ID A0A452QVJ4_URSAM Unreviewed; 1134 AA.
AC A0A452QVJ4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN Name=ABL1 {ECO:0000313|Ensembl:ENSUAMP00000009708.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000009708.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000009708.1}
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|RuleBase:RU362096};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000256|RuleBase:RU362096}.
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DR AlphaFoldDB; A0A452QVJ4; -.
DR Ensembl; ENSUAMT00000010929.1; ENSUAMP00000009708.1; ENSUAMG00000008042.1.
DR GeneTree; ENSGT00940000153838; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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: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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW 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 64..124
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 130..220
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 245..496
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 524..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 873..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1134 AA; 123386 MW; 012DF3ACDA6D077B CRC64;
IYSVNMKPVK CRTNFFPNSS CFLFPLCLPE ALQRPVASDF ETQGLSEAAR WNSKENLLAG
PSENDPNLFV ALYDFVASGD NTLSITKGEK LRVLGYNHNG EWCEAQTKNG QGWVPSNYIT
PVNSLEKHSW YHGPVSRNAA EYLLSSGING SFLVRESESS PGQRSISLRY EGRVYHYRIN
TASDGKLYVS SESRFNTLAE LVHHHSTVAD GLITTLHYPA PKRNKPTVYG VSPNYDKWEM
ERTDITMKHK LGGGQYGEVY EGVWKKYSLT VAVKTLKEDT MEVEEFLKEA AVMKEIKHPN
LVQLLGVCTR EPPFYIITEF MTYGNLLDYL RECNRQEVNA VVLLYMATQI SSAMEYLEKK
NFIHRDLAAR NCLVGENHLV KVADFGLSRL MTGDTYTAHA GAKFPIKWTA PESLAYNKFS
IKSDVWAFGV LLWEIATYGM SPYPGIDLSQ VYELLEKDYR MERPEGCPEK VYELMRACWQ
WNPSDRPSFA EIHQAFETMF QESSISDEVE KELGKKGVRG VASTLLQAPE LPTKTRTSRR
AVEHKDPTDV PETPHSKGPG ETDPLDHEPP VSPLLPRKER GPQDGGLNED ERLLPKDKKT
NLFSALIKKK KKTAPTPPKR SSSFREMDGQ PERKAASEEE GRETSNGGPA LTPSDTTEPA
KSPKPSSGAG VPNGAFRETG GAGFRSPHLW KKSSTLTSSR LAASEEESGS SSSKRFLRSC
SASCVPHGAR DTEWRSVTLP RDLQSTGRQF DSSTFGGHKS EKPALPRKRA SENRSDQVTR
GTVTPPPRLV KKTEDAVDEV FRDTGESSPG SSPPSLTPKL LRRQVAGTPS SGLPHKDEAG
KSGALGTPAT AEPVPPASRA GPGASGGASK ASTEEPRARR HKPSSESPGR DKAKLSKLKP
VPPPPPPASV GKAGKPSQNL SQEAAGEAGT GGKAKATAVV GDAVNSDTIK PGPLGEGVKK
PVLPSMPKPQ SSSKPAGTPT SPAPTPSTVP SASSALAGDQ PASTAFIPLI STRVSLRKTR
QPPERIASGT ITKGVVLDGT EALCLAISKN SEQMASHSAV LEAGKNLCTF CVSYVDSIQQ
MRNKFAFREA INKLENNLRE LQICPATAGS GPAATQDFSK LLSSVKEISD IVQR
//