GOSR1_HUMAN
ID GOSR1_HUMAN Reviewed; 250 AA.
AC O95249; J3KST5; O75392;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Golgi SNAP receptor complex member 1;
DE AltName: Full=28 kDa Golgi SNARE protein;
DE AltName: Full=28 kDa cis-Golgi SNARE p28;
DE Short=GOS-28;
GN Name=GOSR1; Synonyms=GS28;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Colon carcinoma;
RX PubMed=10198168; DOI=10.1006/geno.1998.5649;
RA Bui T.D., Levy E.R., Subramaniam V.N., Lowe S.L., Hong W.;
RT "cDNA characterization and chromosomal mapping of human Golgi SNARE GS27
RT and GS28 to chromosome 17.";
RL Genomics 57:285-288(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15215310; DOI=10.1091/mbc.e03-12-0876;
RA Tai G., Lu L., Wang T.L., Tang B.L., Goud B., Johannes L., Hong W.;
RT "Participation of the syntaxin 5/Ykt6/GS28/GS15 SNARE complex in transport
RT from the early/recycling endosome to the trans-Golgi network.";
RL Mol. Biol. Cell 15:4011-4022(2004).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15728195; DOI=10.1083/jcb.200412003;
RA Zolov S.N., Lupashin V.V.;
RT "Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in
RT HeLa cells.";
RL J. Cell Biol. 168:747-759(2005).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=17274796; DOI=10.1111/j.1600-0854.2006.00533.x;
RA Martinez-Alonso E., Ballesta J., Martinez-Menarguez J.A.;
RT "Low-temperature-induced Golgi tubules are transient membranes enriched in
RT molecules regulating intra-Golgi transport.";
RL Traffic 8:359-368(2007).
RN [9]
RP SUBCELLULAR LOCATION, AND INDUCTION BY MONOCROTALINE.
RX PubMed=17337506; DOI=10.1152/ajplung.00463.2006;
RA Sehgal P.B., Mukhopadhyay S., Xu F., Patel K., Shah M.;
RT "Dysfunction of Golgi tethers, SNAREs, and SNAPs in monocrotaline-induced
RT pulmonary hypertension.";
RL Am. J. Physiol. 292:L1526-L1542(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
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., Buerckstuemmer T.,
RA 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 [12]
RP SUBCELLULAR LOCATION, AND INDUCTION BY OSBPL7.
RX PubMed=21669198; DOI=10.1016/j.yexcr.2011.05.028;
RA Zhong W., Zhou Y., Li S., Zhou T., Ma H., Wei K., Li H., Olkkonen V.M.,
RA Yan D.;
RT "OSBP-related protein 7 interacts with GATE-16 and negatively regulates
RT GS28 protein stability.";
RL Exp. Cell Res. 317:2353-2363(2011).
RN [13]
RP FUNCTION, AND INDUCTION.
RX PubMed=21860593; DOI=10.4196/kjpp.2011.15.3.149;
RA Lee H.O., Byun Y.J., Cho K.O., Kim S.Y., Lee S.B., Kim H.S., Kwon O.J.,
RA Jeong S.W.;
RT "GS28 protects neuronal cell death induced by hydrogen peroxide under
RT glutathione-depleted condition.";
RL Korean J. Physiol. Pharmacol. 15:149-156(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Involved in transport from the ER to the Golgi apparatus as
CC well as in intra-Golgi transport. It belongs to a super-family of
CC proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive
CC factor) attachment protein receptor. May play a protective role against
CC hydrogen peroxide induced cytotoxicity under glutathione depleted
CC conditions in neuronal cells by regulating the intracellular ROS levels
CC via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14).
CC Participates in docking and fusion stage of ER to cis-Golgi transport.
CC Plays an important physiological role in VLDL-transport vesicle-Golgi
CC fusion and thus in VLDL delivery to the hepatic cis-Golgi.
CC {ECO:0000269|PubMed:15215310, ECO:0000269|PubMed:21860593}.
CC -!- SUBUNIT: Component of several multiprotein Golgi SNARE complexes.
CC Identified in a SNARE complex with BET1, STX5 and YKT6, in a SNARE
CC complex with BET1L, STX5 and YKT6, in a SNARE complex with STX5, GOSR2,
CC SEC22B and BET1, and in complex with STX5 and COG3. Interacts with
CC GABARAPL2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:15215310, ECO:0000269|PubMed:15728195,
CC ECO:0000269|PubMed:17274796, ECO:0000269|PubMed:17337506,
CC ECO:0000269|PubMed:21669198}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:15215310, ECO:0000269|PubMed:15728195,
CC ECO:0000269|PubMed:17274796, ECO:0000269|PubMed:17337506,
CC ECO:0000269|PubMed:21669198}. Note=Localizes throughout the Golgi
CC apparatus, with lowest levels in the trans-Golgi network (By
CC similarity). Enriched on vesicular components at the terminal rims of
CC the Golgi. Found in Golgi microtubules at low temperature (15 degrees
CC Celsius). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95249-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95249-2; Sequence=VSP_047326;
CC -!- INDUCTION: Expression induced by hydrogen peroxide in neuronal cells.
CC By monocrotaline in pulmonary epithelial cells (at protein level).
CC Negatively regulated by OSBPL7 via GABARAPL2 leading to degradation on
CC proteasomes (at protein level). {ECO:0000269|PubMed:17337506,
CC ECO:0000269|PubMed:21669198, ECO:0000269|PubMed:21860593}.
CC -!- SIMILARITY: Belongs to the GOSR1 family. {ECO:0000305}.
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DR EMBL; AF047438; AAC39889.1; -; mRNA.
DR EMBL; AF073926; AAD12945.1; -; mRNA.
DR EMBL; AC006050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471159; EAW51229.1; -; Genomic_DNA.
DR EMBL; BC040471; AAH40471.1; -; mRNA.
DR CCDS; CCDS11258.1; -. [O95249-1]
DR CCDS; CCDS45644.1; -. [O95249-2]
DR RefSeq; NP_001007025.1; NM_001007024.1. [O95249-2]
DR RefSeq; NP_001007026.1; NM_001007025.1.
DR RefSeq; NP_004862.1; NM_004871.2. [O95249-1]
DR RefSeq; XP_005258129.1; XM_005258072.2. [O95249-2]
DR AlphaFoldDB; O95249; -.
DR SMR; O95249; -.
DR BioGRID; 114903; 316.
DR IntAct; O95249; 21.
DR MINT; O95249; -.
DR STRING; 9606.ENSP00000225724; -.
DR iPTMnet; O95249; -.
DR MetOSite; O95249; -.
DR PhosphoSitePlus; O95249; -.
DR BioMuta; GOSR1; -.
DR EPD; O95249; -.
DR jPOST; O95249; -.
DR MassIVE; O95249; -.
DR MaxQB; O95249; -.
DR PaxDb; O95249; -.
DR PeptideAtlas; O95249; -.
DR PRIDE; O95249; -.
DR ProteomicsDB; 50745; -. [O95249-1]
DR Antibodypedia; 15149; 189 antibodies from 29 providers.
DR DNASU; 9527; -.
DR Ensembl; ENST00000225724.9; ENSP00000225724.5; ENSG00000108587.16. [O95249-1]
DR Ensembl; ENST00000467337.6; ENSP00000462638.1; ENSG00000108587.16. [O95249-2]
DR GeneID; 9527; -.
DR KEGG; hsa:9527; -.
DR UCSC; uc002hfe.4; human. [O95249-1]
DR CTD; 9527; -.
DR DisGeNET; 9527; -.
DR GeneCards; GOSR1; -.
DR HGNC; HGNC:4430; GOSR1.
DR HPA; ENSG00000108587; Low tissue specificity.
DR MIM; 604026; gene.
DR neXtProt; NX_O95249; -.
DR OpenTargets; ENSG00000108587; -.
DR PharmGKB; PA28815; -.
DR VEuPathDB; HostDB:ENSG00000108587; -.
DR eggNOG; KOG3208; Eukaryota.
DR GeneTree; ENSGT00390000008688; -.
DR HOGENOM; CLU_078034_0_0_1; -.
DR InParanoid; O95249; -.
DR OMA; QAYAVND; -.
DR OrthoDB; 1319902at2759; -.
DR PhylomeDB; O95249; -.
DR TreeFam; TF105782; -.
DR PathwayCommons; O95249; -.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR SignaLink; O95249; -.
DR BioGRID-ORCS; 9527; 35 hits in 1085 CRISPR screens.
DR ChiTaRS; GOSR1; human.
DR GeneWiki; GOSR1; -.
DR GenomeRNAi; 9527; -.
DR Pharos; O95249; Tbio.
DR PRO; PR:O95249; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O95249; protein.
DR Bgee; ENSG00000108587; Expressed in buccal mucosa cell and 214 other tissues.
DR ExpressionAtlas; O95249; baseline and differential.
DR Genevisible; O95249; HS.
DR GO; GO:0005801; C:cis-Golgi network; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005797; C:Golgi medial cisterna; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:HGNC-UCL.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:HGNC-UCL.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR InterPro; IPR023601; Golgi_SNAP_su1.
DR PANTHER; PTHR21094; PTHR21094; 1.
DR PIRSF; PIRSF027109; Golgi_SNARE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; ER-Golgi transport;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..250
FT /note="Golgi SNAP receptor complex member 1"
FT /id="PRO_0000212542"
FT TOPO_DOM 2..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT REGION 38..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 9..30
FT /evidence="ECO:0000255"
FT COILED 68..95
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..65
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_047326"
FT CONFLICT 11
FT /note="D -> GEARRPPD (in Ref. 1; AAC39889)"
FT /evidence="ECO:0000305"
FT CONFLICT 49..50
FT /note="Missing (in Ref. 1; AAC39889)"
FT /evidence="ECO:0000305"
FT CONFLICT 156..157
FT /note="NN -> TT (in Ref. 1; AAC39889)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="R -> G (in Ref. 1; AAC39889)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="L -> F (in Ref. 1; AAC39889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 250 AA; 28613 MW; EEDA4291436162F6 CRC64;
MAAGTSSYWE DLRKQARQLE NELDLKLVSF SKLCTSYSHS STRDGRRDRY SSDTTPLLNG
SSQDRMFETM AIEIEQLLAR LTGVNDKMAE YTNSAGVPSL NAALMHTLQR HRDILQDYTH
EFHKTKANFM AIRERENLMG SVRKDIESYK SGSGVNNRRT ELFLKEHDHL RNSDRLIEET
ISIAMATKEN MTSQRGMLKS IHSKMNTLAN RFPAVNSLIQ RINLRKRRDS LILGGVIGIC
TILLLLYAFH
