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   24-JAN-2024, entry version 167.
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; 11.
DR   IntAct; P34400; 6.
DR   STRING; 6239.F10E9.6c.2; -.
DR   iPTMnet; P34400; -.
DR   EPD; P34400; -.
DR   PaxDb; 6239-F10E9-6c; -.
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   AGR; WB:WBGene00003243; -.
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; CCDDQAT; -.
DR   OrthoDB; 3144731at2759; -.
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 cell types or 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:0018991; P:egg-laying behavior; 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: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; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; GROWTH FACTOR RECEPTOR-BOUND PROTEIN; 1.
DR   PANTHER; PTHR11243:SF23; LD06925P; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00788; RA; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00314; RA; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 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
//