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Contactin rig-6

 RIG6_CAEEL              Reviewed;        1196 AA.
H2KZ60; Q18382; Q8MQA8; Q9BIA2;
05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
21-MAR-2012, sequence version 1.
23-MAY-2018, entry version 57.
RecName: Full=Contactin rig-6 {ECO:0000303|PubMed:23123963};
Flags: Precursor;
Name=rig-6 {ECO:0000312|WormBase:C33F10.5d};
ORFNames=C33F10.5 {ECO:0000312|WormBase:C33F10.5d};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
[1] {ECO:0000312|Proteomes:UP000001940}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=23123963; DOI=10.1016/j.ydbio.2012.10.027;
Katidou M., Tavernarakis N., Karagogeos D.;
"The contactin RIG-6 mediates neuronal and non-neuronal cell migration
in Caenorhabditis elegans.";
Dev. Biol. 373:184-195(2013).
-!- FUNCTION: Probable cell adhesion protein. Involved in patterning
of the nervous system, playing a role in ALM and PLM touch
receptor axon growth and VNC axon navigation. Also required for
non-neuronal cell migration in the excretory canal, regulating
excretory canal elongation and excretory cell morphogenesis.
{ECO:0000269|PubMed:23123963, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor,
GPI-anchor {ECO:0000255}. Perikaryon
{ECO:0000269|PubMed:23123963}. Cell projection, axon
{ECO:0000269|PubMed:23123963}. Cell junction, synapse
{ECO:0000269|PubMed:23123963}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=d {ECO:0000312|WormBase:C33F10.5d};
IsoId=H2KZ60-1; Sequence=Displayed;
Name=a {ECO:0000312|WormBase:C33F10.5a};
IsoId=H2KZ60-2; Sequence=VSP_058505;
Name=b {ECO:0000312|WormBase:C33F10.5b};
IsoId=H2KZ60-3; Sequence=VSP_058506;
Name=c {ECO:0000312|WormBase:C33F10.5c};
IsoId=H2KZ60-4; Sequence=VSP_058504;
-!- TISSUE SPECIFICITY: Expressed in neurons including the I1 and I3
pharyngeal interneurons, NSM and VNC motor neurons, HSN and CAN
neurons, the ALM and PLM touch receptor neurons and other
unidentified head neurons. Also expressed in somatic muscles, the
excretory canal, the excretory cell and the hypodermis.
{ECO:0000269|PubMed:23123963}.
-!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development
and adulthood. {ECO:0000269|PubMed:23123963}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in truncated
or shorter excretory canals, and also truncated ALM axons that
fail to extend above the nerve ring, truncated PLM processes and
abnormal VNC axon patterning. {ECO:0000269|PubMed:23123963}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
family. {ECO:0000305}.
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EMBL; BX284602; CCD66510.1; -; Genomic_DNA.
EMBL; BX284602; CCD66507.1; -; Genomic_DNA.
EMBL; BX284602; CCD66508.1; -; Genomic_DNA.
EMBL; BX284602; CCD66509.1; -; Genomic_DNA.
PIR; T15746; T15746.
RefSeq; NP_001022014.1; NM_001026843.3. [H2KZ60-1]
RefSeq; NP_494861.1; NM_062460.3.
RefSeq; NP_494862.1; NM_062461.4.
RefSeq; NP_740979.1; NM_170981.4. [H2KZ60-4]
UniGene; Cel.5466; -.
ProteinModelPortal; H2KZ60; -.
SMR; H2KZ60; -.
STRING; 6239.C33F10.5b; -.
EPD; H2KZ60; -.
PeptideAtlas; H2KZ60; -.
EnsemblMetazoa; C33F10.5d; C33F10.5d; WBGene00016354. [H2KZ60-1]
GeneID; 173828; -.
KEGG; cel:CELE_C33F10.5; -.
UCSC; C33F10.5c.1; c. elegans.
CTD; 173828; -.
WormBase; C33F10.5a; CE04138; WBGene00016354; rig-6. [H2KZ60-2]
WormBase; C33F10.5b; CE25803; WBGene00016354; rig-6. [H2KZ60-3]
WormBase; C33F10.5c; CE31679; WBGene00016354; rig-6. [H2KZ60-4]
WormBase; C33F10.5d; CE37327; WBGene00016354; rig-6. [H2KZ60-1]
eggNOG; KOG3513; Eukaryota.
eggNOG; ENOG410XSVG; LUCA.
GeneTree; ENSGT00910000145169; -.
HOGENOM; HOG000021866; -.
InParanoid; Q9BIA2; -.
OMA; NISWTWD; -.
OrthoDB; EOG091G00TE; -.
PRO; PR:H2KZ60; -.
Proteomes; UP000001940; Chromosome II.
Bgee; WBGene00016354; -.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0035545; P:determination of left/right asymmetry in nervous system; IMP:UniProtKB.
GO; GO:0033563; P:dorsal/ventral axon guidance; IMP:UniProtKB.
GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
GO; GO:0060562; P:epithelial tube morphogenesis; IMP:UniProtKB.
GO; GO:0008045; P:motor neuron axon guidance; IMP:UniProtKB.
GO; GO:2000747; P:negative regulation of defecation rhythm; IMP:UniProtKB.
GO; GO:0060467; P:negative regulation of fertilization; IMP:UniProtKB.
GO; GO:0090327; P:negative regulation of locomotion involved in locomotory behavior; IMP:UniProtKB.
GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:UniProtKB.
GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IMP:UniProtKB.
GO; GO:1903356; P:positive regulation of distal tip cell migration; IMP:UniProtKB.
GO; GO:0035150; P:regulation of tube size; IMP:UniProtKB.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 8.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
Pfam; PF00041; fn3; 1.
Pfam; PF07679; I-set; 2.
Pfam; PF13895; Ig_2; 1.
SMART; SM00060; FN3; 4.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 4.
SUPFAM; SSF48726; SSF48726; 6.
SUPFAM; SSF49265; SSF49265; 2.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS50853; FN3; 4.
PROSITE; PS50835; IG_LIKE; 6.
2: Evidence at transcript level;
Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
Cell projection; Complete proteome; Disulfide bond; Glycoprotein;
GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
Neurogenesis; Reference proteome; Repeat; Signal; Synapse;
Transmembrane; Transmembrane helix.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 1177 Contactin rig-6. {ECO:0000305}.
/FTId=PRO_5003564315.
PROPEP 1178 1196 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000437246.
TRANSMEM 1174 1194 Helical. {ECO:0000255}.
DOMAIN 144 225 Ig-like C2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 232 319 Ig-like C2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 355 438 Ig-like C2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 441 533 Ig-like C2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 539 626 Ig-like C2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 631 730 Ig-like C2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
DOMAIN 736 844 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 849 961 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 963 1057 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1064 1168 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
LIPID 1177 1177 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 195 195 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 343 343 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 457 457 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 644 644 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 895 895 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 925 925 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 945 945 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 974 974 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 979 979 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 986 986 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1002 1002 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 1092 1092 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 169 220 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 263 316 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 372 420 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 462 517 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 562 610 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 653 718 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 422 Missing (in isoform c). {ECO:0000305}.
/FTId=VSP_058504.
VAR_SEQ 1 313 MMMLIRCISIFLLFGFVNALIDEASCPIGWQIASDQCVRIV
IAPANLKHSKKYCHHEGGELMDTSVTLLLEDVMDLLKNLHE
NGLSEPTFHVGGMGQALNRTEDGNYKIITINPSSHFPFICS
LNKMARRSLLFQQKLLPVGAPQISLTGQSEIYFHPRHDADY
IALPCTVQGNPKPTVAWYKNDVEVLSPSMSNVSYLLSGGNL
LVPASSTLAYSSFHCTARNSLGEVRSPPILLKPSFIDPFRP
HRLDVYSLATGGAKLDCDAPAHQPKSLTYSWLYGSSTDRIL
SQNERKFISLDGTLFFSYVTAEDEDS -> MFSLLFLKCSH
LKVKRGTQEFLVWFSFTISLALLFYPNLVQIFKSTTSIPNI
PKVWWCLFPSSNPITLWSYAQTRTDRSFF (in isoform
a). {ECO:0000305}.
/FTId=VSP_058505.
VAR_SEQ 1 22 MMMLIRCISIFLLFGFVNALID -> MRISKKTILSAYEVI
DVGNKAADSPTISKMLSENFGLKFFSIKRFLAMKYSNH
(in isoform b). {ECO:0000305}.
/FTId=VSP_058506.
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


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