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   24-JAN-2024, entry version 199.
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; 50.
DR   DIP; DIP-48409N; -.
DR   IntAct; P03949; 45.
DR   STRING; 6239.M79.1a.1; -.
DR   iPTMnet; P03949; -.
DR   EPD; P03949; -.
DR   PaxDb; 6239-M79-1a; -.
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   AGR; WB:WBGene00000018; -.
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; TYGMAPY; -.
DR   OrthoDB; 1614410at2759; -.
DR   BRENDA; 2.7.10.2; 1045.
DR   Reactome; R-CEL-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR   Reactome; R-CEL-428890; Role of ABL in ROBO-SLIT signaling.
DR   Reactome; R-CEL-525793; Myogenesis.
DR   Reactome; R-CEL-5663213; RHO GTPases Activate WASPs and WAVEs.
DR   Reactome; R-CEL-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR   Reactome; R-CEL-9013423; RAC3 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 cell types or 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0010212; P:response to ionizing radiation; IMP:WormBase.
DR   GO; GO:0007283; P:spermatogenesis; IMP:WormBase.
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:SF162; TYROSINE-PROTEIN KINASE ABL; 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; 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   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
//