Full text data of TMED9
TMED9
(GP25L2)
[Confidence: high (present in two of the MS resources)]
Transmembrane emp24 domain-containing protein 9 (GMP25; Glycoprotein 25L2; p24 family protein alpha-2; p24alpha2; p25; Flags: Precursor)
Transmembrane emp24 domain-containing protein 9 (GMP25; Glycoprotein 25L2; p24 family protein alpha-2; p24alpha2; p25; Flags: Precursor)
hRBCD
IPI00023542
IPI00023542 gp25L2 protein gp25L2 protein membrane n/a n/a n/a n/a n/a n/a 1 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 integral to membrane n/a found at its expected molecular weight found at molecular weight
IPI00023542 gp25L2 protein gp25L2 protein membrane n/a n/a n/a n/a n/a n/a 1 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 integral to membrane n/a found at its expected molecular weight found at molecular weight
UniProt
Q9BVK6
ID TMED9_HUMAN Reviewed; 235 AA.
AC Q9BVK6; Q14437; Q8WZ61;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-JUN-2009, sequence version 2.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Transmembrane emp24 domain-containing protein 9;
DE AltName: Full=GMP25;
DE AltName: Full=Glycoprotein 25L2;
DE AltName: Full=p24 family protein alpha-2;
DE Short=p24alpha2;
DE AltName: Full=p25;
DE Flags: Precursor;
GN Name=TMED9; Synonyms=GP25L2;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-235.
RC TISSUE=Liver;
RA Dominguez M., Fazel A., Parlati F., Bell A.W., Thomas D.Y.,
RA Bergeron J.J.M.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-235.
RA Wang C., Li Y.;
RT "A novel human cDNA that shares sequence homology with Homo sapiens
RT mRNAs LOC96645 and gp25L2.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 129-138 AND 170-180, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [6]
RP 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 FUNCTION, AND 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 [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 232-LYS-LYS-233.
RX PubMed=14600267; DOI=10.1242/jcs.00802;
RA Emery G., Parton R.G., Rojo M., Gruenberg J.;
RT "The trans-membrane protein p25 forms highly specialized domains that
RT regulate membrane composition and dynamics.";
RL J. Cell Sci. 116:4821-4832(2003).
RN [10]
RP GLYCOSYLATION AT ASN-125.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [11]
RP INTERACTION WITH SPAST.
RX PubMed=15537668; DOI=10.1093/hmg/ddi003;
RA Reid E., Connell J.W., Edwards T.L., Duley S., Brown S.E.,
RA Sanderson C.M.;
RT "The hereditary spastic paraplegia protein spastin interacts with the
RT ESCRT-III complex-associated endosomal protein CHMP1B.";
RL Hum. Mol. Genet. 14:19-38(2005).
RN [12]
RP FUNCTION, AND INTERACTION WITH PTPN2.
RX PubMed=16595549; DOI=10.1242/jcs.02885;
RA Gupta V., Swarup G.;
RT "Evidence for a role of transmembrane protein p25 in localization of
RT protein tyrosine phosphatase TC48 to the ER.";
RL J. Cell Sci. 119:1703-1714(2006).
RN [13]
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 [14]
RP FUNCTION.
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 [15]
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 [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [17]
RP INTERACTION WITH TMED5.
RX PubMed=19948005; DOI=10.1111/j.1600-0854.2009.01009.x;
RA Koegler E., Bonnon C., Waldmeier L., Mitrovic S., Halbeisen R.,
RA Hauri H.P.;
RT "p28, a novel ERGIC/cis Golgi protein, required for Golgi ribbon
RT formation.";
RL Traffic 11:70-89(2010).
RN [18]
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 [19]
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).
CC -!- FUNCTION: Appears to be involved in vesicular protein trafficking,
CC mainly in the early secretory pathway. In COPI vesicle-mediated
CC retrograde transport involved in the coatomer recruitment to
CC membranes of the early secretory pathway. Increases coatomer-
CC dependent activity of ARFGAP2. Thought to play a crucial role in
CC the specific retention of p24 complexes in cis-Golgi membranes;
CC specifically contributes to the coupled localization of TMED2 and
CC TMED10 in the cis-Golgi network. May be involved in organization
CC of intracellular membranes, such as of the ER-Golgi intermediate
CC compartment and the Golgi apparatus. Involved in ER localization
CC of PTPN2 isoform PTPB.
CC -!- SUBUNIT: Monomer and homodimer in endoplasmic reticulum.
CC Predominantly monomeric and to lesser extent homodimeric in
CC endoplasmic reticulum-Golgi intermediate compartment and cis-Golgi
CC network. Probably oligomerizes with other members of the
CC EMP24/GP25L family such as TMED2, TMED7 and TMED10. Interacts with
CC TMED5. Interacts (via C-terminus) with COPG1; the interaction
CC involves dimeric TMED9. Interacts with PTPN2 and SPAST. Interacts
CC with STX17; the interaction is direct.
CC -!- INTERACTION:
CC P17706-1:PTPN2; NbExp=5; IntAct=EBI-1056827, EBI-4409481;
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. Golgi apparatus, trans-Golgi network
CC membrane; Single-pass type I membrane protein (By similarity).
CC Note=Cycles between compartments of the early secretatory pathway.
CC -!- PTM: N-linked glycosylated containing high mannose.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family.
CC -!- SIMILARITY: Contains 1 GOLD domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL35268.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAA62380.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AC139795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001123; AAH01123.2; -; mRNA.
DR EMBL; X90872; CAA62380.1; ALT_INIT; mRNA.
DR EMBL; AF441399; AAL35268.1; ALT_INIT; mRNA.
DR RefSeq; NP_059980.2; NM_017510.4.
DR UniGene; Hs.279929; -.
DR ProteinModelPortal; Q9BVK6; -.
DR IntAct; Q9BVK6; 20.
DR MINT; MINT-5001958; -.
DR STRING; 9606.ENSP00000330945; -.
DR PhosphoSite; Q9BVK6; -.
DR DMDM; 239938724; -.
DR PaxDb; Q9BVK6; -.
DR PRIDE; Q9BVK6; -.
DR Ensembl; ENST00000332598; ENSP00000330945; ENSG00000184840.
DR GeneID; 54732; -.
DR KEGG; hsa:54732; -.
DR UCSC; uc003mhx.3; human.
DR CTD; 54732; -.
DR GeneCards; GC05P177019; -.
DR H-InvDB; HIX0005470; -.
DR HGNC; HGNC:24878; TMED9.
DR HPA; HPA014650; -.
DR neXtProt; NX_Q9BVK6; -.
DR PharmGKB; PA134881976; -.
DR eggNOG; NOG323830; -.
DR HOGENOM; HOG000160228; -.
DR HOVERGEN; HBG105357; -.
DR InParanoid; Q9BVK6; -.
DR OMA; VLWWSIV; -.
DR OrthoDB; EOG74BJT2; -.
DR PhylomeDB; Q9BVK6; -.
DR ChiTaRS; TMED9; human.
DR GenomeRNAi; 54732; -.
DR NextBio; 57312; -.
DR PRO; PR:Q9BVK6; -.
DR Bgee; Q9BVK6; -.
DR CleanEx; HS_TMED9; -.
DR Genevestigator; Q9BVK6; -.
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:0030140; C:trans-Golgi network transport vesicle; TAS:UniProtKB.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0010638; P:positive regulation of organelle organization; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR009038; GOLD.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW Polymorphism; Protein transport; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1 37 By similarity.
FT CHAIN 38 235 Transmembrane emp24 domain-containing
FT protein 9.
FT /FTId=PRO_0000010396.
FT TOPO_DOM 38 202 Lumenal (Potential).
FT TRANSMEM 203 222 Helical; (Potential).
FT TOPO_DOM 223 235 Cytoplasmic (Potential).
FT DOMAIN 47 145 GOLD.
FT REGION 121 160 Required for interaction with STX17.
FT COILED 154 184 Potential.
FT MOTIF 228 235 COPI vesicle coat-binding (Potential).
FT MOTIF 228 229 COPII vesicle coat-binding (Potential).
FT CARBOHYD 125 125 N-linked (GlcNAc...).
FT VARIANT 16 16 T -> S (in dbSNP:rs57960711).
FT /FTId=VAR_061178.
FT MUTAGEN 232 233 KK->SS: Localization to plasma membrane
FT and endocytosis.
FT CONFLICT 83 83 L -> F (in Ref. 2; CAA62380).
FT CONFLICT 86 86 F -> C (in Ref. 2; CAA62380).
FT CONFLICT 101 101 Q -> E (in Ref. 2; CAA62380).
FT CONFLICT 102 102 Y -> C (in Ref. 3; AAL35268).
FT CONFLICT 156 156 A -> P (in Ref. 2; CAA62380).
SQ SEQUENCE 235 AA; 27277 MW; 9B6D2D517D9E77D8 CRC64;
MAVELGVLLV RPRPGTGLGR VMRTLLLVLW LATRGSALYF HIGETEKKCF IEEIPDETMV
IGNYRTQLYD KQREEYQPAT PGLGMFVEVK DPEDKVILAR QYGSEGRFTF TSHTPGEHQI
CLHSNSTKFS LFAGGMLRVH LDIQVGEHAN DYAEIAAKDK LSELQLRVRQ LVEQVEQIQK
EQNYQRWREE RFRQTSESTN QRVLWWSILQ TLILVAIGVW QMRHLKSFFE AKKLV
//
ID TMED9_HUMAN Reviewed; 235 AA.
AC Q9BVK6; Q14437; Q8WZ61;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-JUN-2009, sequence version 2.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Transmembrane emp24 domain-containing protein 9;
DE AltName: Full=GMP25;
DE AltName: Full=Glycoprotein 25L2;
DE AltName: Full=p24 family protein alpha-2;
DE Short=p24alpha2;
DE AltName: Full=p25;
DE Flags: Precursor;
GN Name=TMED9; Synonyms=GP25L2;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-235.
RC TISSUE=Liver;
RA Dominguez M., Fazel A., Parlati F., Bell A.W., Thomas D.Y.,
RA Bergeron J.J.M.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 16-235.
RA Wang C., Li Y.;
RT "A novel human cDNA that shares sequence homology with Homo sapiens
RT mRNAs LOC96645 and gp25L2.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 129-138 AND 170-180, AND MASS SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [6]
RP 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 FUNCTION, AND 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 [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 232-LYS-LYS-233.
RX PubMed=14600267; DOI=10.1242/jcs.00802;
RA Emery G., Parton R.G., Rojo M., Gruenberg J.;
RT "The trans-membrane protein p25 forms highly specialized domains that
RT regulate membrane composition and dynamics.";
RL J. Cell Sci. 116:4821-4832(2003).
RN [10]
RP GLYCOSYLATION AT ASN-125.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [11]
RP INTERACTION WITH SPAST.
RX PubMed=15537668; DOI=10.1093/hmg/ddi003;
RA Reid E., Connell J.W., Edwards T.L., Duley S., Brown S.E.,
RA Sanderson C.M.;
RT "The hereditary spastic paraplegia protein spastin interacts with the
RT ESCRT-III complex-associated endosomal protein CHMP1B.";
RL Hum. Mol. Genet. 14:19-38(2005).
RN [12]
RP FUNCTION, AND INTERACTION WITH PTPN2.
RX PubMed=16595549; DOI=10.1242/jcs.02885;
RA Gupta V., Swarup G.;
RT "Evidence for a role of transmembrane protein p25 in localization of
RT protein tyrosine phosphatase TC48 to the ER.";
RL J. Cell Sci. 119:1703-1714(2006).
RN [13]
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 [14]
RP FUNCTION.
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 [15]
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 [16]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-125, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [17]
RP INTERACTION WITH TMED5.
RX PubMed=19948005; DOI=10.1111/j.1600-0854.2009.01009.x;
RA Koegler E., Bonnon C., Waldmeier L., Mitrovic S., Halbeisen R.,
RA Hauri H.P.;
RT "p28, a novel ERGIC/cis Golgi protein, required for Golgi ribbon
RT formation.";
RL Traffic 11:70-89(2010).
RN [18]
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 [19]
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).
CC -!- FUNCTION: Appears to be involved in vesicular protein trafficking,
CC mainly in the early secretory pathway. In COPI vesicle-mediated
CC retrograde transport involved in the coatomer recruitment to
CC membranes of the early secretory pathway. Increases coatomer-
CC dependent activity of ARFGAP2. Thought to play a crucial role in
CC the specific retention of p24 complexes in cis-Golgi membranes;
CC specifically contributes to the coupled localization of TMED2 and
CC TMED10 in the cis-Golgi network. May be involved in organization
CC of intracellular membranes, such as of the ER-Golgi intermediate
CC compartment and the Golgi apparatus. Involved in ER localization
CC of PTPN2 isoform PTPB.
CC -!- SUBUNIT: Monomer and homodimer in endoplasmic reticulum.
CC Predominantly monomeric and to lesser extent homodimeric in
CC endoplasmic reticulum-Golgi intermediate compartment and cis-Golgi
CC network. Probably oligomerizes with other members of the
CC EMP24/GP25L family such as TMED2, TMED7 and TMED10. Interacts with
CC TMED5. Interacts (via C-terminus) with COPG1; the interaction
CC involves dimeric TMED9. Interacts with PTPN2 and SPAST. Interacts
CC with STX17; the interaction is direct.
CC -!- INTERACTION:
CC P17706-1:PTPN2; NbExp=5; IntAct=EBI-1056827, EBI-4409481;
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. Golgi apparatus, trans-Golgi network
CC membrane; Single-pass type I membrane protein (By similarity).
CC Note=Cycles between compartments of the early secretatory pathway.
CC -!- PTM: N-linked glycosylated containing high mannose.
CC -!- SIMILARITY: Belongs to the EMP24/GP25L family.
CC -!- SIMILARITY: Contains 1 GOLD domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL35268.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=CAA62380.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR EMBL; AC139795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001123; AAH01123.2; -; mRNA.
DR EMBL; X90872; CAA62380.1; ALT_INIT; mRNA.
DR EMBL; AF441399; AAL35268.1; ALT_INIT; mRNA.
DR RefSeq; NP_059980.2; NM_017510.4.
DR UniGene; Hs.279929; -.
DR ProteinModelPortal; Q9BVK6; -.
DR IntAct; Q9BVK6; 20.
DR MINT; MINT-5001958; -.
DR STRING; 9606.ENSP00000330945; -.
DR PhosphoSite; Q9BVK6; -.
DR DMDM; 239938724; -.
DR PaxDb; Q9BVK6; -.
DR PRIDE; Q9BVK6; -.
DR Ensembl; ENST00000332598; ENSP00000330945; ENSG00000184840.
DR GeneID; 54732; -.
DR KEGG; hsa:54732; -.
DR UCSC; uc003mhx.3; human.
DR CTD; 54732; -.
DR GeneCards; GC05P177019; -.
DR H-InvDB; HIX0005470; -.
DR HGNC; HGNC:24878; TMED9.
DR HPA; HPA014650; -.
DR neXtProt; NX_Q9BVK6; -.
DR PharmGKB; PA134881976; -.
DR eggNOG; NOG323830; -.
DR HOGENOM; HOG000160228; -.
DR HOVERGEN; HBG105357; -.
DR InParanoid; Q9BVK6; -.
DR OMA; VLWWSIV; -.
DR OrthoDB; EOG74BJT2; -.
DR PhylomeDB; Q9BVK6; -.
DR ChiTaRS; TMED9; human.
DR GenomeRNAi; 54732; -.
DR NextBio; 57312; -.
DR PRO; PR:Q9BVK6; -.
DR Bgee; Q9BVK6; -.
DR CleanEx; HS_TMED9; -.
DR Genevestigator; Q9BVK6; -.
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:0030140; C:trans-Golgi network transport vesicle; TAS:UniProtKB.
DR GO; GO:0048205; P:COPI coating of Golgi vesicle; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0010638; P:positive regulation of organelle organization; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR009038; GOLD.
DR Pfam; PF01105; EMP24_GP25L; 1.
DR PROSITE; PS50866; GOLD; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Complete proteome; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW Polymorphism; Protein transport; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1 37 By similarity.
FT CHAIN 38 235 Transmembrane emp24 domain-containing
FT protein 9.
FT /FTId=PRO_0000010396.
FT TOPO_DOM 38 202 Lumenal (Potential).
FT TRANSMEM 203 222 Helical; (Potential).
FT TOPO_DOM 223 235 Cytoplasmic (Potential).
FT DOMAIN 47 145 GOLD.
FT REGION 121 160 Required for interaction with STX17.
FT COILED 154 184 Potential.
FT MOTIF 228 235 COPI vesicle coat-binding (Potential).
FT MOTIF 228 229 COPII vesicle coat-binding (Potential).
FT CARBOHYD 125 125 N-linked (GlcNAc...).
FT VARIANT 16 16 T -> S (in dbSNP:rs57960711).
FT /FTId=VAR_061178.
FT MUTAGEN 232 233 KK->SS: Localization to plasma membrane
FT and endocytosis.
FT CONFLICT 83 83 L -> F (in Ref. 2; CAA62380).
FT CONFLICT 86 86 F -> C (in Ref. 2; CAA62380).
FT CONFLICT 101 101 Q -> E (in Ref. 2; CAA62380).
FT CONFLICT 102 102 Y -> C (in Ref. 3; AAL35268).
FT CONFLICT 156 156 A -> P (in Ref. 2; CAA62380).
SQ SEQUENCE 235 AA; 27277 MW; 9B6D2D517D9E77D8 CRC64;
MAVELGVLLV RPRPGTGLGR VMRTLLLVLW LATRGSALYF HIGETEKKCF IEEIPDETMV
IGNYRTQLYD KQREEYQPAT PGLGMFVEVK DPEDKVILAR QYGSEGRFTF TSHTPGEHQI
CLHSNSTKFS LFAGGMLRVH LDIQVGEHAN DYAEIAAKDK LSELQLRVRQ LVEQVEQIQK
EQNYQRWREE RFRQTSESTN QRVLWWSILQ TLILVAIGVW QMRHLKSFFE AKKLV
//