in the transport of GPI-anchored
CC proteins and proposed to act together with TMED2 as their cargo
CC receptor; the function specifically implies SEC24C and SEC24D of
CC the COPII vesicle coat and lipid raft-like microdomains of the ER.
CC Recognizes GPI anchors structural remodeled in the ER by PGAP1 and
CC MPPE1 (By similarity). In COPI vesicle-mediated retrograde
CC transport involved in the biogenesis of COPI vesicles and vesicle
CC coat recruitment. On Golgi membranes, acts as primary receptor for
CC ARF1-GDP which is involved in COPI-vesicle formation. Increases
CC coatomer-dependent GTPase-activating activity of ARFGAP2. Involved
CC in trafficking of G protein-coupled receptors (GPCRs). Regulates
CC F2LR1, OPRM1 and P2RY4 exocytic trafficking from the Golgi to the
CC plasma membrane thus contributing to receptor resensitization.
CC Involved in trafficking of amyloid beta A4 protein and soluble
CC APP-beta release (independent of modulation of gamma-secretase
CC activity). As part of the presenilin-dependent gamma-secretase
CC complex regulates gamma-cleavages of the amyloid beta A4 protein
CC to yield amyloid-beta 40 (Abeta40). Involved in organization of
CC the Golgi apparatus.
CC -!- SUBUNIT: Predominantly homodimeric and to lesser extent monomeric
CC in endoplasmic reticulum. Homodimer and monomer in endoplasmic
CC reticulum-Golgi intermediate compartment and cis-Golgi network.
CC Probably oligomerizes with other members of the EMP24/GP25L family
CC such as TMED2, TMED7 and TMED9. Interacts with TMED2. Associates
CC with the COPI vesicle coat (coatomer); TMED10:TMED2
CC heterotetramers are proposed to be involved in coatomer
CC association. Interacts (via C-terminus) with COPG1; the
CC interaction involves dimeric TMED10. Interacts with ARF1 (GDP-
CC bound); the interaction probably involves a TMED10 oligomer.
CC Interacts with SEC23A; indicative for an association of TMED10
CC with the COPII vesicle coat. Interacts with CD59, SEC24B, SEC24C
CC and SEC24D (By similarity). Interacts with MPPE1/PGAP5. Interacts
CC with F2LR1. Interacts with KDELR2; the interaction is disrupted by
CC KDELR2 ligand (By similarity). Found in a complex composed at
CC least of SURF4, TMED2 and TMED10. Associates with the presenilin-
CC dependent gamma-secretase complex. Interacts with STX17; the
CC interaction is direct.
CC -!- INTERACTION:
CC Q92542:NCSTN; NbExp=5; IntAct=EBI-998422, EBI-998440;
CC P49768:PSEN1; NbExp=3; IntAct=EBI-998422, EBI-297277;
CC Q9NZ42:PSENEN; NbExp=3; IntAct=EBI-998422, EBI-998468;
CC P17706-1:PTPN2; NbExp=5; IntAct=EBI-998422, EBI-4409481;
CC Q15363:TMED2; NbExp=7; IntAct=EBI-998422, EBI-998485;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane;
CC Single-pass type I membrane protein. Melanosome. Endoplasmic
CC reticulum membrane; Single-pass type I membrane protein.
CC Endoplasmic reticulum-Golgi intermediate compartment membrane;
CC Single-pass type I membrane protein. Cytoplasmic vesicle,
CC secretory vesicle membrane; Single-pass type I membrane protein
CC (By similarity). Cell membrane (By similarity). Golgi apparatus,
CC trans-Golgi network membrane; Single-pass type I membrane protein
CC (By similarity). Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV. Cycles between
CC compartments of the early secretatory pathway.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The lumenal domain mediates localization to the plasma
CC membrane by partially overriding the ER retention by the
CC cytoplasmic domain (By similarity).
CC -!- MISCELLANEOUS: Ectopic expression of TMED10 alone does not result
CC in its proper cis-Golgi network localization. Coexpression of
CC TMED2 is necessary, and coexpression of TMED3 and /or TMED9 is
CC facilitating localization.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family.
CC -!- SIMILARITY: Contains 1 GOLD domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC42003.1; Type=Frameshift; Positions=Several;
CC Sequence=CAD66561.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; X97442; CAA66071.1; -; mRNA.
DR EMBL; X97444; CAA66073.1; -; mRNA.
DR EMBL; U61734; AAB03625.1; -; Genomic_DNA.
DR EMBL; L40397; AAC42003.1; ALT_FRAME; mRNA.
DR EMBL; AJ004913; CAA06213.1; -; mRNA.
DR EMBL; BX248754; CAD66561.1; ALT_INIT; mRNA.
DR EMBL; AK312384; BAG35302.1; -; mRNA.
DR EMBL; AL832012; CAD89913.1; -; mRNA.
DR EMBL; AC007055; AAD31941.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81223.1; -; Genomic_DNA.
DR EMBL; BC001496; AAH01496.1; -; mRNA.
DR EMBL; BC001825; AAH01825.1; -; mRNA.
DR PIR; G01159; G01159.
DR RefSeq; NP_006818.3; NM_006827.5.
DR UniGene; Hs.74137; -.
DR ProteinModelPortal; P49755; -.
DR IntAct; P49755; 23.
DR MINT; MINT-3017717; -.
DR STRING; 9606.ENSP00000303145; -.
DR PhosphoSite; P49755; -.
DR DMDM; 3915893; -.
DR PaxDb; P49755; -.
DR PeptideAtlas; P49755; -.
DR PRIDE; P49755; -.
DR DNASU; 10972; -.
DR Ensembl; ENST00000303575; ENSP00000303145; ENSG00000170348.
DR GeneID; 10972; -.
DR KEGG; hsa:10972; -.
DR UCSC; uc001xrm.1; human.
DR CTD; 10972; -.
DR GeneCards; GC14M075598; -.
DR HGNC; HGNC:16998; TMED10.
DR HPA; CAB037251; -.
DR MIM; 605406; gene.
DR neXtProt; NX_P49755; -.
DR PharmGKB; PA128394579; -.
DR eggNOG; NOG323830; -.
DR HOVERGEN; HBG107275; -.
DR InParanoid; P49755; -.
DR OMA; VCFESKS; -.
DR OrthoDB; EOG7PZRZM; -.
DR PhylomeDB; P49755; -.
DR ChiTaRS; TMED10; human.
DR GeneWiki; TMED10; -.
DR GenomeRNAi; 10972; -.
DR NextBio; 41690; -.
DR PRO; PR:P49755; -.
DR ArrayExpress; P49755; -.
DR Bgee; P49755; -.
DR CleanEx; HS_TMED10; -.
DR Genevestigator; P49755; -.
DR GO; GO:0005801; C:cis-Golgi network; ISS:HGNC.
DR GO; GO:0030137; C:COPI-coated vesicle; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070765; C:gamma-secretase complex; IDA:UniProtKB.
DR GO; GO:0016021; C:integral to membrane; ISS:HGNC.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISS:UniProtKB.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042589; C:zymogen granule membrane; ISS:HGNC.
DR GO; GO:0034205; P:beta-amyloid formation; IMP:UniProtKB.
DR GO; GO:0035459; P:cargo loading into vesicle; TAS:UniProtKB.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; TAS:UniProtKB.
DR GO; GO:0048208; P:COPII vesicle coating; TAS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IDA:UniProtKB.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0051259; P:protein oligomerization; IEA:Ensembl.
DR GO; GO:0045055; P:regulated secretory pathway; ISS:HGNC.
DR GO; GO:0001101; P:response to acid; IEA:Ensembl.
DR GO; GO:0043279; P:response to alkaloid; IEA:Ensembl.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; ISS:UniProtKB.
DR InterPro; IPR009038; GOLD.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Complete proteome; Cytoplasmic vesicle;
KW Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW Glycoprotein; Golgi apparatus; Membrane; Methylation; Polymorphism;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1 31
FT CHAIN 32 219 Transmembrane emp24 domain-containing
FT protein 10.
FT /FTId=PRO_0000010399.
FT TOPO_DOM 32 185 Lumenal (Potential).
FT TRANSMEM 186 206 Helical; (Potential).
FT TOPO_DOM 207 219 Cytoplasmic (Potential).
FT DOMAIN 41 193 GOLD.
FT REGION 1 142 Required for interaction with STX17.
FT REGION 147 178 Required for TMED10 and TMED2 cis-Golgi
FT network localization.
FT REGION 204 219 Interaction with COPG1.
FT REGION 207 219 Interaction with ARF1.
FT MOTIF 211 219 COPI vesicle coat-binding.
FT MOTIF 211 212 COPII vesicle coat-binding.
FT MOD_RES 171 171 Omega-N-methylated arginine (By
FT similarity).
FT MOD_RES 176 176 Omega-N-methylated arginine (By
FT similarity).
FT CARBOHYD 179 179 N-linked (GlcNAc...) (Potential).
FT VARIANT 64 64 S -> Y (in dbSNP:rs4929).
FT /FTId=VAR_012051.
FT VARIANT 152 152 R -> G (in dbSNP:rs17103066).
FT /FTId=VAR_049111.
FT MUTAGEN 211 212 FF->AA: Disrupts interaction with COPG1
FT and association with coatomer; when
FT associated with 215-A-A-216.
FT MUTAGEN 211 212 FF->AA: No decrease in binding to COPG1.
FT Disrupts interaction with SEC23A.
FT MUTAGEN 215 216 KK->AA: Disrupts interaction with COPG1
FT and association with coatomer; when
FT associated with 211-A-A-212.
FT MUTAGEN 215 216 KK->AA: Significant reduction in binding
FT to COPG1.
FT CONFLICT 75 75 K -> R (in Ref. 7; CAD89913).
SQ SEQUENCE 219 AA; 24976 MW; 0A0486BE65C4DBBB CRC64;
MSGLSGPPAR RGPFPLALLL LFLLGPRLVL AISFHLPINS RKCLREEIHK DLLVTGAYEI
SDQSGGAGGL RSHLKITDSA GHILYSKEDA TKGKFAFTTE DYDMFEVCFE SKGTGRIPDQ
LVILDMKHGV EAKNYEEIAK VEKLKPLEVE LRRLEDLSES IVNDFAYMKK REEEMRDTNE
STNTRVLYFS IFSMFCLIGL ATWQVFYLRR FFKAKKLIE
//
MIM
605406
*RECORD*
*FIELD* NO
605406
*FIELD* TI
*605406 TRANSMEMBRANE EMP24 TRANSPORT DOMAIN-CONTAINING PROTEIN 10; TMED10
;;TRANSMEMBRANE TRAFFICKING PROTEIN, 21-KD; TMP21
read more*FIELD* TX
CLONING
Blum et al. (1996) identified a 21-kD rat pancreatic microsomal membrane
protein that they designated Tmp21. By probing a human brain cDNA
library with a fragment of the rat sequence, they isolated a cDNA
encoding human TMP21. The deduced 219-amino acid type I intracellular
transmembrane protein contains a signal sequence and is predicted to be
located in the lumen of the endoplasmic reticulum. Northern blot
analysis detected a 1.4-kb TMP21 transcript. Immunoblot analysis showed
that the rat Tmp21 protein is expressed predominantly in the microsomal
fraction of pancreatic acinar cells. Horer et al. (1999) determined that
a putative TMP21 isoform, TMP21-II, is a neutral pseudogene.
MAPPING
By linkage analysis, Sherrington et al. (1995) mapped the TMP21 gene to
14q24.3.
GENE FUNCTION
Chen et al. (2006) identified TMP21 as a component of presenilin
complexes and differentially regulates gamma-secretase cleavage without
affecting epsilon-secretase activity (see 104311).
*FIELD* RF
1. Blum, R.; Feick, P.; Puype, M.; Vandekerckhove, J.; Klengel, R.;
Nastainczyk, W.; Schulz, I.: Tmp21 and p24A, two type I proteins
enriched in pancreatic microsomal membranes, are members of a protein
family involved in vesicular trafficking. J. Biol. Chem. 271: 17183-17189,
1996.
2. Chen, F.; Hasegawa, H.; Schmitt-Ulms, G.; Kawarai, T.; Bohm, C.;
Katayama, T.; Gu, Y.; Sanjo, N.; Glista, M.; Rogaeva, E.; Wakutani,
Y.; Pardossi-Piquard, R.; Ruan, X.; Tandon, A.; Checler, F.; Marambaud,
P.; Hansen, K.; Westaway, D.; St George-Hyslop, P.; Fraser, P.: TMP21
is a presenilin complex component that modulates gamma-secretase but
not epsilon-secretase activity. Nature 440: 1208-1212, 2006.
3. Horer, J.; Blum, R.; Feick, P.; Nastainczyk, W.; Schulz, I.: A
comparative study of rat and human Tmp21 (p23) reveals the pseudogene-like
features of human Tmp21-II. DNA Seq. 10: 121-126, 1999.
4. Sherrington, R.; Rogaev, E. I.; Liang, Y.; Rogaeva, E. A.; Levesque,
G.; Ikeda, M.; Chi, H.; Lin, C.; Li, G.; Holman, K.; Tsuda, T.; Mar,
L.; Foncin, J.-F.; Bruni, A. C.; Montesi, M. P.; Sorbi, S.; Rainero,
I.; Pinessi, L.; Nee, L.; Chumakov, I.; Pollen, D.; Brookes, A.; Sanseau,
P.; Polinsky, R. J.; Wasco, W.; Da Silva, H. A. R.; Haines, J. L.;
Pericak-Vance, M. A.; Tanzi, R. E.; Roses, A. D.; Fraser, P. E.; Rommens,
J. M.; St George-Hyslop, P. H.: Cloning of a gene bearing missense
mutations in early-onset familial Alzheimer's disease. Nature 375:
754-760, 1995.
*FIELD* CN
Ada Hamosh - updated: 5/15/2006
*FIELD* CD
Paul J. Converse: 11/16/2000
*FIELD* ED
alopez: 05/23/2006
alopez: 5/23/2006
terry: 5/15/2006
mgross: 11/16/2000
*RECORD*
*FIELD* NO
605406
*FIELD* TI
*605406 TRANSMEMBRANE EMP24 TRANSPORT DOMAIN-CONTAINING PROTEIN 10; TMED10
;;TRANSMEMBRANE TRAFFICKING PROTEIN, 21-KD; TMP21
read more*FIELD* TX
CLONING
Blum et al. (1996) identified a 21-kD rat pancreatic microsomal membrane
protein that they designated Tmp21. By probing a human brain cDNA
library with a fragment of the rat sequence, they isolated a cDNA
encoding human TMP21. The deduced 219-amino acid type I intracellular
transmembrane protein contains a signal sequence and is predicted to be
located in the lumen of the endoplasmic reticulum. Northern blot
analysis detected a 1.4-kb TMP21 transcript. Immunoblot analysis showed
that the rat Tmp21 protein is expressed predominantly in the microsomal
fraction of pancreatic acinar cells. Horer et al. (1999) determined that
a putative TMP21 isoform, TMP21-II, is a neutral pseudogene.
MAPPING
By linkage analysis, Sherrington et al. (1995) mapped the TMP21 gene to
14q24.3.
GENE FUNCTION
Chen et al. (2006) identified TMP21 as a component of presenilin
complexes and differentially regulates gamma-secretase cleavage without
affecting epsilon-secretase activity (see 104311).
*FIELD* RF
1. Blum, R.; Feick, P.; Puype, M.; Vandekerckhove, J.; Klengel, R.;
Nastainczyk, W.; Schulz, I.: Tmp21 and p24A, two type I proteins
enriched in pancreatic microsomal membranes, are members of a protein
family involved in vesicular trafficking. J. Biol. Chem. 271: 17183-17189,
1996.
2. Chen, F.; Hasegawa, H.; Schmitt-Ulms, G.; Kawarai, T.; Bohm, C.;
Katayama, T.; Gu, Y.; Sanjo, N.; Glista, M.; Rogaeva, E.; Wakutani,
Y.; Pardossi-Piquard, R.; Ruan, X.; Tandon, A.; Checler, F.; Marambaud,
P.; Hansen, K.; Westaway, D.; St George-Hyslop, P.; Fraser, P.: TMP21
is a presenilin complex component that modulates gamma-secretase but
not epsilon-secretase activity. Nature 440: 1208-1212, 2006.
3. Horer, J.; Blum, R.; Feick, P.; Nastainczyk, W.; Schulz, I.: A
comparative study of rat and human Tmp21 (p23) reveals the pseudogene-like
features of human Tmp21-II. DNA Seq. 10: 121-126, 1999.
4. Sherrington, R.; Rogaev, E. I.; Liang, Y.; Rogaeva, E. A.; Levesque,
G.; Ikeda, M.; Chi, H.; Lin, C.; Li, G.; Holman, K.; Tsuda, T.; Mar,
L.; Foncin, J.-F.; Bruni, A. C.; Montesi, M. P.; Sorbi, S.; Rainero,
I.; Pinessi, L.; Nee, L.; Chumakov, I.; Pollen, D.; Brookes, A.; Sanseau,
P.; Polinsky, R. J.; Wasco, W.; Da Silva, H. A. R.; Haines, J. L.;
Pericak-Vance, M. A.; Tanzi, R. E.; Roses, A. D.; Fraser, P. E.; Rommens,
J. M.; St George-Hyslop, P. H.: Cloning of a gene bearing missense
mutations in early-onset familial Alzheimer's disease. Nature 375:
754-760, 1995.
*FIELD* CN
Ada Hamosh - updated: 5/15/2006
*FIELD* CD
Paul J. Converse: 11/16/2000
*FIELD* ED
alopez: 05/23/2006
alopez: 5/23/2006
terry: 5/15/2006
mgross: 11/16/2000