SAR1_ENCCU
ID SAR1_ENCCU Reviewed; 221 AA.
AC Q8SS09;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Small COPII coat GTPase SAR1;
DE EC=3.6.5.-;
GN Name=SAR1; OrderedLocusNames=ECU05_0090;
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1;
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], DEVELOPMENTAL
RP STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=16691553; DOI=10.1002/pmic.200500796;
RA Brosson D., Kuhn L., Delbac F., Garin J., Vivares C.P., Texier C.;
RT "Proteomic analysis of the eukaryotic parasite Encephalitozoon cuniculi
RT (microsporidia): a reference map for proteins expressed in late sporogonial
RT stages.";
RL Proteomics 6:3625-3635(2006).
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 -!- DEVELOPMENTAL STAGE: Expressed in late sporogonial stages.
CC {ECO:0000269|PubMed:16691553}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.
CC {ECO:0000305}.
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DR EMBL; AL590445; CAD26526.1; -; Genomic_DNA.
DR RefSeq; NP_597349.1; NM_001041215.1.
DR PDB; 6VS4; X-ray; 2.40 A; A/B=1-221.
DR PDBsum; 6VS4; -.
DR AlphaFoldDB; Q8SS09; -.
DR SMR; Q8SS09; -.
DR STRING; 284813.Q8SS09; -.
DR GeneID; 859013; -.
DR KEGG; ecu:ECU05_0090; -.
DR VEuPathDB; MicrosporidiaDB:ECU05_0090; -.
DR HOGENOM; CLU_040729_6_0_1; -.
DR InParanoid; Q8SS09; -.
DR OMA; FYNCDGI; -.
DR OrthoDB; 1168548at2759; -.
DR Proteomes; UP000000819; Chromosome V.
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.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Hydrolase; Membrane;
KW Nucleotide-binding; Protein transport; Reference proteome; Transport.
FT CHAIN 1..221
FT /note="Small COPII coat GTPase SAR1"
FT /id="PRO_0000382918"
FT BINDING 48..55
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..94
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 151..154
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT HELIX 5..29
FT /evidence="ECO:0007829|PDB:6VS4"
FT STRAND 36..43
FT /evidence="ECO:0007829|PDB:6VS4"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:6VS4"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6VS4"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:6VS4"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:6VS4"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:6VS4"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:6VS4"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:6VS4"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:6VS4"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6VS4"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:6VS4"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:6VS4"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:6VS4"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:6VS4"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6VS4"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:6VS4"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:6VS4"
FT HELIX 200..219
FT /evidence="ECO:0007829|PDB:6VS4"
SQ SEQUENCE 221 AA; 25103 MW; 6BA2DEA6BE00AB98 CRC64;
MLDNIQEYLG VVKAKLTEFY EKVFQNFVKS LFGKPSSILF LGIDNAGKTT LVNKLKSDST
DVYMPTHHPS TSYIEIGNLK AQVIDLGGHT AARLAWRDYF YDCHGIVFIV DVHDVERFQE
VREAYETVLS LEKRAPVVVL MNKIDLEGHT PETAEADYQW KSWLSQETGI ENQEDPERGQ
VVKIFYVTIT SGSANSITGP LARAFKWLEA MITYNNKKES L
