SAR1_YEAST
ID SAR1_YEAST Reviewed; 190 AA.
AC P20606; D6W3F2;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Small COPII coat GTPase SAR1;
DE EC=3.6.5.- {ECO:0000269|PubMed:8419365, ECO:0000269|PubMed:9756629};
DE AltName: Full=GTP-binding protein SAR1;
DE AltName: Full=Secretion-associated RAS-related protein 1;
GN Name=SAR1; OrderedLocusNames=YPL218W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2512296; DOI=10.1083/jcb.109.6.2677;
RA Nakano A., Muramatsu M.-A.;
RT "A novel GTP-binding protein, Sar1p, is involved in transport from the
RT endoplasmic reticulum to the Golgi apparatus.";
RL J. Cell Biol. 109:2677-2691(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=1907491; DOI=10.1016/0167-4889(91)90114-d;
RA Nishikawa S., Nakano A.;
RT "The GTP-binding Sar1 protein is localized to the early compartment of the
RT yeast secretory pathway.";
RL Biochim. Biophys. Acta 1093:135-143(1991).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=1907973; DOI=10.1083/jcb.114.4.663;
RA d'Enfert C., Wuestehube L.J., Lila T., Schekman R.W.;
RT "Sec12p-dependent membrane binding of the small GTP-binding protein Sar1p
RT promotes formation of transport vesicles from the ER.";
RL J. Cell Biol. 114:663-670(1991).
RN [6]
RP FUNCTION.
RX PubMed=1907974; DOI=10.1083/jcb.114.4.671;
RA Oka T., Nishikawa S., Nakano A.;
RT "Reconstitution of GTP-binding Sar1 protein function in ER to Golgi
RT transport.";
RL J. Cell Biol. 114:671-679(1991).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=1922074; DOI=10.1128/mcb.11.11.5727-5734.1991;
RA d'Enfert C., Barlowe C., Nishikawa S., Nakano A., Schekman R.W.;
RT "Structural and functional dissection of a membrane glycoprotein required
RT for vesicle budding from the endoplasmic reticulum.";
RL Mol. Cell. Biol. 11:5727-5734(1991).
RN [8]
RP CATALYTIC ACTIVITY.
RX PubMed=8419365; DOI=10.1016/s0021-9258(18)54015-1;
RA Barlowe C., d'Enfert C., Schekman R.W.;
RT "Purification and characterization of SAR1p, a small GTP-binding protein
RT required for transport vesicle formation from the endoplasmic reticulum.";
RL J. Biol. Chem. 268:873-879(1993).
RN [9]
RP CHARACTERIZATION, ACTIVITY REGULATION, AND INTERACTION WITH SEC23.
RX PubMed=8451644; DOI=10.1126/science.8451644;
RA Yoshihisa T., Barlowe C., Schekman R.W.;
RT "Requirement for a GTPase-activating protein in vesicle budding from the
RT endoplasmic reticulum.";
RL Science 259:1466-1468(1993).
RN [10]
RP MUTAGENESIS OF ASP-32; LYS-36; THR-54; ASP-73; HIS-77; ASN-132 AND CYS-171.
RX PubMed=7822237; DOI=10.1093/oxfordjournals.jbchem.a124513;
RA Nakano A., Otsuka H., Yamagishi M., Yamamoto E., Kimura K., Nishikawa S.,
RA Oka T.;
RT "Mutational analysis of the Sar1 protein, a small GTPase which is essential
RT for vesicular transport from the endoplasmic reticulum.";
RL J. Biochem. 116:243-247(1994).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8106544; DOI=10.1083/jcb.124.4.425;
RA Oka T., Nakano A.;
RT "Inhibition of GTP hydrolysis by Sar1p causes accumulation of vesicles that
RT are a functional intermediate of the ER-to-Golgi transport in yeast.";
RL J. Cell Biol. 124:425-434(1994).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8548805; DOI=10.1016/0092-8674(95)90144-2;
RA Bednarek S.Y., Ravazzola M., Hosobuchi M., Amherdt M., Perrelet A.,
RA Schekman R.W., Orci L.;
RT "COPI- and COPII-coated vesicles bud directly from the endoplasmic
RT reticulum in yeast.";
RL Cell 83:1183-1196(1995).
RN [13]
RP FUNCTION.
RX PubMed=8530490; DOI=10.1074/jbc.270.51.30567;
RA Yeung T., Barlowe C., Schekman R.W.;
RT "Uncoupled packaging of targeting and cargo molecules during transport
RT vesicle budding from the endoplasmic reticulum.";
RL J. Biol. Chem. 270:30567-30570(1995).
RN [14]
RP MUTAGENESIS OF ASP-32; GLU-112 AND ASN-132.
RX PubMed=8889833; DOI=10.1093/oxfordjournals.jbchem.a021432;
RA Yamanushi T., Hirata A., Oka T., Nakano A.;
RT "Characterization of yeast sar1 temperature-sensitive mutants, which are
RT defective in protein transport from the endoplasmic reticulum.";
RL J. Biochem. 120:452-458(1996).
RN [15]
RP FUNCTION.
RX PubMed=9023343; DOI=10.1073/pnas.94.3.837;
RA Campbell J.L., Schekman R.W.;
RT "Selective packaging of cargo molecules into endoplasmic reticulum-derived
RT COPII vesicles.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:837-842(1997).
RN [16]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9568718; DOI=10.1016/s0092-8674(00)81577-9;
RA Matsuoka K., Orci L., Amherdt M., Bednarek S.Y., Hamamoto S.,
RA Schekman R.W., Yeung T.;
RT "COPII-coated vesicle formation reconstituted with purified coat proteins
RT and chemically defined liposomes.";
RL Cell 93:263-275(1998).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-32; THR-54; HIS-77 AND
RP GLU-112.
RX PubMed=9756629; DOI=10.1093/oxfordjournals.jbchem.a022185;
RA Saito Y., Kimura K., Oka T., Nakano A.;
RT "Activities of mutant Sar1 proteins in guanine nucleotide binding, GTP
RT hydrolysis, and cell-free transport from the endoplasmic reticulum to the
RT Golgi apparatus.";
RL J. Biochem. 124:816-823(1998).
RN [18]
RP FUNCTION.
RX PubMed=9428766; DOI=10.1038/34438;
RA Kuehn M.J., Herrmann J.M., Schekman R.W.;
RT "COPII-cargo interactions direct protein sorting into ER-derived transport
RT vesicles.";
RL Nature 391:187-190(1998).
RN [19]
RP INTERACTION WITH BET1; BOS1; SEC23 AND SEC24.
RX PubMed=9685263; DOI=10.1126/science.281.5377.698;
RA Springer S., Schekman R.W.;
RT "Nucleation of COPII vesicular coat complex by endoplasmic reticulum to
RT Golgi vesicle SNAREs.";
RL Science 281:698-700(1998).
RN [20]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10720463; DOI=10.1006/meth.2000.0955;
RA Matsuoka K., Schekman R.W.;
RT "The use of liposomes to study COPII- and COPI-coated vesicle formation and
RT membrane protein sorting.";
RL Methods 20:417-428(2000).
RN [21]
RP INTERACTION WITH EMP24 AND ERV25.
RX PubMed=11560939; DOI=10.1074/jbc.m108113200;
RA Belden W.J., Barlowe C.;
RT "Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in
RT transport between the endoplasmic reticulum and Golgi complex.";
RL J. Biol. Chem. 276:43040-43048(2001).
RN [22]
RP FUNCTION, AND IDENTIFICATION IN THE COPII COAT.
RX PubMed=11389436; DOI=10.1038/35078500;
RA Antonny B., Madden D.T., Hamamoto S., Orci L., Schekman R.W.;
RT "Dynamics of the COPII coat with GTP and stable analogues.";
RL Nat. Cell Biol. 3:531-537(2001).
RN [23]
RP SUBCELLULAR LOCATION.
RX PubMed=12235121; DOI=10.1083/jcb.200207053;
RA Supek F., Madden D.T., Hamamoto S., Orci L., Schekman R.W.;
RT "Sec16p potentiates the action of COPII proteins to bud transport
RT vesicles.";
RL J. Cell Biol. 158:1029-1038(2002).
RN [24]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12912905; DOI=10.1093/emboj/cdg390;
RA Pathre P., Shome K., Blumental-Perry A., Bielli A., Haney C.J., Alber S.,
RA Watkins S.C., Romero G., Aridor M.;
RT "Activation of phospholipase D by the small GTPase Sar1p is required to
RT support COPII assembly and ER export.";
RL EMBO J. 22:4059-4069(2003).
RN [25]
RP STRUCTURE OF THE COPII COMPLEX.
RX PubMed=12671686; DOI=10.1038/sj.embor.embor812;
RA Antonny B., Gounon P., Schekman R.W., Orci L.;
RT "Self-assembly of minimal COPII cages.";
RL EMBO Rep. 4:419-424(2003).
RN [26]
RP FUNCTION IN COPII COMPLEX ASSEMBLY.
RX PubMed=14627716; DOI=10.1074/jbc.c300457200;
RA Sato K., Nakano A.;
RT "Reconstitution of coat protein complex II (COPII) vesicle formation from
RT cargo-reconstituted proteoliposomes reveals the potential role of GTP
RT hydrolysis by Sar1p in protein sorting.";
RL J. Biol. Chem. 279:1330-1335(2004).
RN [27]
RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16107716; DOI=10.1128/mcb.25.17.7696-7710.2005;
RA Inadome H., Noda Y., Adachi H., Yoda K.;
RT "Immunoisolation of the yeast Golgi subcompartments and characterization of
RT a novel membrane protein, Svp26, discovered in the Sed5-containing
RT compartments.";
RL Mol. Cell. Biol. 25:7696-7710(2005).
RN [28]
RP FUNCTION IN COPII COMPLEX ASSEMBLY AND DISASSEMBLY.
RX PubMed=15665868; DOI=10.1038/nsmb893;
RA Sato K., Nakano A.;
RT "Dissection of COPII subunit-cargo assembly and disassembly kinetics during
RT Sar1p-GTP hydrolysis.";
RL Nat. Struct. Mol. Biol. 12:167-174(2005).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-155 AND SER-157, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [31]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [32]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SEC23 AND A GTP
RP ANALOG.
RX PubMed=12239560; DOI=10.1038/nature01040;
RA Bi X., Corpina R.A., Goldberg J.;
RT "Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle
RT coat.";
RL Nature 419:271-277(2002).
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 by SEC12 binds to membranes first
CC and 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:0000269|PubMed:10720463, ECO:0000269|PubMed:11389436,
CC ECO:0000269|PubMed:12912905, ECO:0000269|PubMed:14627716,
CC ECO:0000269|PubMed:15665868, ECO:0000269|PubMed:1907973,
CC ECO:0000269|PubMed:1907974, ECO:0000269|PubMed:2512296,
CC ECO:0000269|PubMed:8106544, ECO:0000269|PubMed:8530490,
CC ECO:0000269|PubMed:8548805, ECO:0000269|PubMed:9023343,
CC ECO:0000269|PubMed:9428766, ECO:0000269|PubMed:9756629}.
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:0000269|PubMed:8419365, ECO:0000269|PubMed:9756629};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000305|PubMed:8419365, ECO:0000305|PubMed:9756629};
CC -!- SUBUNIT: COPII is composed of at least 5 proteins: the SEC23/24
CC complex, the SEC13/31 complex and SAR1. Interacts with EMP24.
CC {ECO:0000269|PubMed:11389436, ECO:0000269|PubMed:11560939,
CC ECO:0000269|PubMed:12239560, ECO:0000269|PubMed:8451644,
CC ECO:0000269|PubMed:9568718, ECO:0000269|PubMed:9685263}.
CC -!- INTERACTION:
CC P20606; P15303: SEC23; NbExp=3; IntAct=EBI-16472, EBI-16584;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic
CC reticulum membrane; Peripheral membrane protein; Cytoplasmic side.
CC Golgi apparatus membrane {ECO:0000305}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Membrane
CC association requires the presence of the SEC12 exchange factor.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. SAR1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X51667; CAA35978.1; -; Genomic_DNA.
DR EMBL; Z73574; CAA97933.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11218.1; -; Genomic_DNA.
DR PIR; A33619; A33619.
DR RefSeq; NP_015106.1; NM_001184032.1.
DR PDB; 1M2O; X-ray; 2.50 A; B/D=1-190.
DR PDB; 2QTV; X-ray; 2.50 A; B=23-189.
DR PDB; 4BZI; EM; 23.00 A; B/J/K=1-190.
DR PDB; 6GNI; EM; 4.90 A; B=23-189.
DR PDB; 6X90; X-ray; 2.26 A; A=24-190.
DR PDB; 6ZGA; EM; 4.60 A; C=1-190, G=1-189.
DR PDBsum; 1M2O; -.
DR PDBsum; 2QTV; -.
DR PDBsum; 4BZI; -.
DR PDBsum; 6GNI; -.
DR PDBsum; 6X90; -.
DR PDBsum; 6ZGA; -.
DR AlphaFoldDB; P20606; -.
DR SMR; P20606; -.
DR BioGRID; 35967; 79.
DR ComplexPortal; CPX-2523; COPII vesicle coat complex.
DR DIP; DIP-2231N; -.
DR IntAct; P20606; 14.
DR MINT; P20606; -.
DR STRING; 4932.YPL218W; -.
DR iPTMnet; P20606; -.
DR MaxQB; P20606; -.
DR PaxDb; P20606; -.
DR PRIDE; P20606; -.
DR EnsemblFungi; YPL218W_mRNA; YPL218W; YPL218W.
DR GeneID; 855883; -.
DR KEGG; sce:YPL218W; -.
DR SGD; S000006139; SAR1.
DR VEuPathDB; FungiDB:YPL218W; -.
DR eggNOG; KOG0077; Eukaryota.
DR GeneTree; ENSGT00940000171772; -.
DR HOGENOM; CLU_040729_6_0_1; -.
DR InParanoid; P20606; -.
DR OMA; DDRIAQH; -.
DR BioCyc; YEAST:G3O-34107-MON; -.
DR Reactome; R-SCE-204005; COPII-mediated vesicle transport.
DR Reactome; R-SCE-5694530; Cargo concentration in the ER.
DR Reactome; R-SCE-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR EvolutionaryTrace; P20606; -.
DR PRO; PR:P20606; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P20606; protein.
DR GO; GO:0030127; C:COPII vesicle coat; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ComplexPortal.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0061024; P:membrane organization; IMP:SGD.
DR GO; GO:0000266; P:mitochondrial fission; IGI:SGD.
DR GO; GO:0007006; P:mitochondrial membrane organization; IMP:SGD.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:SGD.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IDA:ComplexPortal.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IDA:ComplexPortal.
DR GO; GO:0003400; P:regulation of COPII vesicle coating; IDA:SGD.
DR GO; GO:0016050; P:vesicle organization; IDA:SGD.
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 3D-structure; Cytoplasmic vesicle; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; GTP-binding; Hydrolase;
KW Isopeptide bond; Membrane; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..190
FT /note="Small COPII coat GTPase SAR1"
FT /id="PRO_0000206275"
FT BINDING 30..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 73..76
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 132..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT MOD_RES 155
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 32
FT /note="D->G: No cell growth at 37 degrees Celsius.
FT Decreases GTP binding and ER-to-Golgi vesicle transport."
FT /evidence="ECO:0000269|PubMed:7822237,
FT ECO:0000269|PubMed:8889833, ECO:0000269|PubMed:9756629"
FT MUTAGEN 36
FT /note="K->M: No cell growth at 23 or 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:7822237"
FT MUTAGEN 54
FT /note="T->A: No cell growth at 23 or 37 degrees Celsius.
FT Decreases GTP binding and impairs ER-to-Golgi vesicle
FT transport."
FT /evidence="ECO:0000269|PubMed:7822237,
FT ECO:0000269|PubMed:9756629"
FT MUTAGEN 73
FT /note="D->V: No cell growth at 23 or 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:7822237"
FT MUTAGEN 77
FT /note="H->L: No cell growth at 23 or 37 degrees Celsius.
FT Impairs ER-to-Golgi vesicle transport."
FT /evidence="ECO:0000269|PubMed:7822237,
FT ECO:0000269|PubMed:9756629"
FT MUTAGEN 112
FT /note="E->K: Decreases guanine nucleotide binding."
FT /evidence="ECO:0000269|PubMed:8889833,
FT ECO:0000269|PubMed:9756629"
FT MUTAGEN 132
FT /note="N->I: No cell growth at 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:7822237,
FT ECO:0000269|PubMed:8889833"
FT MUTAGEN 171
FT /note="C->S: Normal cell growth."
FT /evidence="ECO:0000269|PubMed:7822237"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:6X90"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:6X90"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:1M2O"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:6X90"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:6X90"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:6X90"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:6X90"
FT HELIX 106..117
FT /evidence="ECO:0007829|PDB:6X90"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:6X90"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:6X90"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2QTV"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:6X90"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:6X90"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:6X90"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:6X90"
SQ SEQUENCE 190 AA; 21451 MW; E2348B57896B5A13 CRC64;
MAGWDIFGWF RDVLASLGLW NKHGKLLFLG LDNAGKTTLL HMLKNDRLAT LQPTWHPTSE
ELAIGNIKFT TFDLGGHIQA RRLWKDYFPE VNGIVFLVDA ADPERFDEAR VELDALFNIA
ELKDVPFVIL GNKIDAPNAV SEAELRSALG LLNTTGSQRI EGQRPVEVFM CSVVMRNGYL
EAFQWLSQYI
