STK10_CHICK
ID STK10_CHICK Reviewed; 969 AA.
AC F1NBT0;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Serine/threonine-protein kinase 10;
DE EC=2.7.11.1;
GN Name=STK10;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
CC -!- FUNCTION: May act as a polo kinase kinase by mediating phosphorylation
CC of PLK1. {ECO:0000250}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- PTM: Autophosphorylates. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; AADN02028926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02028927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02028928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02028929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02028930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02028931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02028932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02028933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02028934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F1NBT0; -.
DR SMR; F1NBT0; -.
DR STRING; 9031.ENSGALP00000004442; -.
DR PaxDb; F1NBT0; -.
DR PRIDE; F1NBT0; -.
DR Ensembl; ENSGALT00000004451; ENSGALP00000004442; ENSGALG00000002816.
DR VEuPathDB; HostDB:geneid_416204; -.
DR eggNOG; KOG0579; Eukaryota.
DR GeneTree; ENSGT00940000156818; -.
DR InParanoid; F1NBT0; -.
DR OMA; CHMLVEN; -.
DR OrthoDB; 851098at2759; -.
DR PRO; PR:F1NBT0; -.
DR Proteomes; UP000000539; Chromosome 13.
DR Bgee; ENSGALG00000002816; Expressed in granulocyte and 11 other tissues.
DR ExpressionAtlas; F1NBT0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:2000401; P:regulation of lymphocyte migration; ISS:UniProtKB.
DR CDD; cd06644; STKc_STK10; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR022165; PKK.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR042743; STK10_STKc.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF12474; PKK; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell membrane; Coiled coil; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..969
FT /note="Serine/threonine-protein kinase 10"
FT /id="PRO_0000414712"
FT DOMAIN 36..294
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 317..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 574..698
FT /evidence="ECO:0000255"
FT COILED 839..919
FT /evidence="ECO:0000255"
FT COMPBIAS 332..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 42..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 65
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 969 AA; 112504 MW; E6BCE5C577063A8E CRC64;
MAFANFRRIL RLSTFEKRRS KEYEHVRRDL DPGEVWEVVG ELGDGAFGKV YKAKNKETGA
LAAAKVIETK NEDELEDYMV EIEILATCDH PHIVKLLGAF YWEGKLWIMI EFCPGGAVDA
TMLELDRGLT EPQIQVICRQ MLEALHYLHS KKIIHRDLKA GNVLLTQDGD IKLADFGVSA
KNVKTLQKRD SFIGTPYWMA PEVVMCETMK DTPYDYKADI WSLGITLIEM AQIEPPHHEL
NPMRVLLKIA KSDPPTLSCP SKWSLEFRDF LKTALDKNPE TRPSAAQLLE HPFVSKVTSN
RALRELVAEA KAEVLEEIED SRDEAEDDDS SESASLPGKH KRDPSEVSQL SFDGDKPPDS
SSLKTTNGPV ATEKEMVNGQ SDKVLDERIS SDSDKLVNSH STKTLASSGP DEGKATPGKP
DIISLSGRRG SSAEGDKQPM PGSKERRSMV DRPESSHLEN FPEEKLANGS LDSSAVFPGS
RSKGDSDSGS TSASESMDLT ISLSADLSLN RESGSISLKD SRMHNKTLKR TRKFVVDGVE
VSVTTSKIIS EDEKKDEEMR FLRRQELREL RLLQKEEHRN QAQLNSKHQL QLDQMLRRFE
QEMTAKKKFY DTELENLERQ QKQQIEKMEQ DHSLRRREEA KRIRLEQERD HVKFMEQLKQ
KKKEVKNEVE KLPRQQRKEN MKVKMDDFAQ RKQTMEQDFL AKQKEDLELA MKNITAQNKK
EICDKERECL NKKQQLMRDR EACIWDLEER QQQEKHQLIK QQLKDQYFLQ RHELLRKHEK
EREQMQRYNQ RMIEQLKIRQ QQEKARLPKI QRSEGKTRMA MYKKSLHIHS SGSAAEQREK
IKQFSQQEEK RQKAERLHQQ QKHETQMKDM LAQCESNTNE LQQLQNEKCH LLIEHETQKL
KSLDENHNLH MKEWRDKLRP RKKALEDELN QKKREQEMFF KLSVEADEQT PASPVKHTKF
IPFSSTESS
