HTK16_HYDVU
ID HTK16_HYDVU Reviewed; 757 AA.
AC P53356;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Tyrosine-protein kinase HTK16;
DE EC=2.7.10.2;
GN Name=HTK16;
OS Hydra vulgaris (Hydra) (Hydra attenuata).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Aplanulata; Hydridae; Hydra.
OX NCBI_TaxID=6087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Irvine;
RX PubMed=8134129;
RA Chan T.A., Chu C.A., Rauen K.A., Kroiher M., Tatarewicz S.M., Steele R.E.;
RT "Identification of a gene encoding a novel protein-tyrosine kinase
RT containing SH2 domains and ankyrin-like repeats.";
RL Oncogene 9:1253-1259(1994).
CC -!- FUNCTION: May be involved in signal transduction.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- TISSUE SPECIFICITY: Epithelial cells.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U00936; AAC27350.1; -; mRNA.
DR RefSeq; NP_001296681.1; NM_001309752.1.
DR AlphaFoldDB; P53356; -.
DR SMR; P53356; -.
DR PRIDE; P53356; -.
DR GeneID; 100200602; -.
DR KEGG; hmg:100200602; -.
DR OrthoDB; 796831at2759; -.
DR BRENDA; 2.7.10.2; 2720.
DR Proteomes; UP000694840; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR CDD; cd10347; SH2_Nterm_shark_like; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035061; Shark-like_SH2_N.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 2.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF55550; SSF55550; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 2.
PE 2: Evidence at transcript level;
KW ANK repeat; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; SH2 domain; Transferase;
KW Tyrosine-protein kinase.
FT CHAIN 1..757
FT /note="Tyrosine-protein kinase HTK16"
FT /id="PRO_0000088105"
FT DOMAIN 10..102
FT /note="SH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REPEAT 115..147
FT /note="ANK 1"
FT REPEAT 151..180
FT /note="ANK 2"
FT REPEAT 184..214
FT /note="ANK 3"
FT REPEAT 219..248
FT /note="ANK 4"
FT REPEAT 252..281
FT /note="ANK 5"
FT DOMAIN 287..379
FT /note="SH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 484..740
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 381..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 608
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 490..498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 746
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 757 AA; 85598 MW; 144D09E9109D794F CRC64;
MSKNSDALLW YHGKITREVA VQVLLRKGGR DGFFLIRDCG NAPEDYVLSM MFRSQILHFQ
INCLGDNKFS IDNGPIFQGL DMLISYYKVI SDGLPCKLVD FCVGKIAPLY ALKYGLDTRL
HLACEEKNPN TVKELLQDSV IKENVNARSI SGLTALHISC SNGDNDIVAM LLNAGADASA
IDANGRTPVQ VVCFYNHAST LHLLISKGSA DFLKRSPNNG WVPLHEAAMR GSLECVKVLL
SFNASMYPRS LDGDTPRDLA LQYENYNVVE FFDNYPVNQP KTSITQWLHQ NLDRNGALII
LQNASMADGS FLIRSSIKCH GYYVLTLVYE KKTYHFQIKS RADRWFYIDD GPLFETLPHL
VDHYMQYADG LPTLLQFPVP SAENRKRPLP PTPTKNQLKL PVPPSRPIKN NNGLPQPLPY
PEFTNESDSD IFTRLECEKE KPLPKLPRPV VNHTEVPNSV NVGQKGDQTM KNNAQQNIIL
KESISFGKEL GVGEFGSVIK GIWLSPGGKE INVAMKTLHK DKMVQGEKEF LREALVMSQL
NHPCIVSLLG VCLGPPMILV QELVEMGALL DYLMDYQPEI QEVDLKLWAS QIAFGMMYLE
LKRFVHRDLA ARNILLANKK QVKISDFGLS RAVGTGSDYY QAKQGGRWPV RWYAPESINY
GTFSTKSDVW SYGITLWEMF TFGDLPYGEM TGNEVVSFLE HCGRLEKPDE CPIHTYSIML
SCWHIDPNKR PTFNELHSTF STDPEYEDVR IYRDRIK
