ID A0A0D1YSZ3_9EURO Unreviewed; 266 AA.
AC A0A0D1YSZ3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Small COPII coat GTPase SAR1 {ECO:0000256|ARBA:ARBA00021124};
DE AltName: Full=Small COPII coat GTPase sar1 {ECO:0000256|ARBA:ARBA00019961};
GN ORFNames=PV11_01422 {ECO:0000313|EMBL:KIV85762.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV85762.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV85762.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV85762.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00025639}.
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:0000256|ARBA:ARBA00001270};
CC -!- SUBUNIT: COPII is composed of at least 5 proteins: the SEC23/24
CC complex, the SEC13/31 complex and SAR1.
CC {ECO:0000256|ARBA:ARBA00011176}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004397}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004255}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.
CC {ECO:0000256|ARBA:ARBA00007507, ECO:0000256|RuleBase:RU003926}.
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DR EMBL; KN846951; KIV85762.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1YSZ3; -.
DR STRING; 1016849.A0A0D1YSZ3; -.
DR HOGENOM; CLU_040729_6_0_1; -.
DR OrthoDB; 5349301at2759; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR CDD; cd00879; Sar1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR45684; RE74312P; 1.
DR PANTHER; PTHR45684:SF2; RE74312P; 1.
DR Pfam; PF00025; Arf; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00177; ARF; 1.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51417; ARF; 1.
DR PROSITE; PS51422; SAR1; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU003926};
KW ER-Golgi transport {ECO:0000256|RuleBase:RU003926};
KW Golgi apparatus {ECO:0000256|RuleBase:RU003926};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein transport {ECO:0000256|RuleBase:RU003926};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW Transport {ECO:0000256|RuleBase:RU003926}.
SQ SEQUENCE 266 AA; 29833 MW; 54545B92A45381DB CRC64;
MPLGAGHSCC GISFPPEVAQ TTRDNETWPI NPIASEQESA SKRTQSHLAL LDRNPAPPIP
LRSQLSLNET TAYTDRIMWI INWFYDILAS LGLLNKHAKL LFLGLDNAGK TTLLHMLKND
RVAILQPTLH PTSEELAIGN NRFTTFDLGG HQQARRLWRD YFPEVSGIVF LVDAKDHERL
PEAKAELDAL LAMEDLSKTP FLILGNKIDH PDAVSEDELR HQLGLYQTTG KGKVPLEGIR
PIEVFMCSVV MRQGYGEGIR WLAQYV
//
