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 08-NOV-2023, entry version 124. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U00936; AAC27350.1; -; mRNA. DR RefSeq; NP_001296681.1; NM_001309752.1. DR AlphaFoldDB; P53356; -. DR SMR; P53356; -. DR EnsemblMetazoa; NM_001309752.1; NP_001296681.1; LOC100200602. DR GeneID; 100200602; -. DR KEGG; hmg:100200602; -. DR OrthoDB; 1614410at2759; -. 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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd05060; PTKc_Syk_like; 1. DR CDD; cd10348; SH2_Cterm_shark_like; 1. DR CDD; cd10347; SH2_Nterm_shark_like; 1. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1. DR Gene3D; 3.30.505.10; SH2 domain; 2. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1. DR PANTHER; PTHR24418:SF372; TYROSINE-PROTEIN KINASE SHARK; 1. 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; Ankyrin repeat; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF55550; SH2 domain; 2. 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 //