MIG15_CAEEL
ID MIG15_CAEEL Reviewed; 1096 AA.
AC Q23356; Q8I4B5; Q8T8M3; Q95ZI7; Q9UAN7; Q9XYC3; Q9XYC4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Serine/threonine-protein kinase mig-15;
DE EC=2.7.11.1;
DE AltName: Full=Abnormal cell migration protein 15;
GN Name=mig-15; ORFNames=ZC504.4;
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 [MRNA] (ISOFORM A), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 369-1096 (ISOFORM C).
RC STRAIN=Bristol N2;
RA Zhu X., Acharya P., Hedgecock E.M.;
RT "MIG-15, a NIK ortholog of the STE20 family of serine/threonine protein
RT kinases, is involved in cell migration and signal transduction in C.
RT elegans.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP IDENTIFICATION.
RA Zhu X., Hedgecock E.M.;
RT "mig-15 encodes a novel Ser/Thr protein kinase of the Ste-20/p65PAK
RT family.";
RL (er) Worm Breeder's Gazette 14(5):76(1997).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11967148; DOI=10.1016/s0960-9822(02)00764-9;
RA Poinat P., De Arcangelis A., Sookhareea S., Zhu X., Hedgecock E.M.,
RA Labouesse M., Georges-Labouesse E.;
RT "A conserved interaction between beta1 integrin/PAT-3 and Nck-interacting
RT kinase/MIG-15 that mediates commissural axon navigation in C. elegans.";
RL Curr. Biol. 12:622-631(2002).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22732572; DOI=10.1016/j.ydbio.2012.06.011;
RA Martynovsky M., Wong M.C., Byrd D.T., Kimble J., Schwarzbauer J.E.;
RT "mig-38, a novel gene that regulates distal tip cell turning during
RT gonadogenesis in C. elegans hermaphrodites.";
RL Dev. Biol. 368:404-414(2012).
CC -!- FUNCTION: Involved in cell migration and signal transduction
CC (PubMed:11967148, PubMed:22732572). Important in several developmental
CC processes including epidermal development, Q neuroblast migrations and
CC muscle arm targeting. Required with ina-1/pat-3 to stabilize the
CC commissural axons growth cone along a precise direction and are
CC required for the cell to respond appropriately when signaling in the
CC growth cone must change (PubMed:11967148). During gonad morphogenesis,
CC involved in distal tip cell (DTC) migration from the dorsal side of the
CC hermaphrodite body to the midbody to allow for formation of gonad arms
CC (PubMed:22732572). {ECO:0000269|PubMed:11967148,
CC ECO:0000269|PubMed:22732572}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=c;
CC IsoId=Q23356-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q23356-2; Sequence=VSP_014012;
CC Name=b;
CC IsoId=Q23356-3; Sequence=VSP_014011, VSP_014012;
CC Name=d;
CC IsoId=Q23356-4; Sequence=VSP_014010, VSP_014012;
CC -!- DISRUPTION PHENOTYPE: Mutants exhibit premature branching of
CC commissures (PubMed:11967148). RNAi-mediated knockdown results in gonad
CC distal tip cell (DTC) migration defects whereby DTCs do not migrate to
CC the midbody of the hermaphrodite and as a consequence this leads to
CC abnormal gonadal arm formation during gonad morphogenesis
CC (PubMed:22732572). Double knockdown with mig-38 results in enhanced
CC gonad DTC migration defects (PubMed:22732572).
CC {ECO:0000269|PubMed:11967148, ECO:0000269|PubMed:22732572}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; AF087131; AAD14593.1; -; mRNA.
DR EMBL; AF087132; AAD14594.1; -; mRNA.
DR EMBL; AF087133; AAD14595.1; -; mRNA.
DR EMBL; Z50029; CAB63416.1; -; Genomic_DNA.
DR EMBL; Z50029; CAB63417.1; -; Genomic_DNA.
DR EMBL; Z50029; CAC42384.1; -; Genomic_DNA.
DR EMBL; Z50029; CAD57714.1; -; Genomic_DNA.
DR PIR; T27622; T27622.
DR PIR; T43630; T43630.
DR PIR; T43632; T43632.
DR RefSeq; NP_001024971.1; NM_001029800.2. [Q23356-2]
DR RefSeq; NP_001024972.1; NM_001029801.3. [Q23356-3]
DR RefSeq; NP_001024973.1; NM_001029802.3. [Q23356-1]
DR RefSeq; NP_001024974.1; NM_001029803.3. [Q23356-4]
DR AlphaFoldDB; Q23356; -.
DR SMR; Q23356; -.
DR BioGRID; 46161; 22.
DR DIP; DIP-25874N; -.
DR IntAct; Q23356; 7.
DR STRING; 6239.ZC504.4c; -.
DR EPD; Q23356; -.
DR PaxDb; Q23356; -.
DR PeptideAtlas; Q23356; -.
DR EnsemblMetazoa; ZC504.4a.1; ZC504.4a.1; WBGene00003247. [Q23356-2]
DR EnsemblMetazoa; ZC504.4b.1; ZC504.4b.1; WBGene00003247. [Q23356-3]
DR EnsemblMetazoa; ZC504.4c.1; ZC504.4c.1; WBGene00003247. [Q23356-1]
DR EnsemblMetazoa; ZC504.4d.1; ZC504.4d.1; WBGene00003247. [Q23356-4]
DR GeneID; 181248; -.
DR KEGG; cel:CELE_ZC504.4; -.
DR UCSC; ZC504.4c; c. elegans. [Q23356-1]
DR CTD; 181248; -.
DR WormBase; ZC504.4a; CE25672; WBGene00003247; mig-15. [Q23356-2]
DR WormBase; ZC504.4b; CE25673; WBGene00003247; mig-15. [Q23356-3]
DR WormBase; ZC504.4c; CE28273; WBGene00003247; mig-15. [Q23356-1]
DR WormBase; ZC504.4d; CE32767; WBGene00003247; mig-15. [Q23356-4]
DR eggNOG; KOG0587; Eukaryota.
DR GeneTree; ENSGT00950000183196; -.
DR InParanoid; Q23356; -.
DR OMA; LEKRNGW; -.
DR OrthoDB; 533537at2759; -.
DR PhylomeDB; Q23356; -.
DR Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
DR SignaLink; Q23356; -.
DR PRO; PR:Q23356; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003247; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0010171; P:body morphogenesis; IGI:WormBase.
DR GO; GO:0033563; P:dorsal/ventral axon guidance; IMP:WormBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:WormBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IMP:UniProtKB.
DR GO; GO:0000003; P:reproduction; IMP:WormBase.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transducer;
KW Transferase.
FT CHAIN 1..1096
FT /note="Serine/threonine-protein kinase mig-15"
FT /id="PRO_0000086326"
FT DOMAIN 21..288
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 778..1070
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT REGION 293..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..319
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 151
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 27..35
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 356..371
FT /note="RKGFQKLQESSRGFAE -> Q (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_014010"
FT VAR_SEQ 431..435
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_014011"
FT VAR_SEQ 688..696
FT /note="Missing (in isoform a, isoform b and isoform d)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_014012"
SQ SEQUENCE 1096 AA; 122504 MW; C411C11566596386 CRC64;
MSSSGLDEID LNSLRDPAGI FELIEVVGNG TYGQVYKGRH VKTAQLAAIK IMNINEDEED
EIKLEINMLK KHSHHRNVAT YYGAFIKKLP SSTGKHDQLW LVMEFCGSGS ITDLVKNTKG
GSLKEEWIAY ICREILRGLY HLHQSKVIHR DIKGQNVLLT DSAEVKLVDF GVSAQLDKTV
GRRNTFIGTP YWMAPEVIAC DESPEATYDS RSDLWSLGIT ALEMAEGHPP LCDMHPMRAL
FLIPRNPPPK LKRNKKWTKK FETFIETVLV KDYHQRPYTG ALLRHPFIKE QPHEQTIRHS
IKEHIDRNRR VKKDDADYEY SGSEDDEPSP NNRGPSMGIR DDSESSSMIP MDNTLRKGFQ
KLQESSRGFA EPGAQQLRRL PQQPAPAPFQ YQQSRYVEPR RESSEVKLRA VSSRGAADGP
RHSPASRPRP VSHHQRSPQQ SHPAAPHLAD LANYEKRRRS EREERRERER QAHHAMPIAR
VSASVPAPQQ SRKMSEPLLI THVKPEDLDV LASELSKMGG HHNGRSREES MSPPPPAPPP
REASISSITD TIDVGELDNG ADAEWDDLKD IMMNGEGTLR GPNKPLPPTP TDGENTLVSD
VRRNGNGNSG HGAYKGKKIP EIRPGIISLD DDDSDSDNEE GNEPLMFKPI NASSSRGALP
DLLPKSPQLR RQINDQTRQM SDDRADESAS LFGSFYQPNG FQNSDSRSSI QHSFSNRDRE
KSFVGYFGGG AGAGGGTVNR PGRPQDINQV QVNVTPNSNG TPAENDAPEI RKYKKKFSGE
ILCAALWGVN LLIGTDSGLM LLDRSGQGKV YPLISRRRFD QMTVLEGQNI LATISGRKRR
IRVYYLSWLR QKILRTEGAG SANTTEKRNG WVNVGDLQGA IHFKIVRYER IKFLVVGLES
SIEIYAWAPK PYHKFMSFKS FGSLSHVPLI VDLTVEDNAR LKVLYGSTGG FHAIDLDSAA
VYDIYTPAQS GQTTTPHCIV VLPNSNGMQL LLCYDNEGVY VNTYGRMTKN VVLQWGEMPS
SVAYISTGQI MGWGNKAIEI RSVDTGHLDG VFMHKKAQKL KFLCERNDKV FFSSAKGGGS
CQIYFMTLNK PGLTNW
