SAR1_CAEEL
ID SAR1_CAEEL Reviewed; 193 AA.
AC Q23445;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=GTP-binding protein SAR1;
GN Name=sar-1 {ECO:0000312|WormBase:ZK180.4};
GN ORFNames=ZK180.4 {ECO:0000312|WormBase:ZK180.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32053105; DOI=10.7554/elife.50986;
RA Haag A., Walser M., Henggeler A., Hajnal A.;
RT "The CHORD protein CHP-1 regulates EGF receptor trafficking and signaling
RT in C. elegans and in human cells.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Involved in transport from the endoplasmic reticulum to the
CC Golgi apparatus (By similarity). Also plays a role in transporting the
CC tyrosine kinase receptor let-23 from the endoplasmic reticulum to the
CC plasma membrane of vulval precursor cells (PubMed:32053105).
CC {ECO:0000250|UniProtKB:P20606, ECO:0000269|PubMed:32053105}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}. Golgi
CC apparatus {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in the reduced
CC plasma membrane localization and intracellular accumulation of the
CC tyrosine kinase receptor let-23 in vulval precursor cells.
CC {ECO:0000269|PubMed:32053105}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.
CC {ECO:0000305}.
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DR EMBL; BX284604; CCD73074.1; -; Genomic_DNA.
DR PIR; T29706; T29706.
DR RefSeq; NP_500582.1; NM_068181.3.
DR AlphaFoldDB; Q23445; -.
DR SMR; Q23445; -.
DR BioGRID; 42347; 16.
DR DIP; DIP-25417N; -.
DR STRING; 6239.ZK180.4; -.
DR EPD; Q23445; -.
DR PaxDb; Q23445; -.
DR PeptideAtlas; Q23445; -.
DR EnsemblMetazoa; ZK180.4.1; ZK180.4.1; WBGene00022678.
DR GeneID; 177217; -.
DR KEGG; cel:CELE_ZK180.4; -.
DR UCSC; ZK180.4; c. elegans.
DR CTD; 177217; -.
DR WormBase; ZK180.4; CE07622; WBGene00022678; sar-1.
DR eggNOG; KOG0077; Eukaryota.
DR GeneTree; ENSGT00940000171772; -.
DR HOGENOM; CLU_040729_6_0_1; -.
DR InParanoid; Q23445; -.
DR OMA; DDRIAQH; -.
DR OrthoDB; 1168548at2759; -.
DR PhylomeDB; Q23445; -.
DR Reactome; R-CEL-204005; COPII-mediated vesicle transport.
DR Reactome; R-CEL-5694530; Cargo concentration in the ER.
DR Reactome; R-CEL-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:Q23445; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00022678; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0003400; P:regulation of COPII vesicle coating; IBA:GO_Central.
DR GO; GO:0016050; P:vesicle organization; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR InterPro; IPR006687; Small_GTPase_SAR1.
DR PANTHER; PTHR45684; PTHR45684; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51422; SAR1; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW Nucleotide-binding; Protein transport; Reference proteome; Transport.
FT CHAIN 1..193
FT /note="GTP-binding protein SAR1"
FT /id="PRO_0000206263"
FT BINDING 28..35
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 71..74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 130..133
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 193 AA; 21709 MW; 03E76FD1EC163C5F CRC64;
MSFLWDWFNG VLNMLGLANK KGKLVFLGLD NAGKTTLLHM LKDDRIAQHV PTLHPTSEQM
SLGGISFTTY DLGGHAQARR VWKDYFPAVD AVVFLIDVAD AERMQESRVE LESLLQDEQI
ASVPVLILGN KIDKPGALSE DQLKWQLNIQ HMCTGKGDVS RNEMASRPME VFMCSVLQRQ
GYGEGIRWLG QYL
