Full text data of TMED7
TMED7
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Transmembrane emp24 domain-containing protein 7 (p24 family protein gamma-3; p24gamma3; p27; Flags: Precursor)
Transmembrane emp24 domain-containing protein 7 (p24 family protein gamma-3; p24gamma3; p27; Flags: Precursor)
hRBCD
IPI00032825
IPI00032825 Hypothetical protein CGI-109 precursor Hypothetical protein CGI-109 precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 integral membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00032825 Hypothetical protein CGI-109 precursor Hypothetical protein CGI-109 precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 integral membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
Q9Y3B3
ID TMED7_HUMAN Reviewed; 224 AA.
AC Q9Y3B3; Q8NBU8; Q8WUU6; Q96K51;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 29-MAR-2005, sequence version 2.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Transmembrane emp24 domain-containing protein 7;
DE AltName: Full=p24 family protein gamma-3;
DE Short=p24gamma3;
DE AltName: Full=p27;
DE Flags: Precursor;
GN Name=TMED7; ORFNames=CGI-109;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [6]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND 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 [7]
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 [8]
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).
CC -!- FUNCTION: Potential role in vesicular protein trafficking, mainly
CC in the early secretory pathway. Appears to play a role in the
CC biosynthesis of secreted cargo including processing and post-
CC translational modifications.
CC -!- SUBUNIT: Predominantly monomeric and to lesser extent homodimeric
CC in endoplasmic reticulum, endoplasmic reticulum-Golgi intermediate
CC compartment and cis-Golgi network. Oligomerizes with other members
CC of the EMP24/GP25L family such as TMED2, TMED9 and TMED10.
CC Interacts (via C-terminus) with COPG1; the interaction involves
CC dimeric TMED7.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein. Golgi apparatus, cis-Golgi network
CC membrane; Single-pass type I membrane protein. Endoplasmic
CC reticulum-Golgi intermediate compartment membrane; Single-pass
CC type I membrane protein. Cytoplasmic vesicle, COPI-coated vesicle
CC membrane; Single-pass type I membrane protein (By similarity).
CC Cytoplasmic vesicle, COPII-coated vesicle membrane; Single-pass
CC type I membrane protein (By similarity). Note=Cycles between
CC compartments of the early secretatory pathway.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y3B3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3B3-2; Sequence=VSP_046247;
CC Note=No experimental confirmation available;
CC -!- PTM: N-linked glycosylated in complex form containing terminal
CC sialic acid.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family.
CC -!- SIMILARITY: Contains 1 GOLD domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF151867; AAD34104.1; -; mRNA.
DR EMBL; AK027512; BAB55166.1; -; mRNA.
DR EMBL; AK074962; BAC11318.1; -; mRNA.
DR EMBL; AK075218; BAC11479.1; -; mRNA.
DR EMBL; AC010226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019349; AAH19349.1; -; mRNA.
DR RefSeq; NP_001157941.1; NM_001164469.2.
DR RefSeq; NP_861974.1; NM_181836.5.
DR UniGene; Hs.642817; -.
DR UniGene; Hs.718838; -.
DR ProteinModelPortal; Q9Y3B3; -.
DR IntAct; Q9Y3B3; 8.
DR STRING; 9606.ENSP00000405926; -.
DR PhosphoSite; Q9Y3B3; -.
DR DMDM; 62299080; -.
DR PaxDb; Q9Y3B3; -.
DR PRIDE; Q9Y3B3; -.
DR DNASU; 51014; -.
DR Ensembl; ENST00000456936; ENSP00000405926; ENSG00000134970.
DR GeneID; 100302736; -.
DR GeneID; 51014; -.
DR KEGG; hsa:100302736; -.
DR KEGG; hsa:51014; -.
DR UCSC; uc003krd.3; human.
DR CTD; 100302736; -.
DR CTD; 51014; -.
DR GeneCards; GC05M114978; -.
DR HGNC; HGNC:24253; TMED7.
DR HPA; CAB025883; -.
DR HPA; HPA008960; -.
DR neXtProt; NX_Q9Y3B3; -.
DR PharmGKB; PA134891536; -.
DR PharmGKB; PA165660570; -.
DR eggNOG; NOG314667; -.
DR HOGENOM; HOG000160229; -.
DR HOVERGEN; HBG000271; -.
DR KO; K14825; -.
DR OMA; GVYTACF; -.
DR OrthoDB; EOG70ZZP7; -.
DR GenomeRNAi; 51014; -.
DR NextBio; 20796124; -.
DR PRO; PR:Q9Y3B3; -.
DR ArrayExpress; Q9Y3B3; -.
DR Bgee; Q9Y3B3; -.
DR CleanEx; HS_TMED7; -.
DR Genevestigator; Q9Y3B3; -.
DR GO; GO:0030126; C:COPI vesicle coat; TAS:UniProtKB.
DR GO; GO:0030127; C:COPII vesicle coat; TAS: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:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR009038; GOLD.
DR InterPro; IPR015718; P24-related.
DR PANTHER; PTHR22811:SF13; PTHR22811:SF13; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR SUPFAM; SSF101576; SSF101576; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1 34 Potential.
FT CHAIN 35 224 Transmembrane emp24 domain-containing
FT protein 7.
FT /FTId=PRO_0000010395.
FT TOPO_DOM 35 187 Lumenal (Potential).
FT TRANSMEM 188 208 Helical; (Potential).
FT TOPO_DOM 209 224 Cytoplasmic (Potential).
FT DOMAIN 46 128 GOLD.
FT MOTIF 211 224 COPI vesicle coat-binding (Potential).
FT MOTIF 211 212 COPII vesicle coat-binding (Potential).
FT CARBOHYD 103 103 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 189 224 Missing (in isoform 2).
FT /FTId=VSP_046247.
FT CONFLICT 1 23 MPRPGSAQRWAAVAGRWGCRLLA -> MGSTVPRSASVLLL
FT L (in Ref. 1; AAD34104).
FT CONFLICT 27 37 LVPGPGGASEI -> RRAEQPCGAEL (in Ref. 1;
FT AAD34104).
FT CONFLICT 59 59 C -> S (in Ref. 1; AAD34104).
FT CONFLICT 131 139 DPPLFPSEN -> THLCFLVD (in Ref. 1;
FT AAD34104).
FT CONFLICT 213 213 S -> P (in Ref. 2; BAB55166).
SQ SEQUENCE 224 AA; 25172 MW; 9D0D2110579837B3 CRC64;
MPRPGSAQRW AAVAGRWGCR LLALLLLVPG PGGASEITFE LPDNAKQCFY EDIAQGTKCT
LEFQVITGGH YDVDCRLEDP DGKVLYKEMK KQYDSFTFTA SKNGTYKFCF SNEFSTFTHK
TVYFDFQVGE DPPLFPSENR VSALTQMESA CVSIHEALKS VIDYQTHFRL REAQGRSRAE
DLNTRVAYWS VGEALILLVV SIGQVFLLKS FFSDKRTTTT RVGS
//
ID TMED7_HUMAN Reviewed; 224 AA.
AC Q9Y3B3; Q8NBU8; Q8WUU6; Q96K51;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 29-MAR-2005, sequence version 2.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Transmembrane emp24 domain-containing protein 7;
DE AltName: Full=p24 family protein gamma-3;
DE Short=p24gamma3;
DE AltName: Full=p27;
DE Flags: Precursor;
GN Name=TMED7; ORFNames=CGI-109;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [6]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND 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 [7]
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 [8]
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).
CC -!- FUNCTION: Potential role in vesicular protein trafficking, mainly
CC in the early secretory pathway. Appears to play a role in the
CC biosynthesis of secreted cargo including processing and post-
CC translational modifications.
CC -!- SUBUNIT: Predominantly monomeric and to lesser extent homodimeric
CC in endoplasmic reticulum, endoplasmic reticulum-Golgi intermediate
CC compartment and cis-Golgi network. Oligomerizes with other members
CC of the EMP24/GP25L family such as TMED2, TMED9 and TMED10.
CC Interacts (via C-terminus) with COPG1; the interaction involves
CC dimeric TMED7.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein. Golgi apparatus, cis-Golgi network
CC membrane; Single-pass type I membrane protein. Endoplasmic
CC reticulum-Golgi intermediate compartment membrane; Single-pass
CC type I membrane protein. Cytoplasmic vesicle, COPI-coated vesicle
CC membrane; Single-pass type I membrane protein (By similarity).
CC Cytoplasmic vesicle, COPII-coated vesicle membrane; Single-pass
CC type I membrane protein (By similarity). Note=Cycles between
CC compartments of the early secretatory pathway.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y3B3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3B3-2; Sequence=VSP_046247;
CC Note=No experimental confirmation available;
CC -!- PTM: N-linked glycosylated in complex form containing terminal
CC sialic acid.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family.
CC -!- SIMILARITY: Contains 1 GOLD domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF151867; AAD34104.1; -; mRNA.
DR EMBL; AK027512; BAB55166.1; -; mRNA.
DR EMBL; AK074962; BAC11318.1; -; mRNA.
DR EMBL; AK075218; BAC11479.1; -; mRNA.
DR EMBL; AC010226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019349; AAH19349.1; -; mRNA.
DR RefSeq; NP_001157941.1; NM_001164469.2.
DR RefSeq; NP_861974.1; NM_181836.5.
DR UniGene; Hs.642817; -.
DR UniGene; Hs.718838; -.
DR ProteinModelPortal; Q9Y3B3; -.
DR IntAct; Q9Y3B3; 8.
DR STRING; 9606.ENSP00000405926; -.
DR PhosphoSite; Q9Y3B3; -.
DR DMDM; 62299080; -.
DR PaxDb; Q9Y3B3; -.
DR PRIDE; Q9Y3B3; -.
DR DNASU; 51014; -.
DR Ensembl; ENST00000456936; ENSP00000405926; ENSG00000134970.
DR GeneID; 100302736; -.
DR GeneID; 51014; -.
DR KEGG; hsa:100302736; -.
DR KEGG; hsa:51014; -.
DR UCSC; uc003krd.3; human.
DR CTD; 100302736; -.
DR CTD; 51014; -.
DR GeneCards; GC05M114978; -.
DR HGNC; HGNC:24253; TMED7.
DR HPA; CAB025883; -.
DR HPA; HPA008960; -.
DR neXtProt; NX_Q9Y3B3; -.
DR PharmGKB; PA134891536; -.
DR PharmGKB; PA165660570; -.
DR eggNOG; NOG314667; -.
DR HOGENOM; HOG000160229; -.
DR HOVERGEN; HBG000271; -.
DR KO; K14825; -.
DR OMA; GVYTACF; -.
DR OrthoDB; EOG70ZZP7; -.
DR GenomeRNAi; 51014; -.
DR NextBio; 20796124; -.
DR PRO; PR:Q9Y3B3; -.
DR ArrayExpress; Q9Y3B3; -.
DR Bgee; Q9Y3B3; -.
DR CleanEx; HS_TMED7; -.
DR Genevestigator; Q9Y3B3; -.
DR GO; GO:0030126; C:COPI vesicle coat; TAS:UniProtKB.
DR GO; GO:0030127; C:COPII vesicle coat; TAS: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:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR009038; GOLD.
DR InterPro; IPR015718; P24-related.
DR PANTHER; PTHR22811:SF13; PTHR22811:SF13; 1.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR SUPFAM; SSF101576; SSF101576; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1 34 Potential.
FT CHAIN 35 224 Transmembrane emp24 domain-containing
FT protein 7.
FT /FTId=PRO_0000010395.
FT TOPO_DOM 35 187 Lumenal (Potential).
FT TRANSMEM 188 208 Helical; (Potential).
FT TOPO_DOM 209 224 Cytoplasmic (Potential).
FT DOMAIN 46 128 GOLD.
FT MOTIF 211 224 COPI vesicle coat-binding (Potential).
FT MOTIF 211 212 COPII vesicle coat-binding (Potential).
FT CARBOHYD 103 103 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 189 224 Missing (in isoform 2).
FT /FTId=VSP_046247.
FT CONFLICT 1 23 MPRPGSAQRWAAVAGRWGCRLLA -> MGSTVPRSASVLLL
FT L (in Ref. 1; AAD34104).
FT CONFLICT 27 37 LVPGPGGASEI -> RRAEQPCGAEL (in Ref. 1;
FT AAD34104).
FT CONFLICT 59 59 C -> S (in Ref. 1; AAD34104).
FT CONFLICT 131 139 DPPLFPSEN -> THLCFLVD (in Ref. 1;
FT AAD34104).
FT CONFLICT 213 213 S -> P (in Ref. 2; BAB55166).
SQ SEQUENCE 224 AA; 25172 MW; 9D0D2110579837B3 CRC64;
MPRPGSAQRW AAVAGRWGCR LLALLLLVPG PGGASEITFE LPDNAKQCFY EDIAQGTKCT
LEFQVITGGH YDVDCRLEDP DGKVLYKEMK KQYDSFTFTA SKNGTYKFCF SNEFSTFTHK
TVYFDFQVGE DPPLFPSENR VSALTQMESA CVSIHEALKS VIDYQTHFRL REAQGRSRAE
DLNTRVAYWS VGEALILLVV SIGQVFLLKS FFSDKRTTTT RVGS
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