ID Q2PYT3_RAT Unreviewed; 1144 AA. AC Q2PYT3; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 27-MAR-2024, entry version 126. DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096}; DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096}; DE Flags: Fragment; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:ABC46643.1}; RN [1] {ECO:0000313|EMBL:ABC46643.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sprague-Dawley {ECO:0000313|EMBL:ABC46643.1}; RA Li Q.F., Tang D.D.; RT "Rattus norvegicus Abl Abelson murine leukemia variant 1 mRNA."; RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABC46643.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Sprague-Dawley {ECO:0000313|EMBL:ABC46643.1}; RX PubMed=20610769; DOI=10.1152/ajpcell.00095.2010; RA Jia L., Tang D.D.; RT "Abl activation regulates the dissociation of CAS from cytoskeletal RT vimentin by modulating CAS phosphorylation in smooth muscle."; RL Am. J. Physiol. Cell Physiol. 299:C630-C637(2010). 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|RuleBase:RU362096}; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein CC kinase family. {ECO:0000256|RuleBase:RU362096}. 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; DQ294402; ABC46643.1; -; mRNA. DR AlphaFoldDB; Q2PYT3; -. DR GO; GO:0005737; C:cytoplasm; 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:0007154; P:cell communication; IEA:UniProt. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0051128; P:regulation of cellular component organization; IEA:UniProt. DR GO; GO:0023052; P:signaling; IEA:UniProt. DR CDD; cd05052; PTKc_Abl; 1. DR CDD; cd09935; SH2_ABL; 1. DR CDD; cd11850; SH3_Abl; 1. DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR035837; ABL_SH2. DR InterPro; IPR015015; F-actin-binding. 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; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR008266; Tyr_kinase_AS. DR InterPro; IPR020635; Tyr_kinase_cat_dom. DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1. DR PANTHER; PTHR24418:SF438; TYROSINE-PROTEIN KINASE ABL1; 1. DR Pfam; PF08919; F_actin_bind; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00401; SH2DOMAIN. DR PRINTS; PR00109; TYRKINASE. DR SMART; SM00808; FABD; 1. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 1. DR SMART; SM00219; TyrKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR SUPFAM; SSF50044; SH3-domain; 1. 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; 1. DR PROSITE; PS50002; SH3; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141, KW ECO:0000256|RuleBase:RU362096}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362096}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191}; KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE- KW ProRule:PRU00192}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362096}; KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137, KW ECO:0000256|RuleBase:RU362096}. FT DOMAIN 80..140 FT /note="SH3" FT /evidence="ECO:0000259|PROSITE:PS50002" FT DOMAIN 146..236 FT /note="SH2" FT /evidence="ECO:0000259|PROSITE:PS50001" FT DOMAIN 261..512 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 531..704 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 741..1011 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 552..568 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 599..621 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 642..658 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 777..791 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 883..908 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 943..957 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 978..999 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 290 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" FT NON_TER 1144 FT /evidence="ECO:0000313|EMBL:ABC46643.1" SQ SEQUENCE 1144 AA; 124736 MW; 212B1DEA4BBEB83B CRC64; MGQQPGKVLG DQRRPSLPAL HFIKGAGKRD SSRHGGPHCN VFVEHEALQR PVASDFEPQG LSEAARWNSK ENLLAGPSEN DPNLFVALYD FVASGDNTLS ITKGEKLRVL GYNHNGEWCE AQTKNGQGWV PSNYITPVNS LEKHSWYHGP VSRNAAEYLL SSGINGSFLV RESESSPGQR SISLRYEGRV YHYRINTASD GKLYVSSESR FNTLAELVHH HSIVADGLIT TLHYPAPKRN KPTIYGVSPN YDKWEMERTD ITMKHKLGGG QYGEVYEGVW KKYSLTVAVK TLKEDTMEVE EFLKEAAVMK EIKHPNLVQL LGVCTREPPF YIITEFMTYG NLLDYLRECN RQEVSAVVLL YMATQISSAM EYLEKKNFIH RDLAARNCLV GENHLVKVAD FGLSRLMTGD TYTAHAGAKF PIKWTAPESL AYNKFSIKSD VWAFGVLLWE IATYGMSPYP GIDLSQVYEL LEKDYRMERP EGCPEKVYEL MRACWQWNPS DRPSFAEIHQ AFETMFQESS ISDEVEKELG KRGMRGAAGS TLQAPELPTK TRTCRKTAEQ KDAPDALELL HTKGLGESDA ALDSEPAVSP LLPRKERGPP DGSLNEDERL LPKDKKTNLF SALIKKKKKM APTPPKRSSS FREMDGQSER RGASEDDGRE ISNGPPALTS DAVEPTKSPK ASNGAGVPNG AFREPGNSGF RSPHVWKKCS TLTSSRLAAA EEESGLSSSK RFLRSCSASC MPHGVRDTEW RSVTLPRDLP SAGKQFDSST FGGHKSEKPA LPRKRTSESR SEQVAKSTAT PPPRLVKKTE EAAEDVFKDT ESSPGSSPPS LTPKLLRRQV PASPSSGPSH KDEATKGNAS GMGTPATAEP AAPSNKAGLS KASSEEPRAR RHKHSSESPG RDKGRLSKLK PAPPPPPSST GKAGKPAQSP SQDVAGEAGG ATKTKCTSLS VDAVNSDPTK AGQPGEGLRK SVPPSVPKPQ SATKPPGTPT SPVSTPSTAP APSPLAGDQQ PSSAAFIPLI STRVSLRKTR QPPERIASGT ITKGVVLDST EALCLAISRN SEQMASHSAV LEAGKNLYTF CVSYVDSIQQ MRNKFAFREA INKLESNLRE LQICPATASS GPAATQDFSK LLSSVKEISD IVRR //