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 16-SEP-2015, entry version 121. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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- RT length 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 RT GS27 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., RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., RA 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 RT the 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., 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 [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 RT project: 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 RT transport from the early/recycling endosome to the trans-Golgi RT 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 RT in 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 RT enriched in 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- RT induced 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., RA Walther T.C., 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., 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 [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., RA Olkkonen V.M., Yan D.; RT "OSBP-related protein 7 interacts with GATE-16 and negatively RT regulates 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., RA Kwon O.J., 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, IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., 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). CC -!- FUNCTION: Involved in transport from the ER to the Golgi apparatus CC as well as in intra-Golgi transport. It belongs to a super-family CC of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide- CC sensitive factor) attachment protein receptor. May play a CC protective role against hydrogen peroxide induced cytotoxicity CC under glutathione depleted conditions in neuronal cells by CC regulating the intracellular ROS levels via inhibition of p38 MAPK CC (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and CC fusion stage of ER to cis-Golgi transport. Plays an important CC physiological role in VLDL-transport vesicle-Golgi fusion and thus CC 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, CC GOSR2, SEC22B and BET1, and in complex with STX5 and COG3. CC Interacts with 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 CC of the Golgi. Found in Golgi microtubules at low temperature (15 CC degrees 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 Note=Gene prediction based on EST data.; CC -!- INDUCTION: Expression induced by hydrogen peroxide in neuronal CC cells. By monocrotaline in pulmonary epithelial cells (at protein CC level). Negatively regulated by OSBPL7 via GABARAPL2 leading to CC degradation on proteasomes (at protein level). CC {ECO:0000269|PubMed:17337506, ECO:0000269|PubMed:21669198, CC ECO:0000269|PubMed:21860593}. CC -!- SIMILARITY: Belongs to the GOSR1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_005258072.1. [O95249-2] DR UniGene; Hs.462680; -. DR ProteinModelPortal; O95249; -. DR BioGrid; 114903; 27. DR IntAct; O95249; 5. DR STRING; 9606.ENSP00000225724; -. DR PhosphoSite; O95249; -. DR BioMuta; GOSR1; -. DR MaxQB; O95249; -. DR PaxDb; O95249; -. DR PRIDE; O95249; -. DR Ensembl; ENST00000225724; ENSP00000225724; ENSG00000108587. [O95249-1] DR Ensembl; ENST00000467337; ENSP00000462638; ENSG00000108587. [O95249-2] DR GeneID; 9527; -. DR KEGG; hsa:9527; -. DR UCSC; uc002hfe.3; human. [O95249-1] DR CTD; 9527; -. DR GeneCards; GC17P030477; -. DR HGNC; HGNC:4430; GOSR1. DR HPA; HPA020590; -. DR MIM; 604026; gene. DR neXtProt; NX_O95249; -. DR PharmGKB; PA28815; -. DR eggNOG; NOG321250; -. DR GeneTree; ENSGT00390000008688; -. DR HOGENOM; HOG000207760; -. DR HOVERGEN; HBG051764; -. DR InParanoid; O95249; -. DR KO; K08495; -. DR PhylomeDB; O95249; -. DR TreeFam; TF105782; -. DR ChiTaRS; GOSR1; human. DR GeneWiki; GOSR1; -. DR GenomeRNAi; 9527; -. DR NextBio; 35535992; -. DR PRO; PR:O95249; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; O95249; -. DR CleanEx; HS_GOSR1; -. DR ExpressionAtlas; O95249; baseline and differential. DR Genevisible; O95249; HS. DR GO; GO:0005801; C:cis-Golgi network; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0031201; C:SNARE complex; TAS:HGNC. DR GO; GO:0005484; F:SNAP receptor activity; IDA:HGNC. DR GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IEA:Ensembl. DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; TAS:ProtInc. DR GO; GO:0061025; P:membrane fusion; IDA:GOC. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:HGNC. 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; Complete proteome; KW ER-Golgi transport; Golgi apparatus; Membrane; Protein transport; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}. FT CHAIN 2 250 Golgi SNAP receptor complex member 1. FT /FTId=PRO_0000212542. FT TOPO_DOM 2 229 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 230 250 Helical; Anchor for type IV membrane FT protein. {ECO:0000255}. FT COILED 9 30 {ECO:0000255}. FT COILED 68 95 {ECO:0000255}. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000244|PubMed:22223895}. FT VAR_SEQ 1 65 Missing (in isoform 2). {ECO:0000305}. FT /FTId=VSP_047326. FT CONFLICT 11 11 D -> GEARRPPD (in Ref. 1; AAC39889). FT {ECO:0000305}. FT CONFLICT 49 50 Missing (in Ref. 1; AAC39889). FT {ECO:0000305}. FT CONFLICT 156 157 NN -> TT (in Ref. 1; AAC39889). FT {ECO:0000305}. FT CONFLICT 159 159 R -> G (in Ref. 1; AAC39889). FT {ECO:0000305}. FT CONFLICT 170 170 L -> F (in Ref. 1; AAC39889). FT {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 //