ID Q8MQ86_CAEEL Unreviewed; 955 AA.
AC Q8MQ86;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 176.
DE SubName: Full=NCAM (Neural cell adhesion molecule) homolog {ECO:0000313|EMBL:CCD68929.1};
GN Name=ncam-1 {ECO:0000313|EMBL:CCD68929.1,
GN ECO:0000313|WormBase:F02G3.1c};
GN ORFNames=CELE_F02G3.1 {ECO:0000313|EMBL:CCD68929.1}, F02G3.1
GN {ECO:0000313|WormBase:F02G3.1c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD68929.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD68929.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD68929.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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DR EMBL; BX284606; CCD68929.1; -; Genomic_DNA.
DR RefSeq; NP_741709.1; NM_171617.3.
DR AlphaFoldDB; Q8MQ86; -.
DR STRING; 6239.F02G3.1c.1; -.
DR EPD; Q8MQ86; -.
DR PaxDb; 6239-F02G3-1c; -.
DR PeptideAtlas; Q8MQ86; -.
DR EnsemblMetazoa; F02G3.1c.1; F02G3.1c.1; WBGene00017184.
DR GeneID; 180418; -.
DR UCSC; F02G3.1b; c. elegans.
DR AGR; WB:WBGene00017184; -.
DR WormBase; F02G3.1c; CE30935; WBGene00017184; ncam-1.
DR eggNOG; KOG4475; Eukaryota.
DR InParanoid; Q8MQ86; -.
DR OMA; NCNAAQY; -.
DR OrthoDB; 5233206at2759; -.
DR PhylomeDB; Q8MQ86; -.
DR Reactome; R-CEL-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00017184; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR ExpressionAtlas; Q8MQ86; baseline and differential.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00096; Ig; 3.
DR Gene3D; 2.60.40.10; Immunoglobulins; 7.
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 InterPro; IPR009138; Neural_cell_adh.
DR PANTHER; PTHR45080; CONTACTIN 5; 1.
DR PANTHER; PTHR45080:SF8; WRAPPER_REGA-1_KLINGON HOMOLOG; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF13927; Ig_3; 2.
DR PRINTS; PR01838; NCAMFAMILY.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 5.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Proteomics identification {ECO:0007829|EPD:Q8MQ86,
KW ECO:0007829|PeptideAtlas:Q8MQ86};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 889..910
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..142
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 147..236
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 241..329
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 334..500
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 505..596
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 603..704
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 379..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 106398 MW; 4E61C6A8B2A2DF75 CRC64;
MTLCLRCSSN LNYKQCAIVR FSSEVENGNR RIILIFFLLL LLILSGWTLS LSPTEERLQN
RRSGDNFLVV CKVKDFDGAA SDAKIEWYRD GKLIPRFGST MTIERTYSNQ LMINRPKISD
GGKYTCKTEI QGEQQEVSAE ISFVDPPKFL NVQESQHPEE GTRAEIVCEV EGTDQLEVFW
QFNGVTLDET SQRGYEFSEN NQILYIPHFT AKKDDGIYNC NAAQYSSFET LSVNVTGYAR
PTITVFDVPN GNRGIEGHTI ELKCGAVGKP KPTYKWFFED DEVPIARSDK HNVEEGLLII
ESLNSEDAGT YKCVANNTVG SNERTFDLAV FLKPKVDLKH EYVVKEGDDV ELVCSYHGEG
HVTAKFVSGH SEFAVRNEAV SAGNSEEIRP ESNESEEVTT TSENSEETST QDEVELKSAE
NVNDEEDHTS QQDDGEQDEQ EESKKWKRFA DDVNNQRISV RAEENKLILT IKSISLEDAA
DYTCAVSNDA GTVNKVTQVG IIHPPTLRHY TGPHIRSFDG NTVSVYCDVS AVPSPKWHWF
KNGKEVEANG VSIQIFTQGS STKLTLENFD GSDNFGVYTC RADNGVGQLE KQIDVIKVVS
PATPSGMNCK KMVYPNYGKC SFESDIYEKE ESKPQTMELL VAKLEEMESD YNWSHAQPVS
VPFEDDLTIP NLTSNTQYVI KARAVNEAGS SEYSEEISLE TTDPWAPQAP GSVAMKCSDY
CTVSWDTPND HGSPLLKFKV TIQEMKYKTD DDEVEEKSDE KSNNNSEETE TTTSDDNDET
EASNESIEIK ENSEEQETTL AHEDSAEILP TDPSTSVERD EMVPYGSLLV LNVDSEENQV
QLTNIKQHSY YKISVAAENE KGQGEPAEID FQTDDSPTKY EEGIDSTHLI IAIAIGVLFL
LLLVDLGCFI TNKCGLISCI CLNLCGKNAG AKQRDLESGR GGPESNRLLD SSGAR
//
