MIG21_CAEEL
ID MIG21_CAEEL Reviewed; 306 AA.
AC G1FC92; Q19092;
DT 29-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Abnormal cell migration protein 21;
GN Name=mig-21; ORFNames=F01F1.13;
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 B), AND FUNCTION.
RX PubMed=22074987; DOI=10.1016/j.ydbio.2011.10.029;
RA Middelkoop T.C., Williams L., Yang P.T., Luchtenberg J., Betist M.C.,
RA Ji N., van Oudenaarden A., Kenyon C., Korswagen H.C.;
RT "The thrombospondin repeat containing protein MIG-21 controls a left-right
RT asymmetric Wnt signaling response in migrating C. elegans neuroblasts.";
RL Dev. Biol. 361:338-348(2012).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=23051647; DOI=10.1534/genetics.112.145706;
RA Sundararajan L., Lundquist E.A.;
RT "Transmembrane proteins UNC-40/DCC, PTP-3/LAR, and MIG-21 control anterior-
RT posterior neuroblast migration with left-right functional asymmetry in
RT Caenorhabditis elegans.";
RL Genetics 192:1373-1388(2012).
RN [4]
RP GLYCOSYLATION AT TRP-58 AND TRP-61.
RX PubMed=23562325; DOI=10.1016/j.molcel.2013.03.003;
RA Buettner F.F., Ashikov A., Tiemann B., Lehle L., Bakker H.;
RT "C. elegans DPY-19 is a C-mannosyltransferase glycosylating thrombospondin
RT repeats.";
RL Mol. Cell 50:295-302(2013).
CC -!- FUNCTION: Required for determination of left/right asymmetry in nervous
CC system. Acts together with unc-40 to control an initial left-right
CC asymmetric polarization of the Q neuroblasts. Mig-21 and unc-40 may
CC control the asymmetry in Wnt signaling response by restricting
CC posterior polarization to one of the 2 Q neuroblasts. Involved in left-
CC side QL posterior migration. In right-side QR, unc-40 and mig-21
CC pathways mutually inhibit each other in posterior migration, allowing
CC anterior QR migration. {ECO:0000269|PubMed:22074987,
CC ECO:0000269|PubMed:23051647}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=G1FC92-1; Sequence=Displayed;
CC Name=a;
CC IsoId=G1FC92-2; Sequence=VSP_046543;
CC -!- PTM: Glycosylated via C-mannosylation by dpy-19 at Trp-58 and Trp-61.
CC {ECO:0000269|PubMed:23562325}.
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DR EMBL; JN165085; AEK25615.1; -; mRNA.
DR EMBL; BX284603; CCG28107.1; -; Genomic_DNA.
DR EMBL; BX284603; CCD66001.2; -; Genomic_DNA.
DR RefSeq; NP_001254932.1; NM_001268003.1.
DR RefSeq; NP_001254933.2; NM_001268004.2. [G1FC92-2]
DR AlphaFoldDB; G1FC92; -.
DR SMR; G1FC92; -.
DR BioGRID; 48865; 1.
DR STRING; 6239.F01F1.13a; -.
DR iPTMnet; G1FC92; -.
DR PaxDb; G1FC92; -.
DR EnsemblMetazoa; F01F1.13.1; F01F1.13.1; WBGene00003252. [G1FC92-2]
DR GeneID; 184064; -.
DR KEGG; cel:CELE_F01F1.13; -.
DR UCSC; F01F1.13; c. elegans.
DR CTD; 184064; -.
DR WormBase; F01F1.13a; CE48870; WBGene00003252; mig-21. [G1FC92-2]
DR WormBase; F01F1.13b; CE47419; WBGene00003252; mig-21. [G1FC92-1]
DR eggNOG; ENOG502TH1V; Eukaryota.
DR GeneTree; ENSGT00940000174238; -.
DR InParanoid; G1FC92; -.
DR OMA; KIWNCIR; -.
DR PhylomeDB; G1FC92; -.
DR PRO; PR:G1FC92; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003252; Expressed in blast cell (C elegans) and 6 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:WormBase.
DR GO; GO:0038023; F:signaling receptor activity; ISS:WormBase.
DR GO; GO:0035545; P:determination of left/right asymmetry in nervous system; IMP:WormBase.
DR GO; GO:0097402; P:neuroblast migration; IMP:WormBase.
DR GO; GO:0001764; P:neuron migration; IMP:WormBase.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:WormBase.
DR GO; GO:0030334; P:regulation of cell migration; IMP:WormBase.
DR Gene3D; 2.20.100.10; -; 2.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF00090; TSP_1; 1.
DR SMART; SM00209; TSP1; 2.
DR SUPFAM; SSF82895; SSF82895; 2.
DR PROSITE; PS50092; TSP1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Membrane; Neurogenesis;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..306
FT /note="Abnormal cell migration protein 21"
FT /id="PRO_0000422599"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 55..102
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 109..155
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT CARBOHYD 58
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:23562325"
FT CARBOHYD 61
FT /note="C-linked (Man) tryptophan"
FT /evidence="ECO:0000269|PubMed:23562325"
FT DISULFID 121..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 123..154
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 134..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT VAR_SEQ 1..48
FT /note="MERDSNTAKSEIFYSNPAIWRHLKDGKGEGMSKSEKRNKHGCRNFTYS ->
FT MIVMVLFNIFVFVNFSYSLANLNDSSILYSQVVSNKCASNNGIFCECSKQGGEIK (in
FT isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_046543"
SQ SEQUENCE 306 AA; 35886 MW; 59AAE9795271EEF5 CRC64;
MERDSNTAKS EIFYSNPAIW RHLKDGKGEG MSKSEKRNKH GCRNFTYSIW NCIRPGGWST
WSKWSKCREG IRKRRRTCNN PLPIGTTCSG QKVEKQSCAI SSNVPEYLFG SWTSWNPWSR
CDCDRSLRIR TRHCKGNSCE GCDKDYEDCR PDECPISKKW SEWTDWVNYG IEQVRFSAWC
SSSNVANTEV GIRKETQDSM KHANWSEWHM HPGVAYRYRL LHNSSISIEH HLLSRFTSSC
LPLHFAIPIF CFCILTGFLL QNIIYCVVNR FKRRFIRLNY SYDSNPRDYP SHLIRSPGSP
KDESFW
