GOSR1_CRIGR
ID GOSR1_CRIGR Reviewed; 250 AA.
AC O08522;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 87.
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-24; 66-80; 88-108;
RP 111-124; 134-141 AND 159-171, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8636227; DOI=10.1083/jcb.133.3.507;
RA Nagahama M., Orci L., Ravazzola M., Amherdt M., Lacomis L., Tempst P.,
RA Rothman J.E., Soellner T.H.;
RT "A v-SNARE implicated in intra-Golgi transport.";
RL J. Cell Biol. 133:507-516(1996).
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:8636227}.
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:8636227}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:8636227}. 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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GOSR1 family. {ECO:0000305}.
CC -!- CAUTION: Formerly referred to as a v-SNARE. {ECO:0000305}.
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DR EMBL; U49841; AAB51019.1; -; mRNA.
DR RefSeq; NP_001233674.1; NM_001246745.1.
DR AlphaFoldDB; O08522; -.
DR SMR; O08522; -.
DR STRING; 10029.NP_001233674.1; -.
DR Ensembl; ENSCGRT00001017728; ENSCGRP00001013491; ENSCGRG00001014609.
DR GeneID; 100689312; -.
DR KEGG; cge:100689312; -.
DR CTD; 9527; -.
DR eggNOG; KOG3208; Eukaryota.
DR GeneTree; ENSGT00390000008688; -.
DR OrthoDB; 1319902at2759; -.
DR GO; GO:0005801; C:cis-Golgi network; IEA:InterPro.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005484; F:SNAP receptor activity; NAS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:UniProtKB.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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 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_0000212541"
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:0000250|UniProtKB:O95249"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95249"
SQ SEQUENCE 250 AA; 28510 MW; BBDA4DCB808608DD CRC64;
MAAGTSNYWE DLRKQARQLE NELDLKLVSF SKLCTSYSHS SARDGGRDRY SSDTTPLLNG
SSQDRMFETM AIEIEQLLAR LTGVNDKMAE YTNSAGVPSL NAALMHTLQR HRDILQDYTH
EFHKTKANFM AIRERENLMG SVRKDIESYK SGSGVNNRRT ELFLKEHDHL RNSDRLIEET
ISIAMATKEN MTSQRGMLKS IHSKMNTLAN RFPAVNSLIQ RINLRKRRDS LILGGVIGIC
TILLLLYAFH
