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Protein

Nectin-3

Gene

Nectin3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in cell-cell adhesion through heterophilic trans-interactions with nectins-like or other nectins, such as trans-interaction with NECTIN2 at Sertoli-spermatid junctions. Trans-interaction with PVR induces activation of CDC42 and RAC small G proteins through common signaling molecules such as SRC and RAP1. Also involved in the formation of cell-cell junctions, including adherens junctions and synapses. Induces endocytosis-mediated down-regulation of PVR from the cell surface, resulting in reduction of cell movement and proliferation. Plays a role in the morphology of the ciliary body.5 Publications

GO - Molecular functioni

  • cell adhesion molecule binding Source: MGI
  • protein homodimerization activity Source: HGNC

GO - Biological processi

  • cell adhesion Source: MGI
  • fertilization Source: MGI
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: HGNC
  • lens morphogenesis in camera-type eye Source: MGI
  • retina morphogenesis in camera-type eye Source: MGI
  • single organismal cell-cell adhesion Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-418990. Adherens junctions interactions.
R-MMU-420597. Nectin/Necl trans heterodimerization.

Names & Taxonomyi

Protein namesi
Recommended name:
Nectin-3
Alternative name(s):
Nectin cell adhesion molecule 3By similarity
Poliovirus receptor-related protein 3
CD_antigen: CD113
Gene namesi
Name:Nectin3By similarity
Synonyms:Pvrl3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1930171. Pvrl3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini58 – 404347ExtracellularSequence analysisAdd
BLAST
Transmembranei405 – 42521HelicalSequence analysisAdd
BLAST
Topological domaini426 – 549124CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • apical junction complex Source: MGI
  • cell-cell adherens junction Source: MGI
  • cell-cell junction Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: HGNC
  • postsynaptic membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

Mice show an ocular phenotype, microphthalmia, accompanied by a separation of the contact between the pigment and non-pigment cell layers of the ciliary epithelia. Male mice exhibits infertility, suggesting a role in spermatogenesis. In the hippocampus, the formation and the number of adherens junctions at the synapses is impaired, and the trajectory of mossy fiber is abnormal.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5757Sequence analysisAdd
BLAST
Chaini58 – 549492Nectin-3PRO_0000226373Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi73 – 731N-linked (GlcNAc...)Sequence analysis
Disulfide bondi78 ↔ 148PROSITE-ProRule annotation
Glycosylationi83 – 831N-linked (GlcNAc...)Sequence analysis
Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence analysis
Glycosylationi186 – 1861N-linked (GlcNAc...)Sequence analysis
Disulfide bondi193 ↔ 246PROSITE-ProRule annotation
Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence analysis
Disulfide bondi291 ↔ 338PROSITE-ProRule annotation
Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9JLB9.
PaxDbiQ9JLB9.
PRIDEiQ9JLB9.

PTM databases

iPTMnetiQ9JLB9.
PhosphoSiteiQ9JLB9.

Expressioni

Tissue specificityi

Ubiquitous with high expression in testes. Localized in spermatids at Sertoli-spermatid junctions. Expressed in ovarian granulosa cells, but only faintly expressed after ovulation.2 Publications

Gene expression databases

BgeeiQ9JLB9.
CleanExiMM_PVRL3.
ExpressionAtlasiQ9JLB9. baseline and differential.
GenevisibleiQ9JLB9. MM.

Interactioni

Subunit structurei

Cis- and trans-homodimer. Can form trans-heterodimers with NECTIN1, NECTIN2, PVR, IGSF4B/Necl-1 and with IGSF4. Interaction between NECTIN1 and NECTIN3 on the pre- and postsynaptic sites, respectively, initiates the formation of puncta adherentia junctions between axons and dendrites. Interacts (via Cytoplasmic domain) with MLLT4/afadin, providing a connection with the actin cytoskeleton. Binds with low affinity to TIGIT.5 Publications

GO - Molecular functioni

  • cell adhesion molecule binding Source: MGI
  • protein homodimerization activity Source: HGNC

Protein-protein interaction databases

DIPiDIP-41729N.
IntActiQ9JLB9. 2 interactions.
MINTiMINT-254672.
STRINGi10090.ENSMUSP00000023334.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AXAX-ray2.78A/B544-549[»]
ProteinModelPortaliQ9JLB9.
SMRiQ9JLB9. Positions 58-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 165108Ig-like V-typeAdd
BLAST
Domaini170 – 25889Ig-like C2-type 1Add
BLAST
Domaini269 – 35486Ig-like C2-type 2Add
BLAST

Sequence similaritiesi

Belongs to the nectin family.Curated

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IGR7. Eukaryota.
ENOG410ZRVN. LUCA.
GeneTreeiENSGT00770000120512.
HOGENOMiHOG000115805.
HOVERGENiHBG082234.
InParanoidiQ9JLB9.
KOiK06592.
OMAiSKNTFAP.
OrthoDBiEOG73RBB5.
PhylomeDBiQ9JLB9.
TreeFamiTF331051.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR033319. Nectin-3.
[Graphical view]
PANTHERiPTHR23277:SF12. PTHR23277:SF12. 1 hit.
PfamiPF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JLB9-1) [UniParc]FASTAAdd to basket

Also known as: Nectin-3 alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MARTPGPAPL CPGGGKAQLS SAFPPAAGLL LPAPTPPPLL LLLIPLLLFS
60 70 80 90 100
RLCGALAGSI IVEPHVTAVW GKNVSLKCLI EVNETITQIS WEKIHGKSTQ
110 120 130 140 150
TVAVHHPQYG FSVQGDYQGR VLFKNYSLND ATITLHNIGF SDSGKYICKA
160 170 180 190 200
VTFPLGNAQS STTVTVLVEP TVSLIKGPDS LIDGGNETVA AVCVAATGKP
210 220 230 240 250
VAQIDWEGDL GEMESSTTSF PNETATIVSQ YKLFPTRFAR GRRITCVVKH
260 270 280 290 300
PALEKDIRYS FILDIQYAPE VSVTGYDGNW FVGRKGVNLK CNADANPPPF
310 320 330 340 350
KSVWSRLDGQ WPDGLLASDN TLHFVHPLTV NYSGVYVCKV SNSLGQRSDQ
360 370 380 390 400
KVIYISDPPT TTTLQPTVQW HSSPADVQDI ATEHKKLPFP LSTLATLKDD
410 420 430 440 450
TIGTIIASVV GGALFLVLVS ILAGVFCYRR RRTFRGDYFA KNYIPPSDMQ
460 470 480 490 500
KESQIDVLHQ DELDSYPDSV KKENKNPVNN LIRKDYLEEP EKTQWNNVEN
510 520 530 540
LTRFERPMDY YEDLKMGMKF VSDERYNESE DGLVSHVDGS VISRREWYV
Length:549
Mass (Da):60,583
Last modified:October 1, 2000 - v1
Checksum:i5492C9ABB472F185
GO
Isoform 2 (identifier: Q9JLB9-2) [UniParc]FASTAAdd to basket

Also known as: Nectin-3 beta

The sequence of this isoform differs from the canonical sequence as follows:
     358-510: PPTTTTLQPT...LTRFERPMDY → IPLTQTSSIA...LYINPREHYV
     511-549: Missing.

Show »
Length:510
Mass (Da):55,811
Checksum:i45CFE6EF78454864
GO
Isoform 3 (identifier: Q9JLB9-3) [UniParc]FASTAAdd to basket

Also known as: Nectin-3 gamma

The sequence of this isoform differs from the canonical sequence as follows:
     358-438: PPTTTTLQPT...RRRRTFRGDY → IPLTQTSSIA...LGQVRALEDT
     439-549: Missing.

Show »
Length:438
Mass (Da):47,262
Checksum:i2A0A4416E5B02FEF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1811L → S in BAB27933 (PubMed:16141072).Curated
Sequence conflicti195 – 1962AA → SS in BAB27933 (PubMed:16141072).Curated
Sequence conflicti213 – 2219MESSTTSFP → REFSTISFL in BAB27933 (PubMed:16141072).Curated
Sequence conflicti232 – 2321K → E in BAB27933 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei358 – 510153PPTTT…RPMDY → IPLTQTSSIAVAGAVIGAVL ALFIITVFVTVLLTPRKKRP SYLDKVIDLPPTHKPPPVYE ERIPSLPQKDLLGQTEHLPL QTQFKEKGAGGLQPSNGPIS RRFDYEDESTMQEDGTQRMC PLYSQMCHQDRSPRQHHPRN PERLYINPREHYV in isoform 2. 1 PublicationVSP_017437Add
BLAST
Alternative sequencei358 – 43881PPTTT…FRGDY → IPLTQTSSIAVAGAVIGAVL ALFIITVFVTVLLTPRKKRP SYLDKVIDLPPTHKPPPVYE ERIPSLPQKDLLGQVRALED T in isoform 3. 2 PublicationsVSP_017438Add
BLAST
Alternative sequencei439 – 549111Missing in isoform 3. 2 PublicationsVSP_017439Add
BLAST
Alternative sequencei511 – 54939Missing in isoform 2. 1 PublicationVSP_017440Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195833 mRNA. Translation: AAF63685.1.
AF195834 mRNA. Translation: AAF63686.1.
AF195835 mRNA. Translation: AAF63687.1.
AK011949 mRNA. Translation: BAB27933.1.
BC125588 mRNA. Translation: AAI25589.1.
BC132187 mRNA. Translation: AAI32188.1.
CCDSiCCDS28204.1. [Q9JLB9-2]
CCDS28205.1. [Q9JLB9-3]
CCDS28206.1. [Q9JLB9-1]
RefSeqiNP_067470.1. NM_021495.4. [Q9JLB9-1]
NP_067471.1. NM_021496.3. [Q9JLB9-2]
NP_067472.1. NM_021497.2. [Q9JLB9-3]
UniGeneiMm.328072.

Genome annotation databases

EnsembliENSMUST00000023334; ENSMUSP00000023334; ENSMUSG00000022656. [Q9JLB9-1]
ENSMUST00000023335; ENSMUSP00000023335; ENSMUSG00000022656. [Q9JLB9-2]
ENSMUST00000096052; ENSMUSP00000093757; ENSMUSG00000022656. [Q9JLB9-3]
GeneIDi58998.
KEGGimmu:58998.
UCSCiuc007zji.3. mouse. [Q9JLB9-2]
uc007zjj.2. mouse. [Q9JLB9-3]
uc007zjk.3. mouse. [Q9JLB9-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF195833 mRNA. Translation: AAF63685.1.
AF195834 mRNA. Translation: AAF63686.1.
AF195835 mRNA. Translation: AAF63687.1.
AK011949 mRNA. Translation: BAB27933.1.
BC125588 mRNA. Translation: AAI25589.1.
BC132187 mRNA. Translation: AAI32188.1.
CCDSiCCDS28204.1. [Q9JLB9-2]
CCDS28205.1. [Q9JLB9-3]
CCDS28206.1. [Q9JLB9-1]
RefSeqiNP_067470.1. NM_021495.4. [Q9JLB9-1]
NP_067471.1. NM_021496.3. [Q9JLB9-2]
NP_067472.1. NM_021497.2. [Q9JLB9-3]
UniGeneiMm.328072.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AXAX-ray2.78A/B544-549[»]
ProteinModelPortaliQ9JLB9.
SMRiQ9JLB9. Positions 58-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-41729N.
IntActiQ9JLB9. 2 interactions.
MINTiMINT-254672.
STRINGi10090.ENSMUSP00000023334.

PTM databases

iPTMnetiQ9JLB9.
PhosphoSiteiQ9JLB9.

Proteomic databases

MaxQBiQ9JLB9.
PaxDbiQ9JLB9.
PRIDEiQ9JLB9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023334; ENSMUSP00000023334; ENSMUSG00000022656. [Q9JLB9-1]
ENSMUST00000023335; ENSMUSP00000023335; ENSMUSG00000022656. [Q9JLB9-2]
ENSMUST00000096052; ENSMUSP00000093757; ENSMUSG00000022656. [Q9JLB9-3]
GeneIDi58998.
KEGGimmu:58998.
UCSCiuc007zji.3. mouse. [Q9JLB9-2]
uc007zjj.2. mouse. [Q9JLB9-3]
uc007zjk.3. mouse. [Q9JLB9-1]

Organism-specific databases

CTDi58998.
MGIiMGI:1930171. Pvrl3.

Phylogenomic databases

eggNOGiENOG410IGR7. Eukaryota.
ENOG410ZRVN. LUCA.
GeneTreeiENSGT00770000120512.
HOGENOMiHOG000115805.
HOVERGENiHBG082234.
InParanoidiQ9JLB9.
KOiK06592.
OMAiSKNTFAP.
OrthoDBiEOG73RBB5.
PhylomeDBiQ9JLB9.
TreeFamiTF331051.

Enzyme and pathway databases

ReactomeiR-MMU-418990. Adherens junctions interactions.
R-MMU-420597. Nectin/Necl trans heterodimerization.

Miscellaneous databases

NextBioi314506.
PROiQ9JLB9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JLB9.
CleanExiMM_PVRL3.
ExpressionAtlasiQ9JLB9. baseline and differential.
GenevisibleiQ9JLB9. MM.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR013162. CD80_C2-set.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR033319. Nectin-3.
[Graphical view]
PANTHERiPTHR23277:SF12. PTHR23277:SF12. 1 hit.
PfamiPF08205. C2-set_2. 1 hit.
PF07686. V-set. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nectin-3: a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities."
    Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M., Nishimura M., Tachibana K., Mizoguchi A., Takai Y.
    J. Biol. Chem. 275:10291-10299(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBUNIT, TISSUE SPECIFICITY, FUNCTION.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Brain.
  4. "Nectin couples cell-cell adhesion and the actin scaffold at heterotypic testicular junctions."
    Ozaki-Kuroda K., Nakanishi H., Ohta H., Tanaka H., Kurihara H., Mueller S., Irie K., Ikeda W., Sakai T., Wimmer E., Nishimune Y., Takai Y.
    Curr. Biol. 12:1145-1150(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  5. Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  6. "Antagonistic and agonistic effects of an extracellular fragment of nectin on formation of E-cadherin-based cell-cell adhesion."
    Honda T., Shimizu K., Kawakatsu T., Yasumi M., Shingai T., Fukuhara A., Ozaki-Kuroda K., Irie K., Nakanishi H., Takai Y.
    Genes Cells 8:51-63(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Implications of nectin-like molecule-2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion and transmembrane protein localization in epithelial cells."
    Shingai T., Ikeda W., Kakunaga S., Morimoto K., Takekuni K., Itoh S., Satoh K., Takeuchi M., Imai T., Monden M., Takai Y.
    J. Biol. Chem. 278:35421-35427(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGSF4.
  8. "Common signaling pathway is used by the trans-interaction of Necl-5/Tage4/PVR/CD155 and nectin, and of nectin and nectin during the formation of cell-cell adhesion."
    Sato T., Irie K., Okamoto R., Ooshio T., Fujita N., Takai Y.
    Cancer Sci. 96:578-589(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PVR.
  9. "Roles of cell-adhesion molecules nectin 1 and nectin 3 in ciliary body development."
    Inagaki M., Irie K., Ishizaki H., Tanaka-Okamoto M., Morimoto K., Inoue E., Ohtsuka T., Miyoshi J., Takai Y.
    Development 132:1525-1537(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  10. "Nectin-like molecule-1/TSLL1/SynCAM3: a neural tissue-specific immunoglobulin-like cell-cell adhesion molecule localizing at non-junctional contact sites of presynaptic nerve terminals, axons and glia cell processes."
    Kakunaga S., Ikeda W., Itoh S., Deguchi-Tawarada M., Ohtsuka T., Mizoguchi A., Takai Y.
    J. Cell Sci. 118:1267-1277(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGSF4B.
  11. "Involvement of nectins in the formation of puncta adherentia junctions and the mossy fiber trajectory in the mouse hippocampus."
    Honda T., Sakisaka T., Yamada T., Kumazawa N., Hoshino T., Kajita M., Kayahara T., Ishizaki H., Tanaka-Okamoto M., Mizoguchi A., Manabe T., Miyoshi J., Takai Y.
    Mol. Cell. Neurosci. 31:315-325(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Lung and Testis.

Entry informationi

Entry nameiNECT3_MOUSE
AccessioniPrimary (citable) accession number: Q9JLB9
Secondary accession number(s): Q059N7
, Q9D006, Q9JLB7, Q9JLB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.