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   27-MAR-2024, entry version 194.
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).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=33060204; DOI=10.1074/jbc.ra120.014794;
RA   Jain B.K., Roland B.P., Graham T.R.;
RT   "Exofacial membrane composition and lipid metabolism regulates plasma
RT   membrane P4-ATPase substrate specificity.";
RL   J. Biol. Chem. 295:17997-18009(2020).
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   -!- DISRUPTION PHENOTYPE: Simultaneous knockout of FPK1 leads to decreased
CC       phosphatidylcholine and glucosylceramide transport into the cell.
CC       {ECO:0000269|PubMed:33060204}.
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; 152.
DR   DIP; DIP-6460N; -.
DR   IntAct; P25341; 10.
DR   MINT; P25341; -.
DR   STRING; 4932.YCR091W; -.
DR   iPTMnet; P25341; -.
DR   MaxQB; P25341; -.
DR   PaxDb; 4932-YCR091W; -.
DR   PeptideAtlas; P25341; -.
DR   EnsemblFungi; YCR091W_mRNA; YCR091W; YCR091W.
DR   GeneID; 850453; -.
DR   KEGG; sce:YCR091W; -.
DR   AGR; SGD:S000000687; -.
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   OrthoDB; 10768at2759; -.
DR   BioCyc; YEAST:G3O-29385-MONOMER; -.
DR   BioGRID-ORCS; 850453; 1 hit in 13 CRISPR screens.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0000749; P:response to pheromone triggering conjugation with cellular fusion; IMP:SGD.
DR   CDD; cd05574; STKc_phototropin_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR45637; FLIPPASE KINASE 1-RELATED; 1.
DR   PANTHER; PTHR45637:SF22; FLIPPASE KINASE 1-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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
//