IRA2_YEAST
ID IRA2_YEAST Reviewed; 3079 AA.
AC P19158; D6W1Y7; O13592; Q08239;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Inhibitory regulator protein IRA2;
GN Name=IRA2; Synonyms=CCS1, GLC4; OrderedLocusNames=YOL081W; ORFNames=O0985;
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].
RX PubMed=2164637; DOI=10.1128/mcb.10.8.4303-4313.1990;
RA Tanaka K., Nakafuku M., Tamanoi F., Kaziro Y., Matsumoto K., Toh-e A.;
RT "IRA2, a second gene of Saccharomyces cerevisiae that encodes a protein
RT with a domain homologous to mammalian ras GTPase-activating protein.";
RL Mol. Cell. Biol. 10:4303-4313(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2423.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=7900427; DOI=10.1002/yea.320101015;
RA Zumstein E., Griffin H., Schweizer M.;
RT "Sequence of a 10.27 kb segment on the left arm of chromosome XV from
RT Saccharomyces cerevisiae includes part of the IRA2 gene and a putative new
RT gene.";
RL Yeast 10:1383-1387(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2423.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8533473; DOI=10.1002/yea.320111009;
RA Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.;
RT "A 29.425 kb segment on the left arm of yeast chromosome XV contains more
RT than twice as many unknown as known open reading frames.";
RL Yeast 11:975-986(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1982-3079.
RX PubMed=9178509;
RX DOI=10.1002/(sici)1097-0061(199705)13:6<583::aid-yea111>3.0.co;2-y;
RA Tzermia M., Katsoulou C., Alexandraki D.;
RT "Sequence analysis of a 33.2 kb segment from the left arm of yeast
RT chromosome XV reveals eight known genes and ten new open reading frames
RT including homologues of ABC transporters, inositol phosphatases and human
RT expressed sequence tags.";
RL Yeast 13:583-589(1997).
RN [7]
RP IDENTIFICATION OF CCS1 AS IRA2.
RX PubMed=1326414; DOI=10.1007/bf00351690;
RA Bussereau F., Dupont C.H., Boy-Marcotte E., Mallet L., Jacquet M.;
RT "The CCS1 gene from Saccharomyces cerevisiae which is involved in
RT mitochondrial functions is identified as IRA2 an attenuator of RAS1 and
RT RAS2 gene products.";
RL Curr. Genet. 21:325-329(1992).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [10]
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-635, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway.
CC Stimulates the GTPase activity of Ras proteins.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
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DR EMBL; M33779; AAA34710.1; -; Genomic_DNA.
DR EMBL; Z74823; CAA99093.1; -; Genomic_DNA.
DR EMBL; X75449; CAA53202.1; -; Genomic_DNA.
DR EMBL; X83121; CAA58201.1; -; Genomic_DNA.
DR EMBL; Z74822; CAA99092.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10703.1; -; Genomic_DNA.
DR PIR; S66775; RGBYI2.
DR RefSeq; NP_014560.1; NM_001183335.1.
DR SMR; P19158; -.
DR BioGRID; 34321; 992.
DR DIP; DIP-6376N; -.
DR IntAct; P19158; 4.
DR MINT; P19158; -.
DR STRING; 4932.YOL081W; -.
DR iPTMnet; P19158; -.
DR MaxQB; P19158; -.
DR PaxDb; P19158; -.
DR PRIDE; P19158; -.
DR EnsemblFungi; YOL081W_mRNA; YOL081W; YOL081W.
DR GeneID; 854073; -.
DR KEGG; sce:YOL081W; -.
DR SGD; S000005441; IRA2.
DR VEuPathDB; FungiDB:YOL081W; -.
DR eggNOG; KOG1826; Eukaryota.
DR GeneTree; ENSGT00940000176574; -.
DR HOGENOM; CLU_000439_0_0_1; -.
DR InParanoid; P19158; -.
DR OMA; WSELMIL; -.
DR BioCyc; YEAST:G3O-33484-MON; -.
DR Reactome; R-SCE-9696273; RND1 GTPase cycle.
DR PRO; PR:P19158; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P19158; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:SGD.
DR GO; GO:0070417; P:cellular response to cold; IMP:SGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IMP:SGD.
DR GO; GO:0071248; P:cellular response to metal ion; IMP:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:SGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:SGD.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR PANTHER; PTHR10194; PTHR10194; 1.
DR Pfam; PF00616; RasGAP; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..3079
FT /note="Inhibitory regulator protein IRA2"
FT /id="PRO_0000056658"
FT DOMAIN 1701..1890
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT REGION 392..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 635
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 2309
FT /note="D -> V (in Ref. 1; AAA34710)"
FT /evidence="ECO:0000305"
FT CONFLICT 2317
FT /note="K -> I (in Ref. 1; AAA34710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3079 AA; 351669 MW; C14B5396D6FB9B5C CRC64;
MSQPTKNKKK EHGTDSKSSR MTRTLVNHIL FERILPILPV ESNLSTYSEV EEYSSFISCR
SVLINVTVSR DANAMVEGTL ELIESLLQGH EIISDKGSSD VIESILIILR LLSDALEYNW
QNQESLHYND ISTHVEHDQE QKYRPKLNSI LPDYSSTHSN GNKHFFHQSK PQALIPELAS
KLLESCAKLK FNTRTLQILQ NMISHVHGNI LTTLSSSILP RHKSYLTRHN HPSHCKMIDS
TLGHILRFVA ASNPSEYFEF IRKSVQVPVT QTHTHSHSHS HSLPSSVYNS IVPHFDLFSF
IYLSKHNFKK YLELIKNLSV TLRKTIYHCL LLHYSAKAIM FWIMARPAEY YELFNLLKDN
NNEHSKSLNT LNHTLFEEIH STFNVNSMIT TNQNAHQGSS SPSSSSPSSP PSSSSSDNNN
QNIIAKSLSR QLSHHQSYIQ QQSERKLHSS WTTNSQSSTS LSSSTSNSTT TDFSTHTQPG
EYDPSLPDTP TMSNITISAS SLLSQTPTPT TQLQQRLNSA AAAAAAAASP SNSTPTGYTA
EQQSRASYDA HKTGHTGKDY DEHFLSVTRL DNVLELYTHF DDTEVLPHTS VLKFLTTLTM
FDIDLFNELN ATSFKYIPDC TMHRPKERTS SFNNTAHETG SEKTSGIKHI TQGLKKLTSL
PSSTKKTVKF VKMLLRNLNG NQAVSDVALL DTMRALLSFF TMTSAVFLVD RNLPSVLFAK
RLIPIMGTNL SVGQDWNSKI NNSLMVCLKK NSTTFVQLQL IFFSSAIQFD HELLLARLSI
DTMANNLNMQ KLCLYTEGFR IFFDIPSKKE LRKAIAVKIS KFFKTLFSII ADILLQEFPY
FDEQITDIVA SILDGTIINE YGTKKHFKGS SPSLCSTTRS RSGSTSQSSM TPVSPLGLDT
DICPMNTLSL VGSSTSRNSD NVNSLNSSPK NLSSDPYLSH LVAPRARHAL GGPSSIIRNK
IPTTLTSPPG TEKSSPVQRP QTESISATPM AITNSTPLSS AAFGIRSPLQ KIRTRRYSDE
SLGKFMKSTN NYIQEHLIPK DLNEATLQDA RRIMINIFSI FKRPNSYFII PHNINSNLQW
VSQDFRNIMK PIFVAIVSPD VDLQNTAQSF MDTLLSNVIT YGESDENISI EGYHLLCSYT
VTLFAMGLFD LKINNEKRQI LLDITVKFMK VRSHLAGIAE ASHHMEYISD SEKLTFPLIM
GTVGRALFVS LYSSQQKIEK TLKIAYTEYL SAINFHERNI DDADKTWVHN IEFVEAMCHD
NYTTSGSIAF QRRTRNNILR FATIPNAILL DSMRMIYKKW HTYTHSKSLE KQERNDFRNF
AGILASLSGI LFINKKILQE MYPYLLDTVS ELKKNIDSFI SKQCQWLNYP DLLTRENSRD
ILSVELHPLS FNLLFNNLRL KLKELACSDL SIPENESSYV LLEQIIKMLR TILGRDDDNY
VMMLFSTEIV DLIDLLTDEI KKIPAYCPKY LKAIIQMTKM FSALQHSEVN LGVKNHFHVK
NKWLRQITDW FQVSIAREYD FENLSKPLKE MDLVKRDMDI LYIDTAIEAS TAIAYLTRHT
FLEIPPAASD PELSRSRSVI FGFYFNILMK GLEKSSDRDN YPVFLRHKMS VLNDNVILSL
TNLSNTNVDA SLQFTLPMGY SGNRNIRNAF LEVFINIVTN YRTYTAKTDL GKLEAADKFL
RYTIEHPQLS SFGAAVCPAS DIDAYAAGLI NAFETRNATH IVVAQLIKNE IEKSSRPTDI
LRRNSCATRS LSMLARSKGN EYLIRTLQPL LKKIIQNRDF FEIEKLKPED SDAERQIELF
VKYMNELLES ISNSVSYFPP PLFYICQNIY KVACEKFPDH AIIAAGSFVF LRFFCPALVS
PDSENIIDIS HLSEKRTFIS LAKVIQNIAN GSENFSRWPA LCSQKDFLKE CSDRIFRFLA
ELCRTDRTID IQVRTDPTPI AFDYQFLHSF VYLYGLEVRR NVLNEAKHDD GDIDGDDFYK
TTFLLIDDVL GQLGQPKMEF SNEIPIYIRE HMDDYPELYE FMNRHAFRNI ETSTAYSPSV
HESTSSEGIP IITLTMSNFS DRHVDIDTVA YKFLQIYARI WTTKHCLIID CTEFDEGGLD
MRKFISLVMG LLPEVAPKNC IGCYYFNVNE TFMDNYGKCL DKDNVYVSSK IPHYFINSNS
DEGLMKSVGI TGQGLKVLQD IRVSLHDITL YDEKRNRFTP VSLKIGDIYF QVLHETPRQY
KIRDMGTLFD VKFNDVYEIS RIFEVHVSSI TGVAAEFTVT FQDERRLIFS SPKYLEIVKM
FYYAQIRLES EYEMDNNSST SSPNSNNKDK QQKERTKLLC HLLLVSLIGL FDESKKMKNS
SYNLIAATEA SFGLNFGSHF HRSPEVYVPE DTTTFLGVIG KSLAESNPEL TAYMFIYVLE
ALKNNVIPHV YIPHTICGLS YWIPNLYQHV YLADDEEGPE NISHIFRILI RLSVRETDFK
AVYMQYVWLL LLDDGRLTDI IVDEVINHAL ERDSENRDWK KTISLLTVLP TTEVANNIIQ
KILAKIRSFL PSLKLEAMTQ SWSELTILVK ISIHVFFETS LLVQMYLPEI LFIVSLLIDV
GPRELRSSLH QLLMNVCHSL AINSALPQDH RNNLDEISDI FAHQKVKFMF GFSEDKGRIL
QIFSASSFAS KFNILDFFIN NILLLMEYSS TYEANVWKTR YKKYVLESVF TSNSFLSARS
IMIVGIMGKS YITEGLCKAM LIETMKVIAE PKITDEHLFL AISHIFTYSK IVEGLDPNLD
LMKHLFWFST LFLESRHPII FEGALLFVSN CIRRLYMAQF ENESETSLIS TLLKGRKFAH
TFLSKIENLS GIVWNEDNFT HILIFIINKG LSNPFIKSTA FDFLKMMFRN SYFEHQINQK
SDHYLCYMFL LYFVLNCNQF EELLGDVDFE GEMVNIENKN TIPKILLEWL SSDNENANIT
LYQGAILFKC SVTDEPSRFR FALIIRHLLT KKPICALRFY SVIRNEIRKI SAFEQNSDCV
PLAFDILNLL VTHSESNSLE KLHEESIERL TKRGLSIVTS SGIFAKNSDM MIPLDVKPED
IYERKRIMTM ILSRMSCSA
