ID   SAR1_ASPNG              Reviewed;         189 AA.
AC   P0C950; A2Q8E3; P52886;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Small COPII coat GTPase SAR1;
DE            EC=3.6.5.-;
GN   Name=sar1; Synonyms=sarA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=N401;
RX   PubMed=9393442; DOI=10.1007/pl00008613;
RA   Veldhuisen G., Saloheimo M., Fiers M.A., Punt P.J., Contreras R.,
RA   Penttilae M., van den Hondel C.A.;
RT   "Isolation and analysis of functional homologues of the secretion-related
RT   SAR1 gene of Saccharomyces cerevisiae from Aspergillus niger and
RT   Trichoderma reesei.";
RL   Mol. Gen. Genet. 256:446-455(1997).
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; Z67742; CAA91555.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C950; -.
DR   SMR; P0C950; -.
DR   STRING; 5061.CADANGAP00000383; -.
DR   PRIDE; P0C950; -.
DR   VEuPathDB; FungiDB:An01g04040; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1142222; -.
DR   VEuPathDB; FungiDB:ATCC64974_19930; -.
DR   VEuPathDB; FungiDB:M747DRAFT_317527; -.
DR   eggNOG; KOG0077; Eukaryota.
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   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; Transport.
FT   CHAIN           1..189
FT                   /note="Small COPII coat GTPase SAR1"
FT                   /id="PRO_0000206271"
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;  21363 MW;  EB7775F2679DDEB8 CRC64;
     MWLINWFYDL LASLGLLNKH AKLLFLGLDN AGKTTLLHML KNDRVAILQP TAHPTSEELA
     IGNNRFTTFD LGGHQQARRL WKDYFPEVSG IVFLVDAKDH ECFPESKAEL DALLAMEELA
     KVPFLILGNK IDHPDAVSED DVRHQLGLYQ TTGKGKVPLE GIRPIEVFMC SVVMRQGYGE
     GIRWLSQYV