GenomeNet

Database: UniProt
Entry: A0A2U3VSM0_ODORO
LinkDB: A0A2U3VSM0_ODORO
Original site: A0A2U3VSM0_ODORO 
ID   A0A2U3VSM0_ODORO        Unreviewed;      1058 AA.
AC   A0A2U3VSM0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Tyrosine-protein kinase {ECO:0000256|RuleBase:RU362096};
DE            EC=2.7.10.2 {ECO:0000256|RuleBase:RU362096};
GN   Name=ABL2 {ECO:0000313|RefSeq:XP_004398173.1};
OS   Odobenus rosmarus divergens (Pacific walrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC   Odobenus.
OX   NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004398173.1};
RN   [1] {ECO:0000313|RefSeq:XP_004398173.1}
RP   IDENTIFICATION.
RG   RefSeq;
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}.
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   RefSeq; XP_004398173.1; XM_004398116.2.
DR   AlphaFoldDB; A0A2U3VSM0; -.
DR   GeneID; 101370104; -.
DR   CTD; 27; -.
DR   OrthoDB; 1614410at2759; -.
DR   Proteomes; UP000245340; Unplaced.
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:SF87; TYROSINE-PROTEIN KINASE ABL2; 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:UP000245340};
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          86..146
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          152..242
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          267..518
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          633..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          685..772
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          840..920
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..702
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        704..728
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..856
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        877..891
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         296
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1058 AA;  115524 MW;  6E43B1865132CC93 CRC64;
     MGQQVGRVGE APGLQQPQPR GIRVSSAARP SGRRRDLAGR TTEAGFNVFT QHEALHRPYG
     CDVEPQALNE AIRWSSKENL LGATESDPNL FVALYDFVAS GDNTLSITKG EKLRVLGYNQ
     NGEWSEVRSK NGQGWVPSNY ITPVNSLEKH SWYHGPVSRS AAEYLLSSLI NGSFLVRESE
     SSPGQLSISL RYEGRVYHYR INTTTDGKVY VTAESRFSTL AELVHHHSTV ADGLVTTLHY
     PAPKCNKPTV YGVSPIHDKW EMERTDITMK HKLGGGQYGE VYVGVWKKYS LTVAVKTLKE
     DTMEVEEFLK EAAVMKEIKH PNLVQLLGVC TLEPPFYIVT EYMPYGNLLD YLRECSREEV
     TAVVLLYMAT QISSAMEYLE KKNFIHRDLA ARNCLVGENH VVKVADFGLS RLMTGDTYTA
     HAGAKFPIKW TAPESLAYNT FSIKSDVWAF GVLLWEIATY GMSPYPGIDL SQVYDLLEKG
     YRMEQPEGCP PKVYELMRAC WKWSPADRPS FAETHQAFET MFHDSSISEE VAEELGRAAA
     ASSVVPYLPR LPVLPSKTRT LKKQGENKEN IEGAQDATEN SASSSAPGFL RGAQAPSGSP
     ALPRKQRDKS PSSLLEDAKE TCFTRDRKGG FFSSFMKKRN APTPPKRSSS FREMENQPHK
     KYELTGLPEQ DRMAMTLPRN CQRSKLQLER TVSTSSQPEE NVDRANDMLP KKSEEGAAPS
     RERPKAKLLP RGATALPLRT PSGDPAITEK DSPGAGVAGV AAAPKSKERN GGARLGMAGV
     PEDGEQTGWS SPAKAAAALP TTHNHKVPVL ISPTLKHTPA DVQLIGTDSQ GNKFKLLSEH
     QVTSSGDKDR PRRVKPKCAP PPPPVMKLLQ HPSMCADPTE EPTTPTAGQP MAETQEGGKK
     AAPGAVPGGG KAGRPVMPPP QVPLPTSSIS PAKMANGTAG TKVALRKTKQ AAEKISADKI
     SKEALLECAD LLSSAITEPV PNSQLVDTGH QLLDYCSGYV DCIPQTRNKF AFREAVSKLE
     LSLQELQVSS AAAGVPGANP VLNNLLSCVQ EISDVVQR
//
DBGET integrated database retrieval system