ID A0A2I0LJ08_COLLI Unreviewed; 920 AA.
AC A0A2I0LJ08;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=non-specific protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011903};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
DE Flags: Fragment;
GN Name=TYK2 {ECO:0000313|EMBL:PKK17407.1};
GN ORFNames=A306_00014497 {ECO:0000313|EMBL:PKK17407.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK17407.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK17407.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK17407.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PKK17407.1}.
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DR EMBL; AKCR02000326; PKK17407.1; -; Genomic_DNA.
DR RefSeq; XP_013226890.1; XM_013371436.1.
DR AlphaFoldDB; A0A2I0LJ08; -.
DR STRING; 8932.A0A2I0LJ08; -.
DR InParanoid; A0A2I0LJ08; -.
DR Proteomes; UP000053872; Unassembled WGS sequence.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 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 SMART; SM00295; B41; 1.
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 PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Kinase {ECO:0000313|EMBL:PKK17407.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000053872};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999};
KW Transferase {ECO:0000313|EMBL:PKK17407.1}.
FT DOMAIN 18..451
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 568..848
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 848..920
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 881
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 920
FT /evidence="ECO:0000313|EMBL:PKK17407.1"
SQ SEQUENCE 920 AA; 103124 MW; EAFB8792D5B56676 CRC64;
MSLCRRSGPR GRREAEGSGL RVRLLRDPDD DNDDDDGTLS AEEICVRLAR GLGITPLCCS
LFGLYDPQRG LWIPPNHRFH VTADTDVRLL FRMRSALSRL FTSFPPFLPH SRPFYPVPAL
FTSSVPALFY LPHAKAGRDF RLLVPSRFYF RNWHGLNEKE PAVPAERPRG GAVLDKSSFE
YLFEQGKYDF INDVAPLRDA QGEQELQRFK NECLGMAVLH LSHVALTRGL SLEDVARSYS
FKNCIPRSFR RQIQQNNYLT RFRLKNVFRR FVQHFQRHTV GAGRLTAQDV MYKYLATLEQ
LAPRFGAEVF PVLSLETSSE GERAQLGANG GHEPPKEPLV THELLVTGTS GIQWRPVPAE
SVEGFSQRGY FGGRSRSNEA EAKAPAEQRN EAKWAHFCDF REITHVVVKD NRVSVHRQDN
KCLELLLPSA PLALSLVSLL DGYFRLTADS SHYLCHEVAP PRLVMSILNG IHGPMQEQFA
LAKLRRAEPE DGLYVTRWSV LDFNRIILAV AKRSAQPREF PTLRQLLDAL KGCTLRSGHE
SFAVKRCCPP EPGEISDLLI VRKVKDDAKQ ILNLSQLSFH QIRAEYFSTE QNNNSREMHV
VLKVLDPSHR DIALAFFETA SLMSQVSHVH LAFVHGVCVR GSENIMVEEF VEHGPLDVLL
RKEKGRVSVG WKITVAKQLA SALSYLEDKN LVHGNVCAKN VLLARRGLED GAAPFAKLSD
PGVSFAVLSP EGTRSTGSPL SPRLSVCLSV LPAEGAFLRE AASNPPSHPV CLSVCPSSPQ
KERFYEKRHR LPEPSCRALA ALTSRERARG WGTAGNGHLS RFPDLVDVSS VKPEVPVSDP
TVFQKRYLKK IRELGEGHFG KVGLYCYDPG NDGTGEMVAV KSLKAGCSRQ LLSSWKREIE
ILKTLYHENI VKYKGCCSEQ
//
