NECT3_DANRE
ID NECT3_DANRE Reviewed; 574 AA.
AC Q58EG3; A4JYI1; A4JYN6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Nectin-3-like protein;
DE AltName: Full=Nectin cell adhesion molecule 3 {ECO:0000250|UniProtKB:Q9NQS3};
DE AltName: Full=Poliovirus receptor-related protein 3-like;
DE Flags: Precursor;
GN Name=nectin3 {ECO:0000250|UniProtKB:Q9NQS3}; Synonyms=pvrl3l;
GN ORFNames=si:dkey-62a13.5, zgc:113035;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18296487; DOI=10.1101/gr.7187808;
RA Bushell K.M., Soellner C., Schuster-Boeckler B., Bateman A., Wright G.J.;
RT "Large-scale screening for novel low-affinity extracellular protein
RT interactions.";
RL Genome Res. 18:622-630(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in cell-cell adhesion. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM73163.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CU458902; CAM73163.1; ALT_FRAME; mRNA.
DR EMBL; CU458957; CAM73218.1; -; mRNA.
DR EMBL; CR391925; CAX13156.1; -; Genomic_DNA.
DR EMBL; BC091923; AAH91923.1; -; mRNA.
DR RefSeq; NP_001014326.1; NM_001014304.1.
DR AlphaFoldDB; Q58EG3; -.
DR SMR; Q58EG3; -.
DR STRING; 7955.ENSDARP00000121706; -.
DR PaxDb; Q58EG3; -.
DR PRIDE; Q58EG3; -.
DR Ensembl; ENSDART00000031205; ENSDARP00000028921; ENSDARG00000006604.
DR Ensembl; ENSDART00000147593; ENSDARP00000121706; ENSDARG00000006604.
DR GeneID; 541491; -.
DR KEGG; dre:541491; -.
DR CTD; 541491; -.
DR ZFIN; ZDB-GENE-050327-14; nectin3b.
DR eggNOG; ENOG502QTRU; Eukaryota.
DR GeneTree; ENSGT00940000156028; -.
DR HOGENOM; CLU_029618_3_0_1; -.
DR InParanoid; Q58EG3; -.
DR OMA; RCARYPH; -.
DR OrthoDB; 509401at2759; -.
DR PhylomeDB; Q58EG3; -.
DR TreeFam; TF331051; -.
DR Reactome; R-DRE-418990; Adherens junctions interactions.
DR Reactome; R-DRE-420597; Nectin/Necl trans heterodimerization.
DR PRO; PR:Q58EG3; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 21.
DR Bgee; ENSDARG00000006604; Expressed in cleaving embryo and 30 other tissues.
DR ExpressionAtlas; Q58EG3; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0043296; C:apical junction complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050839; F:cell adhesion molecule binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:InterPro.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IEA:InterPro.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR033319; Nectin-3.
DR PANTHER; PTHR23277:SF12; PTHR23277:SF12; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..574
FT /note="Nectin-3-like protein"
FT /id="PRO_0000226374"
FT TOPO_DOM 36..387
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..146
FT /note="Ig-like V-type"
FT DOMAIN 151..240
FT /note="Ig-like C2-type 1"
FT DOMAIN 251..336
FT /note="Ig-like C2-type 2"
FT REGION 442..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 174..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 273..320
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 21
FT /note="L -> V (in Ref. 1; CAM73163 and 3; AAH91923)"
FT /evidence="ECO:0000305"
FT CONFLICT 516
FT /note="Q -> H (in Ref. 1; CAM73163 and 3; AAH91923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 63995 MW; 6283CE7CC3004EA5 CRC64;
MALTMTAHFL RNNPIQLGLN LRVLLMLSFV SGLVYGSQVI VPPKVNAVLG KNVTLSCRVQ
VDTNLSLTQS SWERKLPNGW VTLAVYNPMF GISIPPDYER RLSFRSPSAL DATIMLEDVG
FADIGVYTCK VATFPLGNTQ ASTTVSVLVE PKVYVSAGSS ALIDGGNETT VATCIAERAR
PPADVSWETN LYGMSEAHMQ EDANGTTTTQ VHYIWQPSRH AQGHTLTCVV KHPALQSDFR
IPYIINVQFA PDILVLGYDG DWYVGRENVQ LKCRAKANPP AQHFRWIRLD GEMPNGAERV
NNTLVFTRPL QKNDSGVYRC EVANDIGLHS RDIRIRIQDP PSTTTMPPTT PVRLLTADIS
ATAPGNKQRA LITSPTLAPL HEGSLGTIVG GAVGGALFLL LLLILAGVYY QRQRRTFRGD
YYTKQYHGPS DMQKAPQPHE LQQVYSKGSP DTKLKSNQDN GTIYPDKDRE EWGDFDRERS
PNGRSRALRE AGQLNHHNHQ NHEHGFHSNH HTGHPQSYSP AHHIQRSSLQ PQPRRYPAPQ
VMSNGSPYLP EDCYDNEYVS HTDGSMISRR EWYV
