PXL1_YEAST
ID PXL1_YEAST Reviewed; 706 AA.
AC P36166; D6VXF0;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Paxillin-like protein 1;
GN Name=PXL1; OrderedLocusNames=YKR090W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 688.
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 [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-63, 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 -!- MISCELLANEOUS: Present with 1310 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z28315; CAA82169.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09240.2; -; Genomic_DNA.
DR PIR; S38168; S38168.
DR RefSeq; NP_013016.4; NM_001179880.4.
DR AlphaFoldDB; P36166; -.
DR BioGRID; 34221; 32.
DR DIP; DIP-763N; -.
DR IntAct; P36166; 19.
DR MINT; P36166; -.
DR STRING; 4932.YKR090W; -.
DR iPTMnet; P36166; -.
DR MaxQB; P36166; -.
DR PaxDb; P36166; -.
DR PRIDE; P36166; -.
DR EnsemblFungi; YKR090W_mRNA; YKR090W; YKR090W.
DR GeneID; 853965; -.
DR KEGG; sce:YKR090W; -.
DR SGD; S000001798; PXL1.
DR VEuPathDB; FungiDB:YKR090W; -.
DR eggNOG; KOG1703; Eukaryota.
DR HOGENOM; CLU_016772_0_0_1; -.
DR InParanoid; P36166; -.
DR OMA; IYGSPFP; -.
DR BioCyc; YEAST:G3O-32053-MON; -.
DR PRO; PR:P36166; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36166; protein.
DR GO; GO:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; 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:0030427; C:site of polarized growth; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; IGI:SGD.
DR GO; GO:0030011; P:maintenance of cell polarity; IMP:SGD.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IGI:SGD.
DR InterPro; IPR034962; Pxl1.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24216:SF15; PTHR24216:SF15; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00132; LIM; 2.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW LIM domain; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Zinc.
FT CHAIN 1..706
FT /note="Paxillin-like protein 1"
FT /id="PRO_0000075893"
FT DOMAIN 556..612
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 621..672
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 24..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 688
FT /note="S -> T (in Ref. 1; CAA82169)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 706 AA; 79434 MW; B27DBCE0CA39AA42 CRC64;
MYNSIYGSPF PKINPKVRYK TALERAGFDT KPRNPFSSQR NASTGSLQAS VKSPPITRQR
NVSAAPSVPV TMKSAYTASS KSAYSSVKGE SDIYPPPVLE NSERRSVTPP KNSNFTSSRP
SDISRSISRP SERASQEDPF RFERDLDRQA EQYAASRHTC KSPANKEFQA ADNFPFNFEQ
EDAGNTEREQ DLSPIERSFM MLTQNDTASV VNSMNQTDNR GVLDQKLGKE QQKEESSIEY
ESEGQQEDEN DIESLNFEPD PKLQMNLENE PLQDDFPEAK QEEKNTEPKI PEINVTRESN
TPSLTMNALD SKIYPDDNFS GLESSKEQKS PGVSSSSTKV EDLSLDGLNE KRLSITSSEN
VETPYTATNL QVEQLIAQLD DVSLSRNAKL DMNGNCLNAV DRKASRFKKS SAYLSGYPSM
DIPVTQQTSI VQNSNTNLSR QTILVDKGDV DEDAPSESTT NGGTPIFYKF KQSNVEYSNN
EGMGSQETFR TKLPTIEALQ LQHKRNITDL REEIDNSKSN DSHVLPNGGT TRYSSDADYK
ETEPIEFKYP PGEGPCRACG LEVTGKRMFS KKENELSGQW HRECFKCIEC GIKFNKHVPC
YILGDEPYCQ KHYHEENHSI CKVCSNFIEG ECLENDKVER FHVDCLNCFL CKTAITNDYY
IFNGEIPLCG NHDMEALLKE GIDNATSSND KNNTLSKRRT RLINFN
