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GOSR1_RAT
ID   GOSR1_RAT               Reviewed;         250 AA.
AC   Q62931; A0JN01;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 138.
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;
DE            Short=GOS28;
GN   Name=Gosr1; Synonyms=Gs28;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 18-25; 50-53; 76-86;
RP   113-121; 127-133; 145-149; 160-165; 176-187 AND 212-225, AND FUNCTION.
RC   TISSUE=Brain;
RX   PubMed=8638159; DOI=10.1126/science.272.5265.1161;
RA   Subramaniam V.N., Peter F., Philip R., Wong S.H., Hong W.;
RT   "GS28, a 28-kilodalton Golgi SNARE that participates in ER-Golgi
RT   transport.";
RL   Science 272:1161-1163(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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   [3]
RP   PROTEIN SEQUENCE OF 18-26 AND 66-80, SUBUNIT, AND INTERACTION WITH STX5.
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=9094723; DOI=10.1016/s0092-8674(00)80191-9;
RA   Hay J.C., Chao D.S., Kuo C.S., Scheller R.H.;
RT   "Protein interactions regulating vesicle transport between the endoplasmic
RT   reticulum and Golgi apparatus in mammalian cells.";
RL   Cell 89:149-158(1997).
RN   [4]
RP   INTERACTION WITH BET1 AND STX5, AND SUBCELLULAR LOCATION.
RX   PubMed=9382863; DOI=10.1083/jcb.139.5.1157;
RA   Zhang T., Wong S.H., Tang B.L., Xu Y., Peter F., Subramaniam V.N., Hong W.;
RT   "The mammalian protein (rbet1) homologous to yeast Bet1p is primarily
RT   associated with the pre-Golgi intermediate compartment and is involved in
RT   vesicular transport from the endoplasmic reticulum to the Golgi
RT   apparatus.";
RL   J. Cell Biol. 139:1157-1168(1997).
RN   [5]
RP   INTERACTION WITH STX5, AND SUBCELLULAR LOCATION.
RX   PubMed=9647643; DOI=10.1083/jcb.141.7.1489;
RA   Hay J.C., Klumperman J., Oorschot V., Steegmaier M., Kuo C.S.,
RA   Scheller R.H.;
RT   "Localization, dynamics, and protein interactions reveal distinct roles for
RT   ER and Golgi SNAREs.";
RL   J. Cell Biol. 141:1489-1502(1998).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10585748; DOI=10.1006/abio.1999.4311;
RA   Plonne D., Cartwright I., Linss W., Dargel R., Graham J.M., Higgins J.A.;
RT   "Separation of the intracellular secretory compartment of rat liver and
RT   isolated rat hepatocytes in a single step using self-generating gradients
RT   of iodixanol.";
RL   Anal. Biochem. 276:88-96(1999).
RN   [7]
RP   INTERACTION WITH GABARAPL2, AND SUBCELLULAR LOCATION.
RX   PubMed=10747018; DOI=10.1093/emboj/19.7.1494;
RA   Sagiv Y., Legesse-Miller A., Porat A., Elazar Z.;
RT   "GATE-16, a membrane transport modulator, interacts with NSF and the Golgi
RT   v-SNARE GOS-28.";
RL   EMBO J. 19:1494-1504(2000).
RN   [8]
RP   INTERACTION WITH YKT6; BET1 AND STX5, AND SUBCELLULAR LOCATION.
RX   PubMed=11323436; DOI=10.1074/jbc.m102786200;
RA   Zhang T., Hong W.;
RT   "Ykt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and
RT   participates in a late stage in endoplasmic reticulum-Golgi transport.";
RL   J. Biol. Chem. 276:27480-27487(2001).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11748249; DOI=10.1083/jcb.200108017;
RA   Lanoix J., Ouwendijk J., Stark A., Szafer E., Cassel D., Dejgaard K.,
RA   Weiss M., Nilsson T.;
RT   "Sorting of Golgi resident proteins into different subpopulations of COPI
RT   vesicles: a role for ArfGAP1.";
RL   J. Cell Biol. 155:1199-1212(2001).
RN   [10]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=11927603; DOI=10.1083/jcb.200112127;
RA   Shorter J., Beard M.B., Seemann J., Dirac-Svejstrup A.B., Warren G.;
RT   "Sequential tethering of Golgins and catalysis of SNAREpin assembly by the
RT   vesicle-tethering protein p115.";
RL   J. Cell Biol. 157:45-62(2002).
RN   [11]
RP   INTERACTION WITH BET1L; STX5 AND YTK6, AND SUBCELLULAR LOCATION.
RX   PubMed=12388752; DOI=10.1091/mbc.e02-01-0004;
RA   Xu Y., Martin S., James D.E., Hong W.;
RT   "GS15 forms a SNARE complex with syntaxin 5, GS28, and Ykt6 and is
RT   implicated in traffic in the early cisternae of the Golgi apparatus.";
RL   Mol. Biol. Cell 13:3493-3507(2002).
RN   [12]
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=14742712; DOI=10.1091/mbc.e03-08-0625;
RA   Volchuk A., Ravazzola M., Perrelet A., Eng W.S., Di Liberto M.,
RA   Varlamov O., Fukasawa M., Engel T., Sollner T.H., Rothman J.E., Orci L.;
RT   "Countercurrent distribution of two distinct SNARE complexes mediating
RT   transport within the Golgi stack.";
RL   Mol. Biol. Cell 15:1506-1518(2004).
RN   [13]
RP   INTERACTION WITH BET1L AND COG3.
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   [14]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18648846; DOI=10.1007/s00418-008-0471-2;
RA   Vivero-Salmeron G., Ballesta J., Martinez-Menarguez J.A.;
RT   "Heterotypic tubular connections at the endoplasmic reticulum-Golgi complex
RT   interface.";
RL   Histochem. Cell Biol. 130:709-717(2008).
RN   [15]
RP   FUNCTION, SUBUNIT, INTERACTION WITH SEC22B, AND SUBCELLULAR LOCATION.
RX   PubMed=20450495; DOI=10.1042/bj20100336;
RA   Siddiqi S., Mani A.M., Siddiqi S.A.;
RT   "The identification of the SNARE complex required for the fusion of VLDL-
RT   transport vesicle with hepatic cis-Golgi.";
RL   Biochem. J. 429:391-401(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.
CC       {ECO:0000269|PubMed:14742712, ECO:0000269|PubMed:20450495,
CC       ECO:0000269|PubMed:8638159}.
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. Interacts with the 34 kDa STX5 isoform.
CC       {ECO:0000269|PubMed:10747018, ECO:0000269|PubMed:11323436,
CC       ECO:0000269|PubMed:11927603, ECO:0000269|PubMed:12388752,
CC       ECO:0000269|PubMed:15728195, ECO:0000269|PubMed:20450495,
CC       ECO:0000269|PubMed:9094723, ECO:0000269|PubMed:9382863,
CC       ECO:0000269|PubMed:9647643}.
CC   -!- INTERACTION:
CC       Q62931; Q08851: Stx5; NbExp=15; IntAct=EBI-7837133, EBI-2028244;
CC       Q62931; P41542: Uso1; NbExp=10; IntAct=EBI-7837133, EBI-4423297;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:10585748, ECO:0000269|PubMed:10747018,
CC       ECO:0000269|PubMed:11323436, ECO:0000269|PubMed:11748249,
CC       ECO:0000269|PubMed:11927603, ECO:0000269|PubMed:12388752,
CC       ECO:0000269|PubMed:14742712, ECO:0000269|PubMed:18648846,
CC       ECO:0000269|PubMed:20450495, ECO:0000269|PubMed:9382863,
CC       ECO:0000269|PubMed:9647643}; Single-pass type IV membrane protein
CC       {ECO:0000269|PubMed:10585748, ECO:0000269|PubMed:10747018,
CC       ECO:0000269|PubMed:11323436, ECO:0000269|PubMed:11748249,
CC       ECO:0000269|PubMed:11927603, ECO:0000269|PubMed:12388752,
CC       ECO:0000269|PubMed:14742712, ECO:0000269|PubMed:18648846,
CC       ECO:0000269|PubMed:20450495, ECO:0000269|PubMed:9382863,
CC       ECO:0000269|PubMed:9647643}. 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 apparatus.
CC   -!- SIMILARITY: Belongs to the GOSR1 family. {ECO:0000305}.
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DR   EMBL; U49099; AAC52597.1; -; mRNA.
DR   EMBL; BC126068; AAI26069.1; -; mRNA.
DR   RefSeq; NP_446036.1; NM_053584.2.
DR   AlphaFoldDB; Q62931; -.
DR   SMR; Q62931; -.
DR   CORUM; Q62931; -.
DR   IntAct; Q62931; 7.
DR   MINT; Q62931; -.
DR   STRING; 10116.ENSRNOP00000068434; -.
DR   iPTMnet; Q62931; -.
DR   PhosphoSitePlus; Q62931; -.
DR   jPOST; Q62931; -.
DR   PaxDb; Q62931; -.
DR   PRIDE; Q62931; -.
DR   Ensembl; ENSRNOT00000077038; ENSRNOP00000090076; ENSRNOG00000070896.
DR   GeneID; 94189; -.
DR   KEGG; rno:94189; -.
DR   CTD; 9527; -.
DR   RGD; 71093; Gosr1.
DR   VEuPathDB; HostDB:ENSRNOG00000003971; -.
DR   eggNOG; KOG3208; Eukaryota.
DR   GeneTree; ENSGT00390000008688; -.
DR   HOGENOM; CLU_078034_0_0_1; -.
DR   InParanoid; Q62931; -.
DR   OMA; QAYAVND; -.
DR   OrthoDB; 1319902at2759; -.
DR   PhylomeDB; Q62931; -.
DR   TreeFam; TF105782; -.
DR   Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-RNO-6811438; Intra-Golgi traffic.
DR   PRO; PR:Q62931; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000003971; Expressed in jejunum and 20 other tissues.
DR   Genevisible; Q62931; RN.
DR   GO; GO:0005801; C:cis-Golgi network; IDA:RGD.
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; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IDA:MGI.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0005484; F:SNAP receptor activity; ISO:RGD.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISO:RGD.
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_0000212545"
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..30
FT                   /evidence="ECO:0000255"
FT   COILED          68..95
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"
SQ   SEQUENCE   250 AA;  28534 MW;  0F85EDCE7ADA32E2 CRC64;
     MAAGTSNYWE DLRKQARQLE NELDLKLVSF SKLCTSYSHS SARDGGRDRY SSDTTPLLNG
     SSQDRMFETM AIEIEQLLAR LTGVNDKMAE YTHSAGVPSL NAALMHTLQR HRDILQDYTH
     EFHKTKANFM AIRERENLMG SVRKDIESYK SGSGVNNRRT ELFLKEHDHL RNSDRLIEET
     ISIAMATKEN MTSQRGMLKS IHSKMNTLAN RFPAVNSLIQ RINLRKRRDS LILGGVIGIC
     TILLLLYAFH
 
 
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