NECT4_MOUSE
ID NECT4_MOUSE Reviewed; 508 AA.
AC Q8R007; Q3U318; Q8CED8; Q9DBP8;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Nectin-4;
DE AltName: Full=Ig superfamily receptor LNIR;
DE AltName: Full=Nectin cell adhesion molecule 4 {ECO:0000250|UniProtKB:Q96NY8};
DE AltName: Full=Poliovirus receptor-related protein 4;
DE Flags: Precursor;
GN Name=Nectin4 {ECO:0000250|UniProtKB:Q96NY8}; Synonyms=Lnir, Prr4, Pvrl4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=11544254; DOI=10.1074/jbc.m103810200;
RA Reymond N., Fabre S., Lecocq E., Adelaide J., Dubreuil P., Lopez M.;
RT "Nectin4/PRR4, a new afadin-associated member of the nectin family that
RT trans-interacts with nectin1/PRR1 through V domain interaction.";
RL J. Biol. Chem. 276:43205-43215(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Lung, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Seems to be involved in cell adhesion through trans-
CC homophilic and -heterophilic interactions, the latter including
CC specifically interactions with NECTIN1. {ECO:0000250}.
CC -!- SUBUNIT: Self-associates. Interacts via its Ig-like V-type domain with
CC NECTIN1 Ig-like V-type domain. Interacts via its C-terminus with AFDN
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q96NY8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R007-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R007-2; Sequence=VSP_027336;
CC -!- TISSUE SPECIFICITY: Expressed in brain, lung, testis and embryo.
CC {ECO:0000269|PubMed:11544254}.
CC -!- DEVELOPMENTAL STAGE: Detected at embryonic days 11, 15 and 17.
CC {ECO:0000269|PubMed:11544254}.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE32972.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF472510; AAL79833.1; -; mRNA.
DR EMBL; AK004821; BAB23592.1; -; mRNA.
DR EMBL; AK154983; BAE32972.1; ALT_INIT; mRNA.
DR EMBL; AK028479; BAC25972.1; -; mRNA.
DR EMBL; BC024948; AAH24948.1; -; mRNA.
DR CCDS; CCDS15493.1; -. [Q8R007-1]
DR CCDS; CCDS48442.1; -. [Q8R007-2]
DR RefSeq; NP_001116152.1; NM_001122680.1. [Q8R007-2]
DR RefSeq; NP_082169.2; NM_027893.3. [Q8R007-1]
DR AlphaFoldDB; Q8R007; -.
DR SMR; Q8R007; -.
DR BioGRID; 214892; 2.
DR DIP; DIP-59965N; -.
DR STRING; 10090.ENSMUSP00000006578; -.
DR GlyGen; Q8R007; 1 site.
DR iPTMnet; Q8R007; -.
DR PhosphoSitePlus; Q8R007; -.
DR MaxQB; Q8R007; -.
DR PaxDb; Q8R007; -.
DR PRIDE; Q8R007; -.
DR ProteomicsDB; 253055; -. [Q8R007-1]
DR ProteomicsDB; 253056; -. [Q8R007-2]
DR ABCD; Q8R007; 5 sequenced antibodies.
DR Antibodypedia; 2488; 252 antibodies from 32 providers.
DR DNASU; 71740; -.
DR Ensembl; ENSMUST00000006578; ENSMUSP00000006578; ENSMUSG00000006411. [Q8R007-1]
DR Ensembl; ENSMUST00000094325; ENSMUSP00000091883; ENSMUSG00000006411. [Q8R007-2]
DR Ensembl; ENSMUST00000111286; ENSMUSP00000106917; ENSMUSG00000006411. [Q8R007-1]
DR GeneID; 71740; -.
DR KEGG; mmu:71740; -.
DR UCSC; uc007dof.2; mouse. [Q8R007-1]
DR UCSC; uc011wwc.1; mouse. [Q8R007-2]
DR CTD; 81607; -.
DR MGI; MGI:1918990; Nectin4.
DR VEuPathDB; HostDB:ENSMUSG00000006411; -.
DR eggNOG; ENOG502R9I0; Eukaryota.
DR GeneTree; ENSGT00940000157535; -.
DR HOGENOM; CLU_029618_1_1_1; -.
DR InParanoid; Q8R007; -.
DR OMA; ASFTGQC; -.
DR OrthoDB; 509401at2759; -.
DR PhylomeDB; Q8R007; -.
DR TreeFam; TF338610; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR Reactome; R-MMU-420597; Nectin/Necl trans heterodimerization.
DR BioGRID-ORCS; 71740; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q8R007; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8R007; protein.
DR Bgee; ENSMUSG00000006411; Expressed in lip and 124 other tissues.
DR Genevisible; Q8R007; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
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:0046718; P:viral entry into host cell; 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; IPR033320; Nectin-4.
DR PANTHER; PTHR23277:SF11; PTHR23277:SF11; 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; 2.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..508
FT /note="Nectin-4"
FT /id="PRO_0000297674"
FT TOPO_DOM 31..347
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..143
FT /note="Ig-like V-type"
FT DOMAIN 147..236
FT /note="Ig-like C2-type 1"
FT DOMAIN 247..330
FT /note="Ig-like C2-type 2"
FT REGION 398..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 51..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 170..222
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 269..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 410..434
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027336"
FT CONFLICT 2
FT /note="P -> S (in Ref. 2; BAE32972)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="E -> Q (in Ref. 2; BAC25972)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 55657 MW; 24DAEBD21F22E376 CRC64;
MPLSLGAEMW GPEAWLRLLF LASFTGQYSA GELETSDVVT VVLGQDAKLP CFYRGDPDEQ
VGQVAWARVD PNEGIRELAL LHSKYGLHVN PAYEDRVEQP PPPRDPLDGS VLLRNAVQAD
EGEYECRVST FPAGSFQARM RLRVLVPPLP SLNPGPPLEE GQGLTLAASC TAEGSPAPSV
TWDTEVKGTQ SSRSFTHPRS AAVTSEFHLV PSRSMNGQPL TCVVSHPGLL QDRRITHTLQ
VAFLAEASVR GLEDQNLWQV GREGATLKCL SEGQPPPKYN WTRLDGPLPS GVRVKGDTLG
FPPLTTEHSG VYVCHVSNEL SSRDSQVTVE VLDPEDPGKQ VDLVSASVII VGVIAALLFC
LLVVVVVLMS RYHRRKAQQM TQKYEEELTL TRENSIRRLH SHHSDPRSQP EESVGLRAEG
HPDSLKDNSS CSVMSEEPEG RSYSTLTTVR EIETQTELLS PGSGRTEEDD DQDEGIKQAM
NHFVQENGTL RAKPTGNGIY INGRGHLV
