MIG10_CAEEL
ID MIG10_CAEEL Reviewed; 779 AA.
AC P34400; P34386; P34403; Q7JQ80; Q8WT53;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Abnormal cell migration protein 10;
GN Name=mig-10 {ECO:0000312|WormBase:F10E9.6c};
GN ORFNames=F10E9.6 {ECO:0000312|WormBase:F10E9.6c};
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] (ISOFORMS A AND B), AND FUNCTION.
RX PubMed=9142991; DOI=10.1006/dbio.1997.8516;
RA Manser J., Roonprapunt C., Margolis B.;
RT "C. elegans cell migration gene mig-10 shares similarities with a family of
RT SH2 domain proteins and acts cell nonautonomously in excretory canal
RT development.";
RL Dev. Biol. 184:150-164(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [4]
RP FUNCTION.
RX PubMed=2361334; DOI=10.1002/dvg.1020110107;
RA Manser J., Wood W.B.;
RT "Mutations affecting embryonic cell migrations in Caenorhabditis elegans.";
RL Dev. Genet. 11:49-64(1990).
RN [5]
RP FUNCTION, INTERACTION WITH CED-10, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18499456; DOI=10.1016/j.cub.2008.04.050;
RA Quinn C.C., Pfeil D.S., Wadsworth W.G.;
RT "CED-10/Rac1 mediates axon guidance by regulating the asymmetric
RT distribution of MIG-10/lamellipodin.";
RL Curr. Biol. 18:808-813(2008).
CC -!- FUNCTION: Required cell non-autonomously for proper development of the
CC excretory canals and for the long-range anterior-posterior migrations
CC of embryonic neurons CAN, ALM and HSN (PubMed:9142991, PubMed:2361334).
CC Plays a role, probably downstream of ced-10/rac1, in orientating axonal
CC growth of HSN and AVM neurons in response to guidance cues such as slt-
CC 1 (PubMed:18499456). May regulate growth cone polarization by promoting
CC asymmetric F-actin assembly (PubMed:18499456). May be involved in
CC signal transduction during cell migration (PubMed:9142991).
CC {ECO:0000269|PubMed:18499456, ECO:0000269|PubMed:2361334,
CC ECO:0000269|PubMed:9142991}.
CC -!- SUBUNIT: May interact (via Ras-associating and PH domains) with ced-10
CC (GTP-bound form). {ECO:0000269|PubMed:18499456}.
CC -!- INTERACTION:
CC P34400; Q10929: abi-1; NbExp=6; IntAct=EBI-2315872, EBI-315750;
CC P34400; G5EC32: sorb-1; NbExp=7; IntAct=EBI-2315872, EBI-325337;
CC -!- SUBCELLULAR LOCATION: Perikaryon {ECO:0000269|PubMed:18499456}.
CC Note=Enriched at the ventral edge of HSN cell bodies. This asymmetric
CC distribution is regulated by ced-10/rac1.
CC {ECO:0000269|PubMed:18499456}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=c {ECO:0000312|WormBase:F10E9.6c};
CC IsoId=P34400-3; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F10E9.6a};
CC IsoId=P34400-1; Sequence=VSP_014008;
CC Name=b {ECO:0000312|WormBase:F10E9.6b};
CC IsoId=P34400-2; Sequence=VSP_008867, VSP_014009;
CC -!- DISRUPTION PHENOTYPE: Defects in axon guidance in HSN neurons although
CC axons reach the ventral nerve cord in the end. In max-2 and mig-10
CC double mutants, the phenotype is more severe resulting in axons failing
CC to reach the ventral nerve cord. {ECO:0000269|PubMed:18499456}.
CC -!- SIMILARITY: Belongs to the MRL family. {ECO:0000305}.
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DR EMBL; BX284603; CCD69133.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD69132.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD69134.1; -; Genomic_DNA.
DR PIR; S44806; S44806.
DR RefSeq; NP_001021248.1; NM_001026077.4.
DR RefSeq; NP_498821.2; NM_066420.4. [P34400-2]
DR RefSeq; NP_498822.2; NM_066421.3.
DR AlphaFoldDB; P34400; -.
DR SMR; P34400; -.
DR BioGRID; 41372; 10.
DR IntAct; P34400; 6.
DR STRING; 6239.F10E9.6c; -.
DR iPTMnet; P34400; -.
DR EPD; P34400; -.
DR PaxDb; P34400; -.
DR PeptideAtlas; P34400; -.
DR EnsemblMetazoa; F10E9.6a.1; F10E9.6a.1; WBGene00003243. [P34400-1]
DR EnsemblMetazoa; F10E9.6a.2; F10E9.6a.2; WBGene00003243. [P34400-1]
DR EnsemblMetazoa; F10E9.6a.3; F10E9.6a.3; WBGene00003243. [P34400-1]
DR EnsemblMetazoa; F10E9.6b.1; F10E9.6b.1; WBGene00003243. [P34400-2]
DR EnsemblMetazoa; F10E9.6c.1; F10E9.6c.1; WBGene00003243. [P34400-3]
DR GeneID; 176168; -.
DR UCSC; F10E9.6c; c. elegans. [P34400-1]
DR CTD; 176168; -.
DR WormBase; F10E9.6a; CE29261; WBGene00003243; mig-10. [P34400-1]
DR WormBase; F10E9.6b; CE00150; WBGene00003243; mig-10. [P34400-2]
DR WormBase; F10E9.6c; CE36129; WBGene00003243; mig-10. [P34400-3]
DR eggNOG; KOG3751; Eukaryota.
DR GeneTree; ENSGT00940000171020; -.
DR InParanoid; P34400; -.
DR OMA; QENPGHP; -.
DR OrthoDB; 918824at2759; -.
DR Reactome; R-CEL-354192; Integrin signaling.
DR Reactome; R-CEL-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-CEL-5674135; MAP2K and MAPK activation.
DR SignaLink; P34400; -.
DR PRO; PR:P34400; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003243; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0031941; C:filamentous actin; IDA:WormBase.
DR GO; GO:0032584; C:growth cone membrane; IDA:WormBase.
DR GO; GO:0030027; C:lamellipodium; IDA:WormBase.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO.
DR GO; GO:0017124; F:SH3 domain binding; IPI:WormBase.
DR GO; GO:0031103; P:axon regeneration; IMP:WormBase.
DR GO; GO:0048858; P:cell projection morphogenesis; IMP:WormBase.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0008078; P:mesodermal cell migration; IMP:WormBase.
DR GO; GO:0001764; P:neuron migration; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0099054; P:presynapse assembly; IDA:SynGO.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0040025; P:vulval development; IMP:WormBase.
DR CDD; cd01259; PH_APBB1IP; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR039664; GRB/APBB1IP.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR039665; PH_APBB1IP.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR11243; PTHR11243; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00314; RA; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50200; RA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Neurogenesis;
KW Reference proteome.
FT CHAIN 1..779
FT /note="Abnormal cell migration protein 10"
FT /id="PRO_0000181353"
FT DOMAIN 317..407
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 456..566
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 78..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..95
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..745
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..129
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:9142991"
FT /id="VSP_008867"
FT VAR_SEQ 1..112
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000303|PubMed:9142991"
FT /id="VSP_014008"
FT VAR_SEQ 130..150
FT /note="PQVPPKPPIDTVRYSMNNIKE -> MYHDRRRTGFRQYETYMKQKQ (in
FT isoform b)"
FT /evidence="ECO:0000303|PubMed:9142991"
FT /id="VSP_014009"
SQ SEQUENCE 779 AA; 87502 MW; E5EAE25205EBFAC5 CRC64;
MDSCEEECDL EVDSDEEDQL FGEKCISLLS SLLPLSSSTL LSNAINLELD EVERPPPLLN
VLEEQQFPKV CANIEEENEL EADTEEDIAE TADDEESKDP VEKTENFEPS VTMDTYDFPD
PYPVQIRARP QVPPKPPIDT VRYSMNNIKE SADWQLDELL EELEALETQL NSSNGGDQLL
LGVSGIPASS SRENVKSIST LPPPPPALSY HQTPQQPQLL HHHNNHLGYQ NGIHQITSIN
SAASSCSSPD GDSAFGDSSS TESSNNRCRN SAFSSNDSCR DSLNTPSPTQ VSPRNGELNA
EEAKAQKIRQ ALEKMKEAKV TKIFVKFFVE DGEALQLLID ERWTVADTLK QLAEKNHIAL
MEDHCIVEEY PELYIKRVYE DHEKVVENIQ MWVQDSPNKL YFMRRPDKYA FISRPELYLL
TPKTSDHMEI PSGDQWTIDV KQKFVSEYFH REPVVPPEME GFLYLKSDGR KSWKKHYFVL
RPSGLYYAPK SKKPTTKDLT CLMNLHSNQV YTGIGWEKKY KSPTPWCISI KLTALQMKRS
QFIKYICAED EMTFKKWLVA LRIAKNGAEL LENYERACQI RRETLGPASS MSAASSSTAI
SEVPHSLSHH QRTPSVASSI QLSSHMMNNP THPLSVNVRN QSPASFSVNS CQQSHPSRTS
AKLEIQYDEQ PTGTIKRAPL DVLRRVSRAS TSSPTIPQEE SDSDEEFPAP PPVASVMRMP
PPVTPPKPCT PLTSKKAPPP PPKRSDTTKL QSASPMAPAK NDLEAALARR REKMATMEC
