SAR1_DEBHA
ID SAR1_DEBHA Reviewed; 190 AA.
AC Q6BVA7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Small COPII coat GTPase SAR1;
DE EC=3.6.5.-;
GN Name=SAR1; OrderedLocusNames=DEHA2C04092g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382135; CAG85907.1; -; Genomic_DNA.
DR RefSeq; XP_457862.1; XM_457862.1.
DR AlphaFoldDB; Q6BVA7; -.
DR SMR; Q6BVA7; -.
DR STRING; 4959.XP_457862.1; -.
DR EnsemblFungi; CAG85907; CAG85907; DEHA2C04092g.
DR GeneID; 2900019; -.
DR KEGG; dha:DEHA2C04092g; -.
DR VEuPathDB; FungiDB:DEHA2C04092g; -.
DR eggNOG; KOG0077; Eukaryota.
DR HOGENOM; CLU_040729_6_0_1; -.
DR InParanoid; Q6BVA7; -.
DR OMA; DDRIAQH; -.
DR OrthoDB; 1168548at2759; -.
DR Proteomes; UP000000599; Chromosome C.
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; Reference proteome; Transport.
FT CHAIN 1..190
FT /note="Small COPII coat GTPase SAR1"
FT /id="PRO_0000295514"
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 190 AA; 21341 MW; D3DD172952B8F700 CRC64;
MWLFDWFQDV LASLGLWNKH AKLLFLGLDN AGKTTLLHML KNDRLATLQP TLHPTSEELA
IGSVRFTTFD LGGHQQARRL WKDYFPEVNG IVFLVDAADP ERFAESKAEL ESLFKIEELA
SVPFLILGNK IDASSAVGEM ELKSALGLYN TTGKDTGKLP EGQRPIEVFM VSVVMRMGYG
DGFKWLSQYI
