HUNKA_XENLA
ID HUNKA_XENLA Reviewed; 691 AA.
AC Q5XHI9; Q6VZ18;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Hormonally up-regulated neu tumor-associated kinase homolog A;
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase MAK-V A;
DE Short=xMAK-V A;
GN Name=hunk-a; Synonyms=makv-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAQ85059.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14740210; DOI=10.1007/s00427-004-0381-9;
RA Ruzov A.S., Mertsalov I.B., Meehan R., Kiselev S.L., Buchman V.L.,
RA Korobko I.V.;
RT "Cloning and developmental expression of MARK/Par-1/MELK-related protein
RT kinase xMAK-V in Xenopus laevis.";
RL Dev. Genes Evol. 214:139-143(2004).
RN [2] {ECO:0000312|EMBL:AAH84068.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAH84068.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000250|UniProtKB:P57058};
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; Evidence={ECO:0000250|UniProtKB:P57058};
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000255}.
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DR EMBL; AY318877; AAQ85059.1; -; mRNA.
DR EMBL; BC084068; AAH84068.1; -; mRNA.
DR RefSeq; NP_001084712.1; NM_001091243.1.
DR AlphaFoldDB; Q5XHI9; -.
DR SMR; Q5XHI9; -.
DR DNASU; 414676; -.
DR GeneID; 414676; -.
DR KEGG; xla:414676; -.
DR CTD; 414676; -.
DR Xenbase; XB-GENE-968421; hunk.L.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 414676; Expressed in gastrula and 11 other tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
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; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..691
FT /note="Hormonally up-regulated neu tumor-associated kinase
FT homolog A"
FT /id="PRO_0000347328"
FT DOMAIN 55..313
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 406..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00517,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 61..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00517,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00517,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 279
FT /note="P -> A (in Ref. 1; AAQ85059)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="A -> G (in Ref. 1; AAQ85059)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 691 AA; 78489 MW; C143FDD2974A3798 CRC64;
MPAAAGDGLS ESPSRFLAGE KPPVHLEETF LPACISNVSR ETLRNFQHTK RVGSYLIGRK
LGEGSFAKVR EGLHVVTGEK VAIKVIDKKK AKKDTYVTKN LRREGQIQQM IRHPNITQLL
DILETENSYY LVMELCPGGN LMHKIYEKKR LEEHEARKYI RQLILAVEHL HRAGVVHRDL
KIENLLLDEN NNIKLIDFGL SNCAGILGYS DPFSTQCGSP AYAAPELLAR KKYGPKVDVW
SIGVNMYAML TGTLPFTVEP FSLRALYQKM VDKDMNPLPT HLSPAAISFL RSLLEPDPLK
RPNIQQALAN RWLNDNYHGK GLHTYPNRIH LEDLSQSVVL HMSEKLGYKH SDVINVILSN
RACHTLAVYF LLNRKLEHYL VNMRKPDIND NVCHKNQFHQ LEKYKMNKNS YEERRSKDLE
KRGEPQQRPI QRKLDKCSPS HRQNACLTPQ GHSNKGPVKE RRSSKSERES FGGLSPFHEV
RITKTGCMTS CSLEYLEMQS PDPRTPKIMR RQDSHSQETV NVNMGSRIRE THLNVVRSFE
SVNREDQIES LSPNHQYRVI GSPVSFSPRH SSERTLSPIF QFDNTSPSKS HFNQASFTYD
DKSSPSSPES MSPTSPHSPS CNNNISGNLG SPNCVRSRGR FPMMGIGQML RKRNQVVSPK
GEKPLETRMP PLHQMSPGYA SFNSSDMNGF C
