ID A0A135LX35_PENPA Unreviewed; 248 AA.
AC A0A135LX35;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=PGRI_005740 {ECO:0000313|EMBL:KXG53524.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG53524.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG53524.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG53524.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXG53524.1}.
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DR EMBL; LHQR01000014; KXG53524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135LX35; -.
DR STRING; 5078.A0A135LX35; -.
DR OMA; DCADYER; -.
DR OrthoDB; 5349301at2759; -.
DR Proteomes; UP000070168; 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|ARBA:ARBA00022824,
KW 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:UP000070168};
KW Transport {ECO:0000256|RuleBase:RU003926}.
SQ SEQUENCE 248 AA; 27771 MW; 6F4B894F1EBAF29B CRC64;
MWIVNWFYDV LASLGLLNKH AKLLFLGLDN AGKTTLLHML KNDRVAVLQP TAHPTSEELA
IGNNRFTTFD LGGHQQARRL WKDYFPEVSG IVFLVDAKDY ERFPESKAEL DALLAMEELS
KVPFLVLGNK IDHPDAVSED ELRHQLGLYQ TTGKGKVPLE GIRPIEVFMC SVVMRQESYL
FPDTDLPLSP INAKSIFIHL SKSPNETKMA LVLASPLAHF NIALHLNTQS HTPPTNPIIF
TPGRTCTS
//
