ABL1_CAEEL
ID ABL1_CAEEL Reviewed; 1224 AA.
AC P03949; Q9U3A2; Q9U3A3;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 4.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Tyrosine-protein kinase abl-1;
DE EC=2.7.10.2;
GN Name=abl-1; ORFNames=M79.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-706.
RX PubMed=3457381; DOI=10.1073/pnas.83.7.2172;
RA Goddard J.M., Weiland J.J., Capecchi M.R.;
RT "Isolation and characterization of Caenorhabditis elegans DNA sequences
RT homologous to the v-abl oncogene.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2172-2176(1986).
RN [3]
RP FUNCTION.
RX PubMed=16729024; DOI=10.1038/sj.cdd.4401976;
RA Salinas L.S., Maldonado E., Navarro R.E.;
RT "Stress-induced germ cell apoptosis by a p53 independent pathway in
RT Caenorhabditis elegans.";
RL Cell Death Differ. 13:2129-2139(2006).
RN [4]
RP FUNCTION, INTERACTION WITH MIG-13 AND SOEM-1, AND SUBCELLULAR LOCATION.
RX PubMed=27780040; DOI=10.1016/j.devcel.2016.09.029;
RA Zhu Z., Chai Y., Jiang Y., Li W., Hu H., Li W., Wu J.W., Wang Z.X.,
RA Huang S., Ou G.;
RT "Functional coordination of WAVE and WASP in C. elegans neuroblast
RT migration.";
RL Dev. Cell 39:224-238(2016).
CC -!- FUNCTION: Functions downstream of migratory protein mig-13 and is
CC involved in Q neuroblast migration during larval development
CC (PubMed:27780040). Recruited by mig-13 to the leading edge of Q
CC neuroblasts and their descendents to signal downstream, likely to the
CC wve-1 pathway, and direct migration along the anteroposterior body axis
CC (PubMed:27780040). Promotes germline cell apoptosis in response to
CC oxidative, osmotic and heat shock stresses (PubMed:16729024).
CC {ECO:0000269|PubMed:16729024, ECO:0000269|PubMed:27780040}.
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:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Interacts (via SH2 and SH3 domains) with mig-13; the
CC interaction is direct. May interact with soem-1.
CC {ECO:0000269|PubMed:27780040}.
CC -!- INTERACTION:
CC P03949; G5EEL1: alp-1; NbExp=4; IntAct=EBI-2315883, EBI-2315902;
CC P03949; Q11181: C05D10.4; NbExp=6; IntAct=EBI-2315883, EBI-2316016;
CC P03949; G5ED33: eps-8; NbExp=6; IntAct=EBI-2315883, EBI-2315916;
CC P03949; Q9TYX9: M57.1; NbExp=4; IntAct=EBI-2315883, EBI-2315745;
CC P03949; Q22227: mig-5; NbExp=3; IntAct=EBI-2315883, EBI-316403;
CC P03949; Q95QA6: pat-12; NbExp=3; IntAct=EBI-2315883, EBI-327642;
CC P03949; Q18953: secs-1; NbExp=7; IntAct=EBI-2315883, EBI-318539;
CC P03949; G5EF87: swsn-1; NbExp=5; IntAct=EBI-2315883, EBI-311928;
CC P03949; Q18320: szy-4; NbExp=3; IntAct=EBI-2315883, EBI-327120;
CC P03949; G5EDS1: vab-3; NbExp=4; IntAct=EBI-2315883, EBI-319610;
CC P03949; O02174: zfp-3; NbExp=5; IntAct=EBI-2315883, EBI-2315779;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27780040}.
CC Cytoplasm {ECO:0000269|PubMed:27780040}. Note=Enriched at the leading
CC edge compared to cytoplasm. Targeted to the leading edge of Q
CC neuroblasts by mig-13. {ECO:0000269|PubMed:27780040}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=a;
CC IsoId=P03949-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P03949-2; Sequence=VSP_004963;
CC Name=c;
CC IsoId=P03949-3; Sequence=VSP_004962;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. ABL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; Z50806; CAA90691.2; -; Genomic_DNA.
DR EMBL; Z50806; CAB60296.2; -; Genomic_DNA.
DR EMBL; Z50806; CAB60297.2; -; Genomic_DNA.
DR EMBL; M13235; AAA28129.1; -; Genomic_DNA.
DR PIR; T23832; T23832.
DR RefSeq; NP_509777.2; NM_077376.6. [P03949-2]
DR RefSeq; NP_509778.2; NM_077377.4. [P03949-1]
DR RefSeq; NP_509779.2; NM_077378.2. [P03949-3]
DR AlphaFoldDB; P03949; -.
DR SMR; P03949; -.
DR BioGRID; 46173; 49.
DR DIP; DIP-48409N; -.
DR IntAct; P03949; 45.
DR STRING; 6239.M79.1a; -.
DR iPTMnet; P03949; -.
DR EPD; P03949; -.
DR PaxDb; P03949; -.
DR PRIDE; P03949; -.
DR EnsemblMetazoa; M79.1a.1; M79.1a.1; WBGene00000018. [P03949-1]
DR EnsemblMetazoa; M79.1b.1; M79.1b.1; WBGene00000018. [P03949-2]
DR EnsemblMetazoa; M79.1c.1; M79.1c.1; WBGene00000018. [P03949-3]
DR GeneID; 181261; -.
DR UCSC; M79.1b; c. elegans. [P03949-1]
DR CTD; 181261; -.
DR WormBase; M79.1a; CE31570; WBGene00000018; abl-1. [P03949-1]
DR WormBase; M79.1b; CE31571; WBGene00000018; abl-1. [P03949-2]
DR WormBase; M79.1c; CE31572; WBGene00000018; abl-1. [P03949-3]
DR eggNOG; KOG4278; Eukaryota.
DR GeneTree; ENSGT00940000173757; -.
DR InParanoid; P03949; -.
DR OMA; ATYGMAP; -.
DR OrthoDB; 539311at2759; -.
DR BRENDA; 2.7.10.2; 1045.
DR Reactome; R-CEL-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-CEL-525793; Myogenesis.
DR Reactome; R-CEL-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-CEL-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-CEL-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR SignaLink; P03949; -.
DR PRO; PR:P03949; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00000018; Expressed in pharyngeal muscle cell (C elegans) and 9 other tissues.
DR ExpressionAtlas; P03949; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:WormBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISS:WormBase.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0050832; P:defense response to fungus; IMP:WormBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IGI:WormBase.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; IGI:WormBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:WormBase.
DR GO; GO:0030336; P:negative regulation of cell migration; IGI:WormBase.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:WormBase.
DR GO; GO:1901075; P:negative regulation of engulfment of apoptotic cell; IGI:WormBase.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:WormBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:WormBase.
DR CDD; cd09935; SH2_ABL; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR033221; ABL1.
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:SF162; PTHR24418:SF162; 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; PR00452; SH3DOMAIN.
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; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cytoplasm; Kinase;
KW Membrane; Nucleotide-binding; Reference proteome; SH2 domain; SH3 domain;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..1224
FT /note="Tyrosine-protein kinase abl-1"
FT /id="PRO_0000088055"
FT DOMAIN 115..188
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 194..284
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 311..562
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 579..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 450..474
FT /note="Kinase activation loop"
FT /evidence="ECO:0000250"
FT COMPBIAS 579..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..775
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..831
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..999
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 432
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 317..325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 340
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 385..391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..88
FT /note="MGHSHSTGKEINDNELFTCEDPVFDQPVASPKSEISSKLAEEIERSKSPLIL
FT EVSPRTPDSVQMFRPTFDTFRPPNSDSSTFRGSQSR -> MIMNPCFRERSQKRTKKRA
FT KNRAKSRSTMYLSKVGDSSLAMSRSLPSVALPMHYLHHKLAESICFITATIDSL (in
FT isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_004962"
FT VAR_SEQ 54..63
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_004963"
SQ SEQUENCE 1224 AA; 138326 MW; 56D8513DD2061071 CRC64;
MGHSHSTGKE INDNELFTCE DPVFDQPVAS PKSEISSKLA EEIERSKSPL ILEVSPRTPD
SVQMFRPTFD TFRPPNSDSS TFRGSQSRED LVACSSMNSV NNVHDMNTVS SSSSSSAPLF
VALYDFHGVG EEQLSLRKGD QVRILGYNKN NEWCEARLYS TRKNDASNQR RLGEIGWVPS
NFIAPYNSLD KYTWYHGKIS RSDSEAILGS GITGSFLVRE SETSIGQYTI SVRHDGRVFH
YRINVDNTEK MFITQEVKFR TLGELVHHHS VHADGLICLL MYPASKKDKG RGLFSLSPNA
PDEWELDRSE IIMHNKLGGG QYGDVYEGYW KRHDCTIAVK ALKEDAMPLH EFLAEAAIMK
DLHHKNLVRL LGVCTHEAPF YIITEFMCNG NLLEYLRRTD KSLLPPIILV QMASQIASGM
SYLEARHFIH RDLAARNCLV SEHNIVKIAD FGLARFMKED TYTAHAGAKF PIKWTAPEGL
AFNTFSSKSD VWAFGVLLWE IATYGMAPYP GVELSNVYGL LENGFRMDGP QGCPPSVYRL
MLQCWNWSPS DRPRFRDIHF NLENLISSNS LNDEVQKQLK KNNDKKLESD KRRSNVRERS
DSKSRHSSHH DRDRDRESLH SRNSNPEIPN RSFIRTDDSV SFFNPSTTSK VTSFRAQGPP
FPPPPQQNTK PKLLKSVLNS NARHASEEFE RNEQDDVVPL AEKNVRKAVT RLGGTMPKGQ
RIDAYLDSMR RVDSWKESTD ADNEGAGSSS LSRTVSNDSL DTLPLPDSMN SSTYVKMHPA
SGENVFLRQI RSKLKKRSET PELDHIDSDT ADETTKSEKS PFGSLNKSSI KYPIKNAPEF
SENHSRVSPV PVPPSRNASV SVRPDSKAED SSDETTKDVG MWGPKHAVTR KIEIVKNDSY
PNVEGELKAK IRNLRHVPKE ESNTSSQEDL PLDATDNTND SIIVIPRDEK AKVRQLVTQK
VSPLQHHRPF SLQCPNNSTS SAISHSEHAD SSETSSLSGV YEERMKPELP RKRSNGDTKV
VPVTWIINGE KEPNGMARTK SLRDITSKFE QLGTASTIES KIEEAVPYRE HALEKKGTSK
RFSMLEGSNE LKHVVPPRKN RNQDESGSID EEPVSKDMIV SLLKVIQKEF VNLFNLASSE
ITDEKLQQFV IMADNVQKLH STCSVYAEQI SPHSKFRFKE LLSQLEIYNR QIKFSHNPRA
KPVDDKLKMA FQDCFDQIMR LVDR
