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Database: UniProt
Entry: A0A2K5IU17_COLAP
LinkDB: A0A2K5IU17_COLAP
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ID   A0A2K5IU17_COLAP        Unreviewed;      1187 AA.
AC   A0A2K5IU17;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|RuleBase:RU362096};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000019967.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000019967.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001149,
CC         ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|RuleBase:RU362096};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. JAK subfamily. {ECO:0000256|PIRNR:PIRNR000636}.
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DR   RefSeq; XP_011810254.1; XM_011954864.1.
DR   AlphaFoldDB; A0A2K5IU17; -.
DR   STRING; 336983.ENSCANP00000019967; -.
DR   Ensembl; ENSCANT00000042933.1; ENSCANP00000019967.1; ENSCANG00000033397.1.
DR   GeneID; 105520874; -.
DR   KEGG; cang:105520874; -.
DR   CTD; 7297; -.
DR   OMA; QAKHEFV; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000233080; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-UniRule.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:UniProt.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0030155; P:regulation of cell adhesion; IEA:UniProt.
DR   GO; GO:0051239; P:regulation of multicellular organismal process; IEA:UniProt.
DR   CDD; cd05080; PTKc_Tyk2_rpt2; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR041155; FERM_F1.
DR   InterPro; IPR041046; FERM_F2.
DR   InterPro; IPR041381; JAK1-3/TYK2_PHL_dom.
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; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR016251; Tyr_kinase_non-rcpt_Jak/Tyk2.
DR   InterPro; IPR016045; Tyr_kinase_non-rcpt_TYK2_N.
DR   PANTHER; PTHR45807:SF6; NON-RECEPTOR TYROSINE-PROTEIN KINASE TYK2; 1.
DR   PANTHER; PTHR45807; TYROSINE-PROTEIN KINASE HOPSCOTCH; 1.
DR   Pfam; PF18379; FERM_F1; 1.
DR   Pfam; PF18377; FERM_F2; 1.
DR   Pfam; PF17887; Jak1_Phl; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR   PIRSF; PIRSF000636; TyrPK_Jak; 1.
DR   PRINTS; PR01823; JANUSKINASE.
DR   PRINTS; PR00109; TYRKINASE.
DR   PRINTS; PR01827; YKINASETYK2.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00219; TyrKc; 2.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR000636, ECO:0000256|PIRSR:PIRSR000636-
KW   2}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000636};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR000636,
KW   ECO:0000256|PIRSR:PIRSR000636-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000636};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137,
KW   ECO:0000256|PIRNR:PIRNR000636}.
FT   DOMAIN          26..431
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          589..875
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          897..1176
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          293..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..350
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1023
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-1"
FT   BINDING         903..911
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-2"
FT   BINDING         930
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000636-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1187 AA;  133552 MW;  C1574F268311B067 CRC64;
     MPLRHRGTTR GSKPVGDGAQ PMAAMGGLKV LLHWAGPGGG EPWVTFSESS LTAEEVCIHI
     AHKVGITPPC FNLFALFDAQ AQVWLPPNHI LEIPRDASLM LYFRMRFYFR NWHGMNPQEP
     AVYRCGPPGT EASSDQTAQG MQLLDPASFE YLFEQGKHEF VNDVASLWEL SSEEEIHHFK
     NESLGMAFLH LCHLALRRGV PLEEVAKKTS FKDCIPLSFR RQIRQHSALT RLRLRNVFRR
     FLQDFQPDRL SQQMVMVKYL ATLERLAPRF GTERVPVCHL RLLAQAEGEP CYIRDSGEAP
     TDPGPESAAG PPTHEVLVTG TGGIQWWPVQ EEVNKEEGSS GGSGRNPQAS LSGKKAKAHK
     AIGQPADRLR EPLWAYFCDF RDITHVVLKE RCVSIHRQDN KCLELSLPSR AAALSFVSLV
     DGYFRLTADS SHYLCHEVAP PRLVMSIQDG IHGPLLEPFV QAKLRPEDGL YLIHWSTSHP
     YRLILTVAQR SQAPDGTQSL RLRKFPIEQQ AGAFVLEGWG RSFPSIRELG AALQGCLLRA
     GDDCFSLRRC CLPQPGETSN LIIMRGARAS TRTLNLSQLS FHRVDQKEIT QLSHLGQGTR
     TNVYEGRLRV EGSGDPEEGK MDDEDPLVPG RDRGQELRVV LKVLDPSHHD IALAFYETAS
     LMSQVSHVHL AFVHGVCVRG PENIMVTEYV EHGPLDVWLR RERGHVPLAW KMVVAQQLAS
     ALSYLENKNL VHGNVCGRNI LLARLGLAEG TSPFIKLSDP GVGLGALSRE ERVERIPWMA
     PECLPGGPNS LSIAMDKWGF GATLLEICFD GEAPLQSRSS SEKEHFYQRQ HRLPEPSCPE
     LATLTSQCLT YEPTQRPSFR TILRDLTRLQ PHNLADVLIV NPDSSASDPT VFHKRYLKKI
     RDLGEGHFGK VSLYCYDPTN DGTGEMVAVK ALKADCGPQH RSGWKQEIEI LRTLYHEHIV
     KYKGCCEDQG EKSLQLVMEY VPLGSLRDYL PRHSVGLAQL LLFAQQICEG MAYLHAQRYI
     HRDLAARNVL LDNDKLVKIG DFGLAKAVPE GHEYYRVRED GDSPVFWYAP ECLKEYKFYY
     ASDVWSFGVT LYELLTHCDS SQSPPTKFLE LIGITQGQMT VLRLTEFLER GERLPRPNKC
     PCEVYHLMKN CWETEASFRP TFENLIPILK TVHEKYQGQA PSVFSVC
//
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