SAR1_CANAL
ID SAR1_CANAL Reviewed; 190 AA.
AC Q59S78; A0A1D8PPU1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Small COPII coat GTPase SAR1;
DE EC=3.6.5.- {ECO:0000269|PubMed:11921090};
GN Name=SAR1; OrderedLocusNames=CAALFM_C602220WA;
GN ORFNames=CaO19.10966, CaO19.3462;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP IDENTIFICATION OF INTRON, FUNCTION, CATALYTIC ACTIVITY, AND GTP-BINDING.
RX PubMed=11921090; DOI=10.1002/yea.842;
RA Jiang L., Lee C.-M., Shen S.-H.;
RT "Functional characterization of the Candida albicans homologue of
RT secretion-associated and Ras-related (Sar1) protein.";
RL Yeast 19:423-428(2002).
CC -!- FUNCTION: Small GTPase component of the coat protein complex II (COPII)
CC which promotes the formation of transport vesicles from the endoplasmic
CC reticulum (ER). The coat has two main functions, the physical
CC deformation of the endoplasmic reticulum membrane into vesicles and the
CC selection of cargo molecules. SAR1 controls the coat assembly in a
CC stepwise manner. Activated SAR1-GTP binds to membranes first and
CC recruits the SEC23/24 complex. These SEC23/24-SAR1 prebudding
CC intermediates are then collected by the SEC13/31 complex as subunits
CC polymerize to form coated transport vesicles. Conversion to SAR1-GDP
CC triggers coat release and recycles COPII subunits (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:11921090}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000269|PubMed:11921090};
CC -!- SUBUNIT: COPII is composed of at least 5 proteins: the SEC23/24
CC complex, the SEC13/31 complex and SAR1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.
CC {ECO:0000305}.
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DR EMBL; CP017628; AOW30157.1; -; Genomic_DNA.
DR RefSeq; XP_019331008.1; XM_019475463.1.
DR AlphaFoldDB; Q59S78; -.
DR SMR; Q59S78; -.
DR STRING; 237561.Q59S78; -.
DR PRIDE; Q59S78; -.
DR GeneID; 3645865; -.
DR KEGG; cal:CAALFM_C602220WA; -.
DR CGD; CAL0000177161; SAR1.
DR VEuPathDB; FungiDB:C6_02220W_A; -.
DR eggNOG; KOG0077; Eukaryota.
DR HOGENOM; CLU_040729_6_0_1; -.
DR InParanoid; Q59S78; -.
DR OMA; DDRIAQH; -.
DR OrthoDB; 1168548at2759; -.
DR PRO; PR:Q59S78; -.
DR Proteomes; UP000000559; Chromosome 6.
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:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005525; F:GTP binding; IDA:CGD.
DR GO; GO:0003924; F:GTPase activity; IGI:CGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IGI:CGD.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:0000266; P:mitochondrial fission; IEA:EnsemblFungi.
DR GO; GO:0007006; P:mitochondrial membrane organization; IEA:EnsemblFungi.
DR GO; GO:0006998; P:nuclear envelope organization; IEA:EnsemblFungi.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
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 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; GTP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..190
FT /note="Small COPII coat GTPase SAR1"
FT /id="PRO_0000295510"
FT BINDING 27..32
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:11921090"
FT BINDING 70..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:11921090"
FT BINDING 129..132
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:11921090"
SQ SEQUENCE 190 AA; 21482 MW; B579CFC4558C2A69 CRC64;
MWIFDWFQDI LSSLGLWNKH AKLLFLGLDN AGKTTLLHML KNDRLATLQP TLHPTSEELA
IGSVRFTTFD LGGHQQARRL WKDYFPEVNG IVFLVDAADT ERFAESKAEL ESLFRIEELS
QVPFVILGNK IDVPTAVGEM ELKNALGLYN TTGKDTGKLP EGTRPIEVFM VSVVMRSGYG
EAFKWLSQYI
