TAO3_YEAST
ID TAO3_YEAST Reviewed; 2376 AA.
AC P40468; D6VVF8; Q45T93;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Cell morphogenesis protein PAG1;
DE AltName: Full=Protein TAO3;
GN Name=TAO3; Synonyms=PAG1; OrderedLocusNames=YIL129C;
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 200060 / W303, ATCC 204508 / S288c,
RC ATCC 204626 / S288c / A364A, and Sigma 1278B;
RX PubMed=16273108; DOI=10.1038/ng1674;
RA Deutschbauer A.M., Davis R.W.;
RT "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL Nat. Genet. 37:1333-1340(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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, AND INTERACTION WITH CBK1.
RX PubMed=11854408; DOI=10.1091/mbc.01-07-0365;
RA Du L.L., Novick P.;
RT "Pag1p, a novel protein associated with protein kinase Cbk1p, is required
RT for cell morphogenesis and proliferation in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 13:503-514(2002).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2264 AND SER-2267, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2355, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND THR-2264, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1144 AND THR-2264, 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).
CC -!- FUNCTION: Seems to play a role in cell morphogenesis.
CC {ECO:0000269|PubMed:11854408}.
CC -!- SUBUNIT: Associates with CBK1.
CC -!- INTERACTION:
CC P40468; P53894: CBK1; NbExp=8; IntAct=EBI-18961, EBI-4110;
CC -!- MISCELLANEOUS: Present with 206 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: To S.pombe mor2. {ECO:0000305}.
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DR EMBL; DQ116812; AAZ23264.1; -; Genomic_DNA.
DR EMBL; DQ116814; AAZ23266.1; -; Genomic_DNA.
DR EMBL; DQ116817; AAZ23269.1; -; Genomic_DNA.
DR EMBL; DQ116824; AAZ23276.1; -; Genomic_DNA.
DR EMBL; Z38059; CAA86149.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08424.1; -; Genomic_DNA.
DR PIR; S48405; S48405.
DR RefSeq; NP_012137.3; NM_001179477.3.
DR AlphaFoldDB; P40468; -.
DR BioGRID; 34862; 670.
DR DIP; DIP-5950N; -.
DR IntAct; P40468; 12.
DR MINT; P40468; -.
DR STRING; 4932.YIL129C; -.
DR iPTMnet; P40468; -.
DR MaxQB; P40468; -.
DR PaxDb; P40468; -.
DR PRIDE; P40468; -.
DR EnsemblFungi; YIL129C_mRNA; YIL129C; YIL129C.
DR GeneID; 854677; -.
DR KEGG; sce:YIL129C; -.
DR SGD; S000001391; TAO3.
DR VEuPathDB; FungiDB:YIL129C; -.
DR eggNOG; KOG1825; Eukaryota.
DR GeneTree; ENSGT00610000086058; -.
DR HOGENOM; CLU_000325_0_0_1; -.
DR InParanoid; P40468; -.
DR OMA; GPTQFCQ; -.
DR BioCyc; YEAST:G3O-31380-MON; -.
DR PRO; PR:P40468; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40468; protein.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0005933; C:cellular bud; IDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
DR GO; GO:0007114; P:cell budding; IMP:SGD.
DR GO; GO:0000902; P:cell morphogenesis; IMP:SGD.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR025614; Cell_morpho_N.
DR InterPro; IPR025481; Cell_Morphogen_C.
DR InterPro; IPR039867; Furry/Tao3/Mor2.
DR InterPro; IPR029473; MOR2-PAG1_mid.
DR PANTHER; PTHR12295; PTHR12295; 1.
DR Pfam; PF14225; MOR2-PAG1_C; 1.
DR Pfam; PF14228; MOR2-PAG1_mid; 3.
DR Pfam; PF14222; MOR2-PAG1_N; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..2376
FT /note="Cell morphogenesis protein PAG1"
FT /id="PRO_0000072430"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 1144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 2264
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 2267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 2355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 2376 AA; 269858 MW; 08958191BE969C1B CRC64;
MASRFTFPPQ RDQGIGFTFP PTNKAEGSSN NNQISIDIDP SGQDVLEEIN EAPLNTFPLH
QSVTDAPIID IPSPTDMSEG TSLNNQLLLR QQQQQGTGEG QALPPTFVEE QSDQNKISML
LPEQKQQRMQ ESAPPDITAK SVAEDYVTTL RQQMATDWKS PSEYALHILF TKFIRYAENK
LNMCLQQLDM AEPPIVEILG EGVDPSFDEI IKSLGHIAKK KPKPVIDAMM FWRKTKSEAA
NSASEEMEKL LKEYEFEKAH PSQAHFLMNR RLSRSSSNTT SKYKHNNNTN NLPGMKRHVS
SSFNNKVPLI KASSSNNSAT SSPSIANSQL KSLENTIEVA KEEAFLADRK SLISIYILCR
VLNEIVKQAS SNEEEDLSDK LEEIVFTQLK TTDPLSISTS LIKSSNWNSF AELLGSMSEK
KFLSVSDRFI ADLEKIPAYI PPELEPSTHL LILGMRYLKL RNYPLEKFEE SADFMKSLSK
FFAKTENFPV CLAYAEVTNQ LLLPLAGSLT AEVNHPTWVE AMSTLLNTAK RLQADSKYWV
SGFKLTVSIL CASPPDLFSK QWLSLLEANA SKVKSKSLNE RIIFAVGLSR LVWVYLYRCP
ETLNNTTRTL TKLLQLYLNT RKKENWITGD FGLLNPLTDA LISIGFLHPN FLMEQALIPL
IRQSFNGSNL ENINYEKLIL TINTYKGLLV TKERPRFPED DNRLYELNLN NITVNQVQEA
SSINHTEISD YFYKLFLLLD SSIGSEVWSP ENQHQKQSSN AFSPFGFSFS NDNDSSKNKS
LYVILFGTII EAIPCCLSIS RTIPYKSTIE ILSRNAVHSE VIISSSSQNA LRALASKKNP
YTLITWFAKY SFDFDEKTQS SYNMSYLSSK EYNRLLILYV ELLECWLEEF QSSNKEENKK
ETGLDGIRLL PIDAEQEESN ETEKLEWKNT VTVIEEVEGN GLFFLCSHDA KIRRLGIQIL
RIIFKFDEAM MEKTEKLSNG HSRSSSHFAA DRGTRLIDLL NECNTTTLIN PHKATLSAVE
KTRFSRLNSK YKRGLLIKLA ESEYGVDAAL WQRAFPKLLA LVFKTCPMAM ALCRSIVCIR
LVQVHEIILR VANDVDFKLK NVLPETIVNQ WKLYLIAACT SLTSTFDQKL HIPSNIPQHG
RKKSQQIFTV QHQKIKSAKS IFKMVLPLLN AKYIMIRDAI ITGLSSMNIN IFKAYVEAID
VFLVAWKEGS SNNQIRVEMF HILTILSPYL KSDMIFNDEW ILRKLSEFLQ KTKQFLEKDS
VQISYEYQSL RSYFAGLILS YYMAVREHPL IDELFPFQAR ASCFNFLKEW CGYGEYEPIS
EERYAIMIKN TESGRDRTAI TTGIEFQKNR LQMIVLETMV VLCSDPITQT LDDDLELPIV
ISFDTEDLLA WIEALFDSDN TTVKNLGVRA LENLLDKNRE NFKLFRDVAF QCVSHHSHPS
VAVLYYTTLC KSVLKLDNLV LDEDELVSLG LYGLVADKED TRTFAVDLLS AVETKLHNSS
YTKVFKERLA NSSKTVYKST AKEISSIFAE LLSQDLCLRI FSSLVRILDL FPFEIKRDLL
VLMVPWVNKF TLKSLEELDT FMVLNNLFYI TIDLNDSLPN EVEQLWISLG KGNSFQNIHV
SLEYIINSSM NHCNPLFVQY ARDIVLYLAN IPGGIGLLDT LLNNLEPKYM VPLAKHTFNE
PMNNNKYSFL GNIWERLNYN GKRIIFSKAQ LSIIFLVNLL TNLSESVKAK IPLLLHMSIC
LLDHYVPLIH ESACKIASTL IFGLAPSHEK SEETVKLLRN KHALWSYDNL MKKGARSPKT
MDLLIRNIIS IFSDLDEFQV TWQRIALKWA TTCSVRHIAC RSFQIFRSLL TFLDQEMLRD
MLHRLSNTIS DGNVDIQGFA MQILMTLNAI MAELDPTNLI SFPQLFWSIT ACLSSIHEQE
FIEVLSCLSK FISKIDLDSP DTVQCLVAIF PSNWEGRFDG LQQIVMTGLR SANSLEITWK
FLDKLNLLKD SRIIANTESR LLFALIANLP RFLNAMDRKD FTGIQVAADS LIELANAYKQ
PSLSRLIDSL AKNKFRSKKD FMSQVVSFIS RNYFPSYSAQ TLVFLLGLLF NKIGWIRVQT
LEILKYVFPL IDLRRPEFIG VGADLISPLL RLLFTEYEAK ALEVLDCVPN VSGSKMDKDV
LRITMGNKDV KDGDNATTTL FGLPEDSGWS VPMPTMTAAT TRHNVHAVFM TCGTGKSDEV
SAHGSDDMDA VIEFHADGDY ELGRMDTIVE FHADGDYDLG RMDTNDSISV AEEKDASLSH
MWAELDNLDS FFTKDTNVPN ISSKMGMGIP HGRSDSIETT RTDQTFSFES APQLYDKKVS
VILNRSLSRT PSNVSFKTHL ADSFAVKINR NGKPRI