SAR1_ASPCL
ID SAR1_ASPCL Reviewed; 189 AA.
AC A1CRG9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Small COPII coat GTPase sar1;
DE EC=3.6.5.-;
GN Name=sar1; ORFNames=ACLA_029700;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
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 -!- 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; DS027059; EAW08240.1; -; Genomic_DNA.
DR RefSeq; XP_001269666.1; XM_001269665.1.
DR AlphaFoldDB; A1CRG9; -.
DR SMR; A1CRG9; -.
DR STRING; 5057.CADACLAP00002299; -.
DR PRIDE; A1CRG9; -.
DR EnsemblFungi; EAW08240; EAW08240; ACLA_029700.
DR GeneID; 4700605; -.
DR KEGG; act:ACLA_029700; -.
DR VEuPathDB; FungiDB:ACLA_029700; -.
DR eggNOG; KOG0077; Eukaryota.
DR HOGENOM; CLU_040729_6_0_1; -.
DR OMA; DDRIAQH; -.
DR OrthoDB; 1168548at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:EnsemblFungi.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:EnsemblFungi.
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; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:EnsemblFungi.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR GO; GO:0006886; P:intracellular protein transport; IEA:EnsemblFungi.
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; IEA:EnsemblFungi.
DR GO; GO:0003400; P:regulation of COPII vesicle coating; IEA:EnsemblFungi.
DR GO; GO:0016050; P:vesicle organization; IEA:EnsemblFungi.
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 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..189
FT /note="Small COPII coat GTPase sar1"
FT /id="PRO_0000295506"
FT BINDING 27..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 70..73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 129..132
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 189 AA; 21434 MW; E96B4181C6F95BFE CRC64;
MWIINWFYDV LASLGLLNKH AKLLFLGLDN AGKTTLLHML KNDRVATLQP TAHPTSEELA
IGNNRFTTFD LGGHQQARRL WKDYFPEVSG IVFLVDAKDH ERFPESKAEL DALLAMEELS
KVPFLILGNK IDHPDAVSED ELRHQLGLYQ TTGKGKVPLE GIRPIEVFMC SVVMRQGYGE
GIRWLSQYV
