GYP2_YEAST
ID GYP2_YEAST Reviewed; 950 AA.
AC P53258; D6VUN2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=GTPase-activating protein GYP2;
DE AltName: Full=MAC1-dependent regulator;
DE AltName: Full=Protein MIC1;
GN Name=MDR1; Synonyms=GYP2, MIC1; OrderedLocusNames=YGR100W; ORFNames=G5717;
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].
RC STRAIN=ATCC 204511 / S288c / AB972;
RA Serpe M., Kosman D.J.;
RT "MIC1 encodes a protein interacting with Mac1p, a nuclear metal
RT activator.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 FUNCTION.
RX PubMed=10559187; DOI=10.1074/jbc.274.47.33186;
RA Albert S., Gallwitz D.;
RT "Two new members of a family of Ypt/Rab GTPase activating proteins.
RT Promiscuity of substrate recognition.";
RL J. Biol. Chem. 274:33186-33189(1999).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12807768; DOI=10.1093/genetics/164.2.469;
RA Lafourcade C., Galan J.-M., Peter M.;
RT "Opposite roles of the F-box protein Rcy1p and the GTPase-activating
RT protein Gyp2p during recycling of internalized proteins in yeast.";
RL Genetics 164:469-477(2003).
RN [6]
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 [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION.
RX PubMed=15574876; DOI=10.1091/mbc.e04-08-0700;
RA Sciorra V.A., Audhya A., Parsons A.B., Segev N., Boone C., Emr S.D.;
RT "Synthetic genetic array analysis of the PtdIns 4-kinase Pik1p identifies
RT components in a Golgi-specific Ypt31/rab-GTPase signaling pathway.";
RL Mol. Biol. Cell 16:776-793(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-764 AND SER-871, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-764 AND SER-871, AND
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 SER-764, 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).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Stimulates specifically the GTPase activity of SEC4, YPT6 and
CC YPT36. Inactivates YPT6 during recycling between the endosome and the
CC Golgi compartments. {ECO:0000269|PubMed:10559187,
CC ECO:0000269|PubMed:12807768, ECO:0000269|PubMed:15574876}.
CC -!- SUBUNIT: Interacts with MAC1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12807768,
CC ECO:0000269|PubMed:14562095}. Note=Distributed throughout the cytoplasm
CC and accumulates in punctate structures, which concentrate in an actin-
CC dependent manner at sites of polarized growth.
CC -!- MISCELLANEOUS: Present with 768 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U52667; AAB01977.1; -; Genomic_DNA.
DR EMBL; Z72885; CAA97103.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08193.1; -; Genomic_DNA.
DR PIR; S64405; S64405.
DR RefSeq; NP_011614.1; NM_001181229.1.
DR AlphaFoldDB; P53258; -.
DR SMR; P53258; -.
DR BioGRID; 33343; 95.
DR DIP; DIP-4578N; -.
DR IntAct; P53258; 4.
DR STRING; 4932.YGR100W; -.
DR iPTMnet; P53258; -.
DR MaxQB; P53258; -.
DR PaxDb; P53258; -.
DR PRIDE; P53258; -.
DR EnsemblFungi; YGR100W_mRNA; YGR100W; YGR100W.
DR GeneID; 852992; -.
DR KEGG; sce:YGR100W; -.
DR SGD; S000003332; MDR1.
DR VEuPathDB; FungiDB:YGR100W; -.
DR eggNOG; KOG4347; Eukaryota.
DR GeneTree; ENSGT00940000173529; -.
DR HOGENOM; CLU_003538_0_1_1; -.
DR InParanoid; P53258; -.
DR OMA; LTAYSWI; -.
DR BioCyc; YEAST:G3O-30810-MON; -.
DR PRO; PR:P53258; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53258; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IDA:SGD.
DR GO; GO:0090630; P:activation of GTPase activity; IGI:SGD.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR000195; Rab-GTPase-TBC_dom.
DR InterPro; IPR035969; Rab-GTPase_TBC_sf.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF00566; RabGAP-TBC; 1.
DR SMART; SM00568; GRAM; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47923; SSF47923; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; GTPase activation; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..950
FT /note="GTPase-activating protein GYP2"
FT /id="PRO_0000208011"
FT DOMAIN 29..116
FT /note="GRAM"
FT DOMAIN 244..432
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00163"
FT DOMAIN 602..637
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 638..673
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 878..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 885..902
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 903..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 764
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
SQ SEQUENCE 950 AA; 109259 MW; 888BC930C1358657 CRC64;
MSFFDSLRQK APFLDKLADS FTPTLTRDEK FRLKYKLPAN ENILEDTNAE VSFATSIKDG
KGHSDRVNNK GRKTAYVYSG RLFLTPHFLV FRDAFDHSSC VLILNISTIK RVERSPSESY
EFALLVTLYT GAKVLIQFIG IRYRSEQFCD KLKLNLKENI PNAKTLPAFL ETSYSEFLIA
KNILGKKDIT VPRAGLGQHF KYPGNPTMVK EKAKLRLWFD YFRENGRNLA VVQTPMFRKL
IRIGVPNRMR GEIWELCSGA MYMRYANSGE YERILNENAG KTSQAIDEIE KDLKRSLPEY
SAYQTEEGIQ RLRNVLTAYS WKNPDVGYCQ AMNIVVAGFL IFMSEEQAFW CLCNLCDIYV
PGYYSKTMYG TLLDQRVFES FVEDRMPVLW EYILQHDIQL SVVSLPWFLS LFFTSMPLEY
AVRIMDIFFM NGSITLFQVA LAVLKINADD ILQADDDGMF IAIIKHYFQT LGQSAHPDSS
DIKYRQITKF QELLVTAFKE FSVISEEMAM HARHKYEKGI FQNIETFMKR TQLRHMPKTF
NLSSDDLSNI YDMFYQSIET YKISMGTGSS NMGFEVFIQF LSKFCDSCRP CEKDKDPAFR
KQKRNFLQRL FDNWDSAHIG ELTLNDVVTG LDKLVTVDLL QAINYFFSLY DTDGDGELHR
EEVLQLSEGL LLLTEPWKSG RYVDLLTKKR IEDDIAENII KESGGEIATM NQIELPTGVT
IDEEKYKVEQ AERYLKAASN FLQRSFEYAK AVDLAEEVNL IDLSDDEGEE KRTVKQKQLE
SIKANAALDP THPKVIDLPT FRMIILADET YELFFSNTLR SSVHVDEHVN IDNKNKVLRS
MFDGILADGK RVAEQVRRRV DSVATRSSIA SVESTPTAAA SSITTKEEKY DDLDDFTSEH
QPENEELLQS SWFEIDDANE TSTKAIQERS FEPLSANSSE EKSNLIEFEA
