HUNK_XENTR
ID HUNK_XENTR Reviewed; 697 AA.
AC B1WAS2;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Hormonally up-regulated neu tumor-associated kinase homolog;
DE EC=2.7.11.1;
DE AltName: Full=Serine/threonine-protein kinase MAK-V {ECO:0000250|UniProtKB:Q5XHI9};
GN Name=hunk; Synonyms=makv;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAI61479.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAI61479.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2008) 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; BC161479; AAI61479.1; -; mRNA.
DR RefSeq; NP_001120549.1; NM_001127077.1.
DR AlphaFoldDB; B1WAS2; -.
DR SMR; B1WAS2; -.
DR STRING; 8364.ENSXETP00000002771; -.
DR PaxDb; B1WAS2; -.
DR GeneID; 100145703; -.
DR KEGG; xtr:100145703; -.
DR CTD; 30811; -.
DR Xenbase; XB-GENE-968418; hunk.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_017161_0_0_1; -.
DR InParanoid; B1WAS2; -.
DR OrthoDB; 1127668at2759; -.
DR Proteomes; UP000008143; Chromosome 2.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000007352; Expressed in gastrula and 12 other tissues.
DR ExpressionAtlas; B1WAS2; baseline.
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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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..697
FT /note="Hormonally up-regulated neu tumor-associated kinase
FT homolog"
FT /id="PRO_0000347330"
FT DOMAIN 55..313
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 405..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..639
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"
SQ SEQUENCE 697 AA; 79008 MW; 5AA3456B0095A5FE CRC64;
MPAAAGDGLG ESPSRFLAGE KPPVQLAESF LPACVSSVSR ETLRTFQHTK RVGSYLIGRK
LGEGSFAKVR EGLHVGTGEK VAIKVIDKKK AKKDTYVTKN LRREGQIQQM IRHPNITQLL
DILETENSYY LVMELCTGGN LMHKIYERKR IEEHEARKYI RQLILAVEHL HRAGVVHRDL
KIENLLLDEN NNIKLIDFGL SNCAGILGYT DPFSTQCGSP AYAAPELLAR KKYGPKVDVW
SIGVNMYAML TGTLPFTVEP FSLRALYQKM VDKDMNPLPT HLSPAAISFL RSLLEPDPLK
RPNIQQALAN RWLNDNYHGK GLHTYPNRIH LEDLSQSVVL HMSEKLGYKH SDVINVILSN
RACHTLAVYF LLNRKLENYL LNMRKPDIND NVCHKNQFHQ LEKYKMNKNS YEERRSKDLE
KRGEQQQQQQ RAMQRKLEKC SPSHRQSNCL TPQGHISKGP VKERRSSKSE RESFGGLSPF
HEVRITKPGC MTSCSLEYLE MQSPDPRTPK IMRRQDSHSQ ETVNVNMGSR IRETHLNVVR
SFESVNREDQ IESLSPNHQY RVLGSPVSFS PRHSSERILS PIFQFDNTSP IKGHSNQASF
TYDDKSSPSS PESMSPTSPH SPHSPSCNNN ISGNLGSPNC VRSRGRFPMM GIGQMLRKRN
QVVSPKAEKP LETRMPALHQ MSPGYASFNS SDMNGFC
