KIN82_YEAST
ID KIN82_YEAST Reviewed; 720 AA.
AC P25341; D6VR91;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Serine/threonine-protein kinase KIN82;
DE EC=2.7.11.1;
DE AltName: Full=Flippase kinase 2;
GN Name=KIN82; Synonyms=FPK2; OrderedLocusNames=YCR091W;
GN ORFNames=YCR1153, YCR91W;
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=1580103; DOI=10.1002/yea.320080108;
RA Wilson C., Bergantino E., Lanfranchi G., Valle G., Carignani G.,
RA Frontali L.;
RT "A putative serine/threonine protein kinase gene on chromosome III of
RT Saccharomyces cerevisiae.";
RL Yeast 8:71-77(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
RN [3]
RP SEQUENCE REVISION TO 341 AND C-TERMINUS.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 341.
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 [5]
RP FUNCTION.
RX PubMed=18199685; DOI=10.1091/mbc.e07-07-0646;
RA Nakano K., Yamamoto T., Kishimoto T., Noji T., Tanaka K.;
RT "Protein kinases Fpk1p and Fpk2p are novel regulators of phospholipid
RT asymmetry.";
RL Mol. Biol. Cell 19:1783-1797(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, 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: Flippase activator that phosphorylates DFN1 and DFN2 and
CC which is involved in the generation of phospholipid asymmetry in
CC membranes by the inward translocation of phospholipids.
CC {ECO:0000269|PubMed:18199685}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. KIN82 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; X59720; CAA42256.2; -; Genomic_DNA.
DR EMBL; BK006937; DAA07560.2; -; Genomic_DNA.
DR PIR; S22258; S22258.
DR RefSeq; NP_010015.3; NM_001178797.2.
DR AlphaFoldDB; P25341; -.
DR SMR; P25341; -.
DR BioGRID; 31063; 150.
DR DIP; DIP-6460N; -.
DR IntAct; P25341; 10.
DR MINT; P25341; -.
DR STRING; 4932.YCR091W; -.
DR iPTMnet; P25341; -.
DR MaxQB; P25341; -.
DR PaxDb; P25341; -.
DR PRIDE; P25341; -.
DR EnsemblFungi; YCR091W_mRNA; YCR091W; YCR091W.
DR GeneID; 850453; -.
DR KEGG; sce:YCR091W; -.
DR SGD; S000000687; KIN82.
DR VEuPathDB; FungiDB:YCR091W; -.
DR eggNOG; KOG0610; Eukaryota.
DR GeneTree; ENSGT00940000175956; -.
DR HOGENOM; CLU_000288_84_2_1; -.
DR InParanoid; P25341; -.
DR OMA; IPNEAIC; -.
DR BioCyc; YEAST:G3O-29385-MON; -.
DR PRO; PR:P25341; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25341; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; HDA:SGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0045332; P:phospholipid translocation; IGI:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IGI:SGD.
DR GO; GO:0000749; P:response to pheromone triggering conjugation with cellular fusion; IMP:SGD.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Lipid transport; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transport.
FT CHAIN 1..720
FT /note="Serine/threonine-protein kinase KIN82"
FT /id="PRO_0000086136"
FT DOMAIN 324..602
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 449
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 330..338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 353
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 341
FT /note="V -> M (in Ref. 1; no nucleotide entry and 2;
FT CAA42256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 81462 MW; FBE3C038C18605E0 CRC64;
MTQQEYRSPS QRLSKGRSMS LPKIFARNLR SLQNNAPPGK NINVNCLNVN SCSLSASPSS
QINMACNGNK QDLPIPFPLH VECNDSWSSS KLNKFKSMFN HNRSKSSGTT DASTSEKGTH
KREPRSTIHT ELLQSSIIGE PNVHSTTSST LIPNEAICST PNEISGSSSP DAELFTFDMP
TDPSSFHTPS SPSYIAKDSR NLSNGSLNDI NENEELQNFH RKISENGSAS PLANLSLSNS
PIDSPRKNSE TRKDQIPMNI TPRLRRAASE PFNTAKDGLM REDYIALKQP PSLGDIVEPR
RSRRLRTKSF GNKFQDITVE PQSFEKIRLL GQGDVGKVYL VRERDTNQIF ALKVLNKHEM
IKRKKIKRVL TEQEILATSD HPFIVTLYHS FQTKDYLYLC MEYCMGGEFF RALQTRKSKC
IAEEDAKFYA SEVVAALEYL HLLGFIYRDL KPENILLHQS GHVMLSDFDL SIQATGSKKP
TMKDSTYLDT KICSDGFRTN SFVGTEEYLA PEVIRGNGHT AAVDWWTLGI LIYEMLFGCT
PFKGDNSNET FSNILTKDVK FPHDKEVSKN CKDLIKKLLN KNEAKRLGSK SGAADIKRHP
FFKKVQWSFL RNQDPPLIPA LNDNGCELPF ILSCNKHPKR NSVSEQETKM FCEKVANDDE
IDEADPFHDF NSMSLTKKDH NILTYSENYT YGKILYKATC TRPRHNSSHR SFFKDIIPEL
