HUNKB_XENLA
ID HUNKB_XENLA Reviewed; 626 AA.
AC Q6VZ17;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Hormonally up-regulated neu tumor-associated kinase homolog B;
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase MAK-V B;
DE Short=xMAK-V B;
DE Flags: Fragment;
GN Name=hunk-b; Synonyms=makv-b;
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:0000305, ECO:0000312|EMBL:AAQ85060.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
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 -!- TISSUE SPECIFICITY: In the egg, expressed predominantly in the animal
CC hemisphere. This pattern of expression persists throughout the cleavage
CC and blastula stages. At the gastrula stage, expression is restricted to
CC the ectoderm. In later-stage embryos, expressed over the entire
CC embryonic surface including the open neural plate at stage 15 and the
CC neural tube at stage 22. In tadpoles, strongly expressed in the neural
CC tube, motor neurons, brain regions and sensory organs (otic vesicle and
CC eye). Also expressed in the perisomitic mesoderm, brachial arches and
CC embryonic epidermis of tadpoles. {ECO:0000269|PubMed:14740210}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed throughout development. {ECO:0000269|PubMed:14740210}.
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; AY318878; AAQ85060.1; -; mRNA.
DR AlphaFoldDB; Q6VZ17; -.
DR SMR; Q6VZ17; -.
DR Proteomes; UP000186698; Genome assembly.
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; 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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN <1..626
FT /note="Hormonally up-regulated neu tumor-associated kinase
FT homolog B"
FT /id="PRO_0000347329"
FT DOMAIN <1..246
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 336..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 112
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P00517,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING <1..2
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00517,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P00517,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AAQ85060.1"
SQ SEQUENCE 626 AA; 71353 MW; E62B330CB85DBFCD CRC64;
KVREGLHVGT GEKVAVKVID KKKAKKDTYV TKNLRREGQI QQMIRHPNIT QLLDILETEN
SYYLVMELCP GGNLMHKIYE KKRLEEHEAR KYIRQLILAV EHLHRAGVVH RDLKIENLLL
DENNNIKLID FGLSNCAGIL GYSDPFSTQC GSPAYAAPEL LARKKYGPKV DVWSIGVNMY
AMLTGTLPFT VEPFSLRALY QKMVDKDMNP LPTHISPAAI SCLRSLLEPD PLKRPNIQQA
LANRWLNDNY HGKGHHTFPN RIHLEDLSQS VVLHMSEKLG YKHSDVINVI LSNRACHTLA
VYFLLNWKLE HYLVNMRKPD INDNVCHKNQ FHQSEKYKMN KNSYEERRSK DLEKRGEQQQ
QRAIPRKLEK CSPSHRQSTC LTPQGHSSSK GPIKERRSSK SERESFGGLS PFHEVRITKT
GCMNSCSLEY LEIQSPDPRT PKIMRRQDSH SQETVNVNMG SRIRETHLNV VRSFESVNRE
DQIESLSPNH QYRVLGSPMS FSPRHSSERT LSPIFHFDNT SPLKGHSNQA SFTYDDKSSP
SSPESMSPTS PHSPSCNNNI SGNLGSPNCV RSRGRFPMMG IGQMLRKRNQ VVSPKGEKPL
ETRMPPLHQM SPGYASFNSS DMNGFC
