SAR1_SCHPO
ID SAR1_SCHPO Reviewed; 190 AA.
AC Q01475;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Small COPII coat GTPase sar1;
DE EC=3.6.5.-;
GN Name=sar1; ORFNames=SPBC31F10.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1396601; DOI=10.1002/j.1460-2075.1992.tb05514.x;
RA d'Enfert C., Gensse M., Gaillardin C.;
RT "Fission yeast and a plant have functional homologues of the Sar1 and Sec12
RT proteins involved in ER to Golgi traffic in budding yeast.";
RL EMBO J. 11:4205-4211(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION.
RX PubMed=11839792; DOI=10.1242/jcs.115.2.421;
RA Matynia A., Salus S.S., Sazer S.;
RT "Three proteins required for early steps in the protein secretory pathway
RT also affect nuclear envelope structure and cell cycle progression in
RT fission yeast.";
RL J. Cell Sci. 115:421-431(2002).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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, ECO:0000269|PubMed:11839792}.
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; M95797; AAA35309.1; -; mRNA.
DR EMBL; CU329671; CAB10083.1; -; Genomic_DNA.
DR PIR; S28605; S28605.
DR RefSeq; NP_596568.1; NM_001022489.2.
DR AlphaFoldDB; Q01475; -.
DR SMR; Q01475; -.
DR BioGRID; 276967; 12.
DR STRING; 4896.SPBC31F10.06c.1; -.
DR iPTMnet; Q01475; -.
DR MaxQB; Q01475; -.
DR PaxDb; Q01475; -.
DR EnsemblFungi; SPBC31F10.06c.1; SPBC31F10.06c.1:pep; SPBC31F10.06c.
DR GeneID; 2540439; -.
DR KEGG; spo:SPBC31F10.06c; -.
DR PomBase; SPBC31F10.06c; sar1.
DR VEuPathDB; FungiDB:SPBC31F10.06c; -.
DR eggNOG; KOG0077; Eukaryota.
DR HOGENOM; CLU_040729_6_0_1; -.
DR InParanoid; Q01475; -.
DR OMA; DDRIAQH; -.
DR PhylomeDB; Q01475; -.
DR Reactome; R-SPO-204005; COPII-mediated vesicle transport.
DR Reactome; R-SPO-5694530; Cargo concentration in the ER.
DR Reactome; R-SPO-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:Q01475; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0030127; C:COPII vesicle coat; ISO:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:PomBase.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:PomBase.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; ISM:PomBase.
DR GO; GO:0003924; F:GTPase activity; ISM:PomBase.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:PomBase.
DR GO; GO:0006886; P:intracellular protein transport; IMP:PomBase.
DR GO; GO:0061024; P:membrane organization; IBA:GO_Central.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:PomBase.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0003400; P:regulation of COPII vesicle coating; IBA:GO_Central.
DR GO; GO:0016050; P:vesicle organization; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; GTP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..190
FT /note="Small COPII coat GTPase sar1"
FT /id="PRO_0000206273"
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"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 190 AA; 21280 MW; 27388CC7A033E0F1 CRC64;
MFIINWFYDA LAMLGLVNKH AKMLFLGLDN AGKTTLLHML KNDRLAVMQP TLHPTSEELA
IGNVRFTTFD LGGHQQARRL WRDYFPEVNG IVYLVDCCDF ERLSESKAEL DALLAMEELA
RVPFLILGNK IDAPGAISED ELKAALGLYQ TTGKGVSKPV PGIRPIEVFM CSVVLRQGYG
EGFKWLAQYV
