RIG6_CAEEL
ID RIG6_CAEEL Reviewed; 1196 AA.
AC H2KZ60; Q18382; Q8MQA8; Q9BIA2;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Contactin rig-6 {ECO:0000303|PubMed:23123963};
DE Flags: Precursor;
GN Name=rig-6 {ECO:0000312|WormBase:C33F10.5d};
GN ORFNames=C33F10.5 {ECO:0000312|WormBase:C33F10.5d};
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|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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=23123963; DOI=10.1016/j.ydbio.2012.10.027;
RA Katidou M., Tavernarakis N., Karagogeos D.;
RT "The contactin RIG-6 mediates neuronal and non-neuronal cell migration in
RT Caenorhabditis elegans.";
RL Dev. Biol. 373:184-195(2013).
RN [3]
RP FUNCTION, INTERACTION WITH SAX-7, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF 438-ARG--LEU-1196.
RX PubMed=28901288; DOI=10.7554/elife.29257;
RA Kim B., Emmons S.W.;
RT "Multiple conserved cell adhesion protein interactions mediate neural
RT wiring of a sensory circuit in C. elegans.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: Probable cell adhesion protein involved in patterning of the
CC nervous system, playing a role in ALM and PLM touch receptor axon
CC growth and VNC axon navigation (PubMed:23123963). By associating with
CC the transmembrane protein sax-7, mediates axonal interactions to
CC establish synaptic connections between the AVG interneuron and the two
CC PHC sensory neurons (PubMed:28901288). Also required for non-neuronal
CC cell migration in the excretory canal, regulating excretory canal
CC elongation and excretory cell morphogenesis (PubMed:23123963). Plays a
CC role in regulating male mating behavior (PubMed:28901288).
CC {ECO:0000269|PubMed:23123963, ECO:0000269|PubMed:28901288}.
CC -!- SUBUNIT: Interacts with sax-7; the interaction establishes synaptic
CC connections between neurons. {ECO:0000269|PubMed:28901288}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}. Perikaryon {ECO:0000269|PubMed:23123963,
CC ECO:0000269|PubMed:28901288}. Cell projection, axon
CC {ECO:0000269|PubMed:23123963, ECO:0000269|PubMed:28901288}. Synapse
CC {ECO:0000269|PubMed:23123963}. Cytoplasm {ECO:0000269|PubMed:28901288}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=d {ECO:0000312|WormBase:C33F10.5d};
CC IsoId=H2KZ60-1; Sequence=Displayed;
CC Name=c {ECO:0000312|WormBase:C33F10.5c};
CC IsoId=H2KZ60-4; Sequence=VSP_058504;
CC -!- TISSUE SPECIFICITY: Expressed in neurons including the I1 and I3
CC pharyngeal interneurons, NSM and VNC motor neurons, HSN and CAN
CC neurons, the ALM and PLM touch receptor neurons and other unidentified
CC head neurons (PubMed:23123963). Expressed in AVG interneurons
CC (PubMed:28901288). Also expressed in somatic muscles, the excretory
CC canal, the excretory cell and the hypodermis (PubMed:23123963).
CC {ECO:0000269|PubMed:23123963, ECO:0000269|PubMed:28901288}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development and
CC adulthood. {ECO:0000269|PubMed:23123963}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in truncated or
CC shorter excretory canals, and also truncated ALM axons that fail to
CC extend above the nerve ring, truncated PLM processes and abnormal VNC
CC axon patterning. {ECO:0000269|PubMed:23123963}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC family. {ECO:0000305}.
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DR EMBL; BX284602; CCD66510.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD66509.1; -; Genomic_DNA.
DR PIR; T15746; T15746.
DR RefSeq; NP_001022014.1; NM_001026843.3. [H2KZ60-1]
DR RefSeq; NP_740979.1; NM_170981.4.
DR AlphaFoldDB; H2KZ60; -.
DR SMR; H2KZ60; -.
DR STRING; 6239.C33F10.5b; -.
DR EPD; H2KZ60; -.
DR PeptideAtlas; H2KZ60; -.
DR PRIDE; H2KZ60; -.
DR EnsemblMetazoa; C33F10.5c.1; C33F10.5c.1; WBGene00016354. [H2KZ60-4]
DR EnsemblMetazoa; C33F10.5d.1; C33F10.5d.1; WBGene00016354. [H2KZ60-1]
DR GeneID; 173828; -.
DR KEGG; cel:CELE_C33F10.5; -.
DR UCSC; C33F10.5c.1; c. elegans.
DR CTD; 173828; -.
DR WormBase; C33F10.5c; CE31679; WBGene00016354; rig-6. [H2KZ60-4]
DR WormBase; C33F10.5d; CE37327; WBGene00016354; rig-6. [H2KZ60-1]
DR eggNOG; KOG3513; Eukaryota.
DR OrthoDB; 655902at2759; -.
DR Reactome; R-CEL-1474228; Degradation of the extracellular matrix.
DR Reactome; R-CEL-210991; Basigin interactions.
DR Reactome; R-CEL-216083; Integrin cell surface interactions.
DR Reactome; R-CEL-376172; DSCAM interactions.
DR Reactome; R-CEL-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
DR Reactome; R-CEL-433692; Proton-coupled monocarboxylate transport.
DR Reactome; R-CEL-70268; Pyruvate metabolism.
DR Reactome; R-CEL-9749641; Aspirin ADME.
DR PRO; PR:H2KZ60; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00016354; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0035545; P:determination of left/right asymmetry in nervous system; IMP:UniProtKB.
DR GO; GO:0033563; P:dorsal/ventral axon guidance; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0060562; P:epithelial tube morphogenesis; IMP:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:UniProtKB.
DR GO; GO:2000747; P:negative regulation of defecation rhythm; IMP:UniProtKB.
DR GO; GO:0060467; P:negative regulation of fertilization; IMP:UniProtKB.
DR GO; GO:0090327; P:negative regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:UniProtKB.
DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IMP:UniProtKB.
DR GO; GO:1903356; P:positive regulation of distal tip cell migration; IMP:UniProtKB.
DR GO; GO:0035150; P:regulation of tube size; IMP:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 8.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR PANTHER; PTHR10075; PTHR10075; 3.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00060; FN3; 4.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Cell projection;
KW Cytoplasm; Disulfide bond; Glycoprotein; GPI-anchor; Immunoglobulin domain;
KW Lipoprotein; Membrane; Neurogenesis; Reference proteome; Repeat; Signal;
KW Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1177
FT /note="Contactin rig-6"
FT /evidence="ECO:0000305"
FT /id="PRO_5003564315"
FT PROPEP 1178..1196
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000437246"
FT TRANSMEM 1174..1194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 144..225
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 232..319
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 355..438
FT /note="Ig-like C2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 441..533
FT /note="Ig-like C2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 539..626
FT /note="Ig-like C2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 631..730
FT /note="Ig-like C2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 736..844
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 849..961
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 963..1057
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1064..1168
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT LIPID 1177
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 925
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 974
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 979
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 986
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1002
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1092
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 169..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 263..316
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 372..420
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 462..517
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 562..610
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 653..718
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..422
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058504"
FT MUTAGEN 438..1196
FT /note="Missing: In gk438569; disrupts axonal connections
FT between the male-specific sensory neuron HOA and the
FT interneuron AVG, and between the two PHC sensory neurons
FT and the AVG interneuron. No disruption to the connection
FT between HOA and the PHC neurons."
FT /evidence="ECO:0000269|PubMed:28901288"
SQ SEQUENCE 1196 AA; 132852 MW; DD9C91B21F228CBA CRC64;
MMMLIRCISI FLLFGFVNAL IDEASCPIGW QIASDQCVRI VIAPANLKHS KKYCHHEGGE
LMDTSVTLLL EDVMDLLKNL HENGLSEPTF HVGGMGQALN RTEDGNYKII TINPSSHFPF
ICSLNKMARR SLLFQQKLLP VGAPQISLTG QSEIYFHPRH DADYIALPCT VQGNPKPTVA
WYKNDVEVLS PSMSNVSYLL SGGNLLVPAS STLAYSSFHC TARNSLGEVR SPPILLKPSF
IDPFRPHRLD VYSLATGGAK LDCDAPAHQP KSLTYSWLYG SSTDRILSQN ERKFISLDGT
LFFSYVTAED EDSYACSLSV YSTQSGHYGP FFRLISSTPK LVNSTFPPKL DSTQPQIFPE
DPKVGDSIYL ECFAYASPLP QYKWSRVDGK PIPARSHISN YGRVLKIEKV NYGDAGKYKC
VAMNAFGSAA GEVHVKLRAP PSILQGLHDR LVPTESNVSF ECLLSNADSY SSVEWFKDAK
PIVPLLLPAE KRKRLKIDHN VLHLKFADET DSGVYQCVAS NDVGSSSSSA LLTVKDSAPV
FPPNAMSRKV FAAFGSTVSI PCIFEASPRF HGKWADAGGS KLPQKGRIRD EEGVISIEKV
LHEDAGLFFC TAHNKLGKAH AQVQLIVVNK PSIKTNFLDE ETVNMSCEVE LTCENSAECP
EALFEWKIND RPAKEYPSLK SKVHEKKSGH KGRHLKQKVD LEVPKSLAGS RQIGRFACSS
LYGGSSEFVT KPQLPSPIAL TVEQMDEDGK KKKMFRLRWR LPPQHRDTRD HSPKVEGYLV
ELRTRKNRKW RAAERQLVGN MEKDSITVEN LLPNTEYQFR VRSVESAAIG EPSIPSDWVK
TAPGAPSETI DNLKWRSLDS QTLLVEWQPI EIGQESSGDN LRYRVSWSEA TVGKNATDDM
KLSNQDDDFE NHLDSDQPQA ILKLNTTEGC RMVVLAVRPV NDQGNGSVGT DTIAFLNSHG
ELKKVSLHNV KPINASHVNI SWTWDNTSDC DTKHAVQITC INLSGSEISA TVASDRIFWM
LGGLEAETAY DCDLKAIDNH GSFGPASKKF RIHTKQHPPS ETPLIGKLMM KQMKDTYTTI
LEWSSIELQK PNRTENGCGY KIFIYISETA TEAIELDMPL QRLSDRRNPS ARLDGLKLMY
MYTIKVAGYN PGGIGPISEP RSIRLGSPGT MDYTTGSSDV PIPSLLLLLL LLLWRL
