GOSR1_MOUSE
ID GOSR1_MOUSE Reviewed; 250 AA.
AC O88630; Q91VU9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 139.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bui T.D., Subramaniam V.N., Hong W.;
RT "Mouse cis-Golgi p28 (GS28) mRNA.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 PROTEIN SEQUENCE OF 33-49, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP SUBCELLULAR LOCATION, AND INDUCTION BY 25-HYDROXYCHOLESTEROL.
RX PubMed=15250942; DOI=10.1111/j.1600-0749.2004.00161.x;
RA Hall A.M., Krishnamoorthy L., Orlow S.J.;
RT "25-hydroxycholesterol acts in the Golgi compartment to induce degradation
RT of tyrosinase.";
RL Pigment Cell Res. 17:396-406(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By
CC similarity). {ECO:0000250}.
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:15250942}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:15250942}. Note=Localizes throughout the Golgi
CC apparatus, with lowest levels in the trans-Golgi network. Enriched on
CC vesicular components at the terminal rims of the Golgi. {ECO:0000250}.
CC -!- INDUCTION: Decreased levels in 25-hydroxycholesterol treated
CC melanocytes (at protein level). {ECO:0000269|PubMed:15250942}.
CC -!- SIMILARITY: Belongs to the GOSR1 family. {ECO:0000305}.
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DR EMBL; AF079901; AAC32189.1; -; mRNA.
DR EMBL; AK133836; BAE21873.1; -; mRNA.
DR EMBL; AK134515; BAE22167.1; -; mRNA.
DR EMBL; AK147799; BAE28147.1; -; mRNA.
DR EMBL; AK154972; BAE32964.1; -; mRNA.
DR EMBL; AK161386; BAE36365.1; -; mRNA.
DR EMBL; BX000359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466596; EDL12868.1; -; Genomic_DNA.
DR EMBL; BC008542; AAH08542.1; -; mRNA.
DR CCDS; CCDS25070.1; -.
DR RefSeq; NP_058090.2; NM_016810.3.
DR AlphaFoldDB; O88630; -.
DR SMR; O88630; -.
DR BioGRID; 207294; 5.
DR STRING; 10090.ENSMUSP00000010536; -.
DR iPTMnet; O88630; -.
DR PhosphoSitePlus; O88630; -.
DR SwissPalm; O88630; -.
DR EPD; O88630; -.
DR PaxDb; O88630; -.
DR PeptideAtlas; O88630; -.
DR PRIDE; O88630; -.
DR ProteomicsDB; 271009; -.
DR Antibodypedia; 15149; 189 antibodies from 29 providers.
DR DNASU; 53334; -.
DR Ensembl; ENSMUST00000010536; ENSMUSP00000010536; ENSMUSG00000010392.
DR GeneID; 53334; -.
DR KEGG; mmu:53334; -.
DR UCSC; uc007kfz.1; mouse.
DR CTD; 9527; -.
DR MGI; MGI:1858260; Gosr1.
DR VEuPathDB; HostDB:ENSMUSG00000010392; -.
DR eggNOG; KOG3208; Eukaryota.
DR GeneTree; ENSGT00390000008688; -.
DR HOGENOM; CLU_078034_0_0_1; -.
DR InParanoid; O88630; -.
DR OMA; QAYAVND; -.
DR OrthoDB; 1319902at2759; -.
DR PhylomeDB; O88630; -.
DR TreeFam; TF105782; -.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR BioGRID-ORCS; 53334; 20 hits in 73 CRISPR screens.
DR PRO; PR:O88630; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O88630; protein.
DR Bgee; ENSMUSG00000010392; Expressed in lumbar subsegment of spinal cord and 237 other tissues.
DR Genevisible; O88630; MM.
DR GO; GO:0005801; C:cis-Golgi network; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0005797; C:Golgi medial cisterna; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005484; F:SNAP receptor activity; ISO:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:MGI.
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; Coiled coil; Direct protein sequencing; 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:0000250|UniProtKB:O95249"
FT CHAIN 2..250
FT /note="Golgi SNAP receptor complex member 1"
FT /id="PRO_0000212543"
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 37..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 9..27
FT /evidence="ECO:0000255"
FT COILED 72..93
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O95249"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95249"
FT CONFLICT 30
FT /note="F -> S (in Ref. 1; AAC32189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 250 AA; 28489 MW; ACF7FF5CCA0C2D52 CRC64;
MAAGTSNYWE DLRKQARQLE NELDLKLVSF SKLCTSYSHS GSRDGGRDRY SSDTTPLLNG
SSQDRMFETM AIEIEQLLAR LTGVNDKMAE YTHSAGVPSL NAALMHTLQR HRDILQDYTH
EFHKTKANFT AIRERENLMG SVRKDIESYK SGSGVNNRRT ELFLKEHDHL RNSDRLIEET
ISIAMATKEN MTSQRGMLKS IHSKMNTLAN RFPAVNSLIQ RINLRKRRDS LILGGVIGIC
TILLLLYAFH
