MIG13_CAEEL
ID MIG13_CAEEL Reviewed; 362 AA.
AC G5EF33; H2KZ96;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Abnormal cell migration protein 13 {ECO:0000305};
DE Flags: Precursor;
GN Name=mig-13 {ECO:0000312|WormBase:F43C9.4a};
GN ORFNames=F43C9.4 {ECO:0000312|WormBase:F43C9.4a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAD43178.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP CYS-190.
RX PubMed=10412978; DOI=10.1016/s0092-8674(00)80603-0;
RA Sym M., Robinson N., Kenyon C.;
RT "MIG-13 positions migrating cells along the anteroposterior body axis of C.
RT elegans.";
RL Cell 98:25-36(1999).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION.
RX PubMed=8898225; DOI=10.1242/dev.122.10.3117;
RA Harris J., Honigberg L., Robinson N., Kenyon C.;
RT "Neuronal cell migration in C. elegans: regulation of Hox gene expression
RT and cell position.";
RL Development 122:3117-3131(1996).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=15750187; DOI=10.1242/dev.01569;
RA Yang L., Sym M., Kenyon C.;
RT "The roles of two C. elegans HOX co-factor orthologs in cell migration and
RT vulva development.";
RL Development 132:1413-1428(2005).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22293500; DOI=10.1016/j.febslet.2012.01.031;
RA Masuda H., Nakamura K., Takata N., Itoh B., Hirose T., Moribe H.,
RA Mekada E., Okada M.;
RT "MIG-13 controls anteroposterior cell migration by interacting with UNC-
RT 71/ADM-1 and SRC-1 in Caenorhabditis elegans.";
RL FEBS Lett. 586:740-746(2012).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP GLY-167.
RX PubMed=23784779; DOI=10.1073/pnas.1301849110;
RA Wang X., Zhou F., Lv S., Yi P., Zhu Z., Yang Y., Feng G., Li W., Ou G.;
RT "Transmembrane protein MIG-13 links the Wnt signaling and Hox genes to the
RT cell polarity in neuronal migration.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:11175-11180(2013).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26022293; DOI=10.1534/g3.115.018770;
RA Sundararajan L., Norris M.L., Lundquist E.A.;
RT "SDN-1/Syndecan acts in parallel to the transmembrane molecule MIG-13 to
RT promote anterior neuroblast migration.";
RL G3 (Bethesda) 5:1567-1574(2015).
RN [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ABL-1 AND SEM-5, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
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).
RN [9] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=26762178; DOI=10.1002/1873-3468.12043;
RA Zhou X., Zeng J., Ouyang C., Luo Q., Yu M., Yang Z., Wang H., Shen K.,
RA Shi A.;
RT "A novel bipartite UNC-101/AP-1 mu1 binding signal mediates KVS-4/Kv2.1
RT somatodendritic distribution in Caenorhabditis elegans.";
RL FEBS Lett. 590:76-92(2016).
CC -!- FUNCTION: Probable receptor that acts as an upstream signaling protein
CC to promote the guidance, migration and positioning of the right Q
CC neuroblast (QR) and its descendants along the anteroposterior body
CC axis, and also the anterior migration of BDU interneurons during larval
CC development (PubMed:10412978, PubMed:8898225, PubMed:15750187,
CC PubMed:22293500, PubMed:23784779, PubMed:26022293, PubMed:27780040).
CC Associates with and recruits the downstream components tyrosine kinase
CC abl-1 and the tyrosine kinase adapter protein sem-5 to the leading edge
CC of migrating Q neuroblasts and their descendants to activate signaling
CC through the two parallel wve-1 and wsp-1 pathways, respectively, and
CC direct migration along the anteroposterior body axis (PubMed:27780040).
CC Involved in cytoskeleton dynamics regulating the organization of the
CC actin cytoskeleton at the leading edge of migrating cells to ensure
CC correct Q cell polarity and promote migration (PubMed:23784779,
CC PubMed:27780040). Role in cytoskeleton organization may be by
CC activation of the wve-1 and wsp-1 pathways which recruit the Arp2/3
CC complex to the leading edge of migrating cells (PubMed:27780040). Plays
CC a role in regulating the asymmetric distribution of the actin
CC cytoskeleton-binding protein cor-1 in Q neuroblasts which is required
CC for the anterior migration of QR neuroblasts (PubMed:23784779).
CC {ECO:0000269|PubMed:10412978, ECO:0000269|PubMed:15750187,
CC ECO:0000269|PubMed:22293500, ECO:0000269|PubMed:23784779,
CC ECO:0000269|PubMed:26022293, ECO:0000269|PubMed:27780040,
CC ECO:0000269|PubMed:8898225}.
CC -!- SUBUNIT: Interacts with abl-1 (via SH2 and SH3 domains); the
CC interaction is direct. Interacts with sem-5; the interaction is direct.
CC {ECO:0000269|PubMed:27780040}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10412978,
CC ECO:0000269|PubMed:23784779, ECO:0000269|PubMed:27780040}; Single-pass
CC type I membrane protein {ECO:0000255}. Perikaryon
CC {ECO:0000269|PubMed:10412978}. Cell projection, axon
CC {ECO:0000269|PubMed:10412978, ECO:0000269|PubMed:26762178}. Cell
CC projection, dendrite {ECO:0000269|PubMed:26762178}. Note=Localizes to
CC the leading edge of migrating Q-neuroblasts.
CC {ECO:0000269|PubMed:27780040}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F43C9.4a};
CC IsoId=G5EF33-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F43C9.4b};
CC IsoId=G5EF33-2; Sequence=VSP_058961;
CC -!- TISSUE SPECIFICITY: Expressed in pharyngeal-intestinal valve cells and
CC ventral cord neurons. {ECO:0000269|PubMed:10412978}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryogenesis to adulthood
CC (PubMed:10412978). First expressed in the anterior region of comma
CC stage embryos (PubMed:10412978). During embryogenesis, expressed in
CC pharyngeal, hypodermal and neuronal precursors in the anterior body
CC region (PubMed:10412978). During larval development, expressed in the
CC pharyngeal-intestinal valve cells and neurons in the retrovesicular
CC ganglion and the ventral cord (PubMed:10412978). Expressed in migrating
CC QR neuroblasts with higher expression in migrating QR.a/ap cells than
CC QR.p/pa cells (PubMed:23784779). {ECO:0000269|PubMed:10412978,
CC ECO:0000269|PubMed:23784779}.
CC -!- DISRUPTION PHENOTYPE: Abnormal migration of QR neuroblast lineage cells
CC and BDU interneurons (PubMed:10412978, PubMed:22293500,
CC PubMed:26022293). QR neuroblast descendants QR.paa and QR.pap
CC irregularly migrate towards the posterior side of the body axis while
CC QR.ap descendants fail to migrate towards the head and remain in the
CC central body region or migrate towards the tail (PubMed:10412978).
CC Irregular AQR neuron morphology and polarity during migration in larva
CC at the L4 stage (PubMed:26022293, PubMed:27780040). Loss of F-actin at
CC the leading edge of AQR neurons and as a result AQR neurons do not
CC extend the lamellipodium and thus fail to translocate the cell body
CC towards the anterior of the body leading to posteriorly positioned AQR
CC neurons (PubMed:27780040). {ECO:0000269|PubMed:10412978,
CC ECO:0000269|PubMed:22293500, ECO:0000269|PubMed:26022293,
CC ECO:0000269|PubMed:27780040}.
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DR EMBL; AF150958; AAD43178.1; -; mRNA.
DR EMBL; BX284606; CCD67084.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD67085.1; -; Genomic_DNA.
DR PIR; T16359; T16359.
DR RefSeq; NP_001024660.1; NM_001029489.2. [G5EF33-1]
DR RefSeq; NP_001024661.1; NM_001029490.2. [G5EF33-2]
DR AlphaFoldDB; G5EF33; -.
DR SMR; G5EF33; -.
DR STRING; 6239.F43C9.4a; -.
DR PaxDb; G5EF33; -.
DR EnsemblMetazoa; F43C9.4a.1; F43C9.4a.1; WBGene00003245. [G5EF33-1]
DR EnsemblMetazoa; F43C9.4a.2; F43C9.4a.2; WBGene00003245. [G5EF33-1]
DR EnsemblMetazoa; F43C9.4b.1; F43C9.4b.1; WBGene00003245. [G5EF33-2]
DR GeneID; 180755; -.
DR KEGG; cel:CELE_F43C9.4; -.
DR CTD; 180755; -.
DR WormBase; F43C9.4a; CE28324; WBGene00003245; mig-13. [G5EF33-1]
DR WormBase; F43C9.4b; CE34562; WBGene00003245; mig-13. [G5EF33-2]
DR eggNOG; ENOG502SC3N; Eukaryota.
DR InParanoid; G5EF33; -.
DR OMA; RNDVHRN; -.
DR OrthoDB; 866864at2759; -.
DR PhylomeDB; G5EF33; -.
DR PRO; PR:G5EF33; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00003245; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:WormBase.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.60.120.290; -; 1.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF57424; SSF57424; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Disulfide bond;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..362
FT /note="Abnormal cell migration protein 13"
FT /evidence="ECO:0000305"
FT /id="PRO_5008958413"
FT TOPO_DOM 21..237
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 36..175
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 182..225
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT REGION 275..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 36..68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 98..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DISULFID 183..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 190..208
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 202..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT VAR_SEQ 1..25
FT /note="MTKLLIALILFSICWKPYSAEPIAS -> MICIIFLSDSITSTCFYSG (in
FT isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058961"
FT MUTAGEN 167
FT /note="G->E: In cas65; reduced AVM neuron migration."
FT /evidence="ECO:0000269|PubMed:23784779"
FT MUTAGEN 190
FT /note="C->Y: In mu294; abnormal Q neuroblast lineage
FT migration."
FT /evidence="ECO:0000269|PubMed:10412978"
SQ SEQUENCE 362 AA; 40149 MW; ABD2EFE14FA622E4 CRC64;
MTKLLIALIL FSICWKPYSA EPIASFFDGL DSRNECKARL DRRLTGFSGL LYSHSKYGQE
PYNTSRNCVL MLVAPIGYSI RVRALQFDVA STENARTCEK DTLHVFDHET TLDPESYAPA
RIDDITSPGP IIGQFCGHFE NRILNTSSHN ALTLWWHSNP NGSNSKGFKL HWGSFRVSKT
GNCVTGEFSC GNGECIPIES ACDRFADCSN GEDLIHSRQM AANCQNIELD PLTTVSGVFV
LLFSATIILS LCGFIMFVCC LCKCLKSTIP IKGASSHTTT TTATDYKPDP PQFYPPSPPK
MPPPSAASSY TPRLHHHFEG PLVPSETSAF HSSNRMQNHY SVNSDINGDY TYVRNDVHRN
LL
