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Nectin-3 (Nectin cell adhesion molecule 3) (Poliovirus receptor-related protein 3) (CD antigen CD113)

 NECT3_MOUSE             Reviewed;         549 AA.
Q9JLB9; Q059N7; Q9D006; Q9JLB7; Q9JLB8;
07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
18-JUL-2018, entry version 136.
RecName: Full=Nectin-3;
AltName: Full=Nectin cell adhesion molecule 3 {ECO:0000250|UniProtKB:Q9NQS3};
AltName: Full=Poliovirus receptor-related protein 3;
AltName: CD_antigen=CD113;
Flags: Precursor;
Name=Nectin3 {ECO:0000250|UniProtKB:Q9NQS3}; Synonyms=Pvrl3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBUNIT, TISSUE
SPECIFICITY, AND FUNCTION.
PubMed=10744716; DOI=10.1074/jbc.275.14.10291;
Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M.,
Nishimura M., Tachibana K., Mizoguchi A., Takai Y.;
"Nectin-3: a new member of immunoglobulin-like cell adhesion molecules
that shows homophilic and heterophilic cell-cell adhesion
activities.";
J. Biol. Chem. 275:10291-10299(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12121624; DOI=10.1016/S0960-9822(02)00922-3;
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.;
"Nectin couples cell-cell adhesion and the actin scaffold at
heterotypic testicular junctions.";
Curr. Biol. 12:1145-1150(2002).
[5]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=11827984; DOI=10.1083/jcb.200103113;
Mizoguchi A., Nakanishi H., Kimura K., Matsubara K., Ozaki-Kuroda K.,
Katata T., Honda T., Kiyohara Y., Heo K., Higashi M., Tsutsumi T.,
Sonoda S., Ide C., Takai Y.;
"Nectin: an adhesion molecule involved in formation of synapses.";
J. Cell Biol. 156:555-565(2002).
[6]
FUNCTION.
PubMed=12558799; DOI=10.1046/j.1365-2443.2003.00616.x;
Honda T., Shimizu K., Kawakatsu T., Yasumi M., Shingai T.,
Fukuhara A., Ozaki-Kuroda K., Irie K., Nakanishi H., Takai Y.;
"Antagonistic and agonistic effects of an extracellular fragment of
nectin on formation of E-cadherin-based cell-cell adhesion.";
Genes Cells 8:51-63(2003).
[7]
INTERACTION WITH IGSF4.
PubMed=12826663; DOI=10.1074/jbc.M305387200;
Shingai T., Ikeda W., Kakunaga S., Morimoto K., Takekuni K., Itoh S.,
Satoh K., Takeuchi M., Imai T., Monden M., Takai Y.;
"Implications of nectin-like molecule-
2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion and
transmembrane protein localization in epithelial cells.";
J. Biol. Chem. 278:35421-35427(2003).
[8]
FUNCTION, AND INTERACTION WITH PVR.
PubMed=16128743; DOI=10.1111/j.1349-7006.2005.00087.x;
Sato T., Irie K., Okamoto R., Ooshio T., Fujita N., Takai Y.;
"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.";
Cancer Sci. 96:578-589(2005).
[9]
DISRUPTION PHENOTYPE.
PubMed=15728677; DOI=10.1242/dev.01697;
Inagaki M., Irie K., Ishizaki H., Tanaka-Okamoto M., Morimoto K.,
Inoue E., Ohtsuka T., Miyoshi J., Takai Y.;
"Roles of cell-adhesion molecules nectin 1 and nectin 3 in ciliary
body development.";
Development 132:1525-1537(2005).
[10]
INTERACTION WITH IGSF4B.
PubMed=15741237; DOI=10.1242/jcs.01656;
Kakunaga S., Ikeda W., Itoh S., Deguchi-Tawarada M., Ohtsuka T.,
Mizoguchi A., Takai Y.;
"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.";
J. Cell Sci. 118:1267-1277(2005).
[11]
DISRUPTION PHENOTYPE.
PubMed=16300961; DOI=10.1016/j.mcn.2005.10.002;
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.;
"Involvement of nectins in the formation of puncta adherentia
junctions and the mossy fiber trajectory in the mouse hippocampus.";
Mol. Cell. Neurosci. 31:315-325(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: 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. {ECO:0000269|PubMed:10744716,
ECO:0000269|PubMed:11827984, ECO:0000269|PubMed:12121624,
ECO:0000269|PubMed:12558799, ECO:0000269|PubMed:16128743}.
-!- SUBUNIT: 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 AFDN, providing a connection with
the actin cytoskeleton. Binds with low affinity to TIGIT.
{ECO:0000269|PubMed:10744716, ECO:0000269|PubMed:11827984,
ECO:0000269|PubMed:12826663, ECO:0000269|PubMed:15741237,
ECO:0000269|PubMed:16128743}.
-!- INTERACTION:
Q24008:inaD (xeno); NbExp=2; IntAct=EBI-4306755, EBI-195326;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
membrane protein {ECO:0000250}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000269|PubMed:11827984}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Nectin-3 alpha;
IsoId=Q9JLB9-1; Sequence=Displayed;
Name=2; Synonyms=Nectin-3 beta;
IsoId=Q9JLB9-2; Sequence=VSP_017437, VSP_017440;
Name=3; Synonyms=Nectin-3 gamma;
IsoId=Q9JLB9-3; Sequence=VSP_017438, VSP_017439;
-!- TISSUE SPECIFICITY: Ubiquitous with high expression in testes.
Localized in spermatids at Sertoli-spermatid junctions. Expressed
in ovarian granulosa cells, but only faintly expressed after
ovulation. {ECO:0000269|PubMed:10744716,
ECO:0000269|PubMed:12121624}.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:15728677, ECO:0000269|PubMed:16300961}.
-!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
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EMBL; AF195833; AAF63685.1; -; mRNA.
EMBL; AF195834; AAF63686.1; -; mRNA.
EMBL; AF195835; AAF63687.1; -; mRNA.
EMBL; AK011949; BAB27933.1; -; mRNA.
EMBL; BC125588; AAI25589.1; -; mRNA.
EMBL; BC132187; AAI32188.1; -; mRNA.
CCDS; CCDS28204.1; -. [Q9JLB9-2]
CCDS; CCDS28205.1; -. [Q9JLB9-3]
CCDS; CCDS28206.1; -. [Q9JLB9-1]
RefSeq; NP_067470.1; NM_021495.4. [Q9JLB9-1]
RefSeq; NP_067471.1; NM_021496.3. [Q9JLB9-2]
RefSeq; NP_067472.1; NM_021497.2. [Q9JLB9-3]
UniGene; Mm.328072; -.
UniGene; Mm.40477; -.
PDB; 3AXA; X-ray; 2.78 A; A/B=544-549.
PDB; 5B22; X-ray; 2.58 A; A/B=59-266.
PDBsum; 3AXA; -.
PDBsum; 5B22; -.
ProteinModelPortal; Q9JLB9; -.
SMR; Q9JLB9; -.
BioGrid; 208471; 1.
DIP; DIP-41729N; -.
IntAct; Q9JLB9; 4.
MINT; Q9JLB9; -.
STRING; 10090.ENSMUSP00000023334; -.
iPTMnet; Q9JLB9; -.
PhosphoSitePlus; Q9JLB9; -.
PaxDb; Q9JLB9; -.
PeptideAtlas; Q9JLB9; -.
PRIDE; Q9JLB9; -.
Ensembl; ENSMUST00000023334; ENSMUSP00000023334; ENSMUSG00000022656. [Q9JLB9-1]
Ensembl; ENSMUST00000023335; ENSMUSP00000023335; ENSMUSG00000022656. [Q9JLB9-2]
Ensembl; ENSMUST00000096052; ENSMUSP00000093757; ENSMUSG00000022656. [Q9JLB9-3]
GeneID; 58998; -.
KEGG; mmu:58998; -.
UCSC; uc007zji.3; mouse. [Q9JLB9-2]
UCSC; uc007zjj.2; mouse. [Q9JLB9-3]
UCSC; uc007zjk.3; mouse. [Q9JLB9-1]
CTD; 25945; -.
MGI; MGI:1930171; Nectin3.
eggNOG; ENOG410IGR7; Eukaryota.
eggNOG; ENOG410ZRVN; LUCA.
GeneTree; ENSGT00900000140811; -.
HOGENOM; HOG000115805; -.
HOVERGEN; HBG082234; -.
InParanoid; Q9JLB9; -.
KO; K06592; -.
OMA; DVPFKQT; -.
OrthoDB; EOG091G0BLQ; -.
PhylomeDB; Q9JLB9; -.
TreeFam; TF331051; -.
Reactome; R-MMU-418990; Adherens junctions interactions.
Reactome; R-MMU-420597; Nectin/Necl trans heterodimerization.
PRO; PR:Q9JLB9; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022656; -.
CleanEx; MM_PVRL3; -.
ExpressionAtlas; Q9JLB9; baseline and differential.
Genevisible; Q9JLB9; MM.
GO; GO:0043296; C:apical junction complex; IDA:MGI.
GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
GO; GO:0044291; C:cell-cell contact zone; IDA:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:HGNC.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0007155; P:cell adhesion; IDA:MGI.
GO; GO:0008037; P:cell recognition; IBA:GO_Central.
GO; GO:0098609; P:cell-cell adhesion; IDA:MGI.
GO; GO:0009566; P:fertilization; IMP:MGI.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:HGNC.
GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
GO; GO:1902414; P:protein localization to cell junction; IDA:MGI.
GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:MGI.
GO; GO:0007286; P:spermatid development; IEA:InterPro.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR013162; CD80_C2-set.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR033319; Nectin-3.
PANTHER; PTHR23277:SF12; PTHR23277:SF12; 1.
Pfam; PF08205; C2-set_2; 1.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SUPFAM; SSF48726; SSF48726; 3.
PROSITE; PS50835; IG_LIKE; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell junction;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
Immunoglobulin domain; Membrane; Postsynaptic cell membrane;
Reference proteome; Repeat; Signal; Synapse; Transmembrane;
Transmembrane helix.
SIGNAL 1 57 {ECO:0000255}.
CHAIN 58 549 Nectin-3.
/FTId=PRO_0000226373.
TOPO_DOM 58 404 Extracellular. {ECO:0000255}.
TRANSMEM 405 425 Helical. {ECO:0000255}.
TOPO_DOM 426 549 Cytoplasmic. {ECO:0000255}.
DOMAIN 58 165 Ig-like V-type.
DOMAIN 170 258 Ig-like C2-type 1.
DOMAIN 269 354 Ig-like C2-type 2.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 186 186 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 331 331 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 78 148 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 193 246 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 291 338 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 358 510 PPTTTTLQPTVQWHSSPADVQDIATEHKKLPFPLSTLATLK
DDTIGTIIASVVGGALFLVLVSILAGVFCYRRRRTFRGDYF
AKNYIPPSDMQKESQIDVLHQDELDSYPDSVKKENKNPVNN
LIRKDYLEEPEKTQWNNVENLTRFERPMDY -> IPLTQTS
SIAVAGAVIGAVLALFIITVFVTVLLTPRKKRPSYLDKVID
LPPTHKPPPVYEERIPSLPQKDLLGQTEHLPLQTQFKEKGA
GGLQPSNGPISRRFDYEDESTMQEDGTQRMCPLYSQMCHQD
RSPRQHHPRNPERLYINPREHYV (in isoform 2).
{ECO:0000303|PubMed:10744716}.
/FTId=VSP_017437.
VAR_SEQ 358 438 PPTTTTLQPTVQWHSSPADVQDIATEHKKLPFPLSTLATLK
DDTIGTIIASVVGGALFLVLVSILAGVFCYRRRRTFRGDY
-> IPLTQTSSIAVAGAVIGAVLALFIITVFVTVLLTPRKK
RPSYLDKVIDLPPTHKPPPVYEERIPSLPQKDLLGQVRALE
DT (in isoform 3).
{ECO:0000303|PubMed:10744716,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_017438.
VAR_SEQ 439 549 Missing (in isoform 3).
{ECO:0000303|PubMed:10744716,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_017439.
VAR_SEQ 511 549 Missing (in isoform 2).
{ECO:0000303|PubMed:10744716}.
/FTId=VSP_017440.
CONFLICT 181 181 L -> S (in Ref. 2; BAB27933).
{ECO:0000305}.
CONFLICT 195 196 AA -> SS (in Ref. 2; BAB27933).
{ECO:0000305}.
CONFLICT 213 221 MESSTTSFP -> REFSTISFL (in Ref. 2;
BAB27933). {ECO:0000305}.
CONFLICT 232 232 K -> E (in Ref. 2; BAB27933).
{ECO:0000305}.
STRAND 64 69 {ECO:0000244|PDB:5B22}.
STRAND 74 76 {ECO:0000244|PDB:5B22}.
STRAND 83 95 {ECO:0000244|PDB:5B22}.
STRAND 98 106 {ECO:0000244|PDB:5B22}.
TURN 107 109 {ECO:0000244|PDB:5B22}.
STRAND 110 113 {ECO:0000244|PDB:5B22}.
HELIX 115 117 {ECO:0000244|PDB:5B22}.
STRAND 120 124 {ECO:0000244|PDB:5B22}.
STRAND 133 135 {ECO:0000244|PDB:5B22}.
HELIX 140 142 {ECO:0000244|PDB:5B22}.
STRAND 144 153 {ECO:0000244|PDB:5B22}.
STRAND 156 168 {ECO:0000244|PDB:5B22}.
STRAND 171 175 {ECO:0000244|PDB:5B22}.
STRAND 188 200 {ECO:0000244|PDB:5B22}.
STRAND 203 210 {ECO:0000244|PDB:5B22}.
STRAND 212 219 {ECO:0000244|PDB:5B22}.
STRAND 225 233 {ECO:0000244|PDB:5B22}.
HELIX 237 239 {ECO:0000244|PDB:5B22}.
STRAND 243 249 {ECO:0000244|PDB:5B22}.
STRAND 257 262 {ECO:0000244|PDB:5B22}.
SEQUENCE 549 AA; 60583 MW; 5492C9ABB472F185 CRC64;
MARTPGPAPL CPGGGKAQLS SAFPPAAGLL LPAPTPPPLL LLLIPLLLFS RLCGALAGSI
IVEPHVTAVW GKNVSLKCLI EVNETITQIS WEKIHGKSTQ TVAVHHPQYG FSVQGDYQGR
VLFKNYSLND ATITLHNIGF SDSGKYICKA VTFPLGNAQS STTVTVLVEP TVSLIKGPDS
LIDGGNETVA AVCVAATGKP VAQIDWEGDL GEMESSTTSF PNETATIVSQ YKLFPTRFAR
GRRITCVVKH PALEKDIRYS FILDIQYAPE VSVTGYDGNW FVGRKGVNLK CNADANPPPF
KSVWSRLDGQ WPDGLLASDN TLHFVHPLTV NYSGVYVCKV SNSLGQRSDQ KVIYISDPPT
TTTLQPTVQW HSSPADVQDI ATEHKKLPFP LSTLATLKDD TIGTIIASVV GGALFLVLVS
ILAGVFCYRR RRTFRGDYFA KNYIPPSDMQ KESQIDVLHQ DELDSYPDSV KKENKNPVNN
LIRKDYLEEP EKTQWNNVEN LTRFERPMDY YEDLKMGMKF VSDERYNESE DGLVSHVDGS
VISRREWYV


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EIAAB05126 Brain immunoglobulin receptor,CADM3,Cell adhesion molecule 3,Homo sapiens,Human,IgSF4B,IGSF4B,Immunoglobulin superfamily member 4B,NECL1,NECL-1,Nectin-like protein 1,Synaptic cell adhesion molecule 3,
EIAAB05125 Cadm3,Cell adhesion molecule 3,IgSF4B,Igsf4b,Immunoglobulin superfamily member 4B,Mouse,Mus musculus,Necl1,NECL-1,Nectin-like protein 1,Synaptic cell adhesion molecule 3,Syncam3,TSLC1-like protein 1,T
EIAAB33218 Bos taurus,Bovine,Nectin-4,Poliovirus receptor-related protein 4,PVRL4
EIAAB33215 Mouse,Mus musculus,Nectin-3,Poliovirus receptor-related protein 3,Pvrl3
EIAAB33214 CDw113,Homo sapiens,Human,Nectin-3,Poliovirus receptor-related protein 3,PRR3,PVRL3
EIAAB33217 Ig superfamily receptor LNIR,Lnir,Mouse,Mus musculus,Nectin-4,Poliovirus receptor-related protein 4,Prr4,Pvrl4
20-272-191358 Nectin 2 - Rat monoclonal [502-57] to Nectin 2; Herpes virus entry mediator B; HveB; Nectin-2; CD112 antigen Monoclonal 0.05 mg
EIAAB33216 Homo sapiens,Human,Ig superfamily receptor LNIR,LNIR,Nectin-4,Poliovirus receptor-related protein 4,PRR4,PVRL4
'H00025945-P01-25 CD113 _ Nectin 3 antigen 25
'H00025945-P01-10 CD113 _ Nectin 3 antigen 10
'H00025945-Q01-10 CD113 _ Nectin 3 antigen 10
'H00025945-G01 CD113 _ Nectin 3 antigen 10
'H00025945-Q01-25 CD113 _ Nectin 3 antigen 25
EIAAB33213 Herpes virus entry mediator B,Herpesvirus entry mediator B,HveB,mHveB,Mouse,Mph,Murine herpes virus entry protein B,Mus musculus,Nectin-2,Poliovirus receptor homolog,Poliovirus receptor-related protei
EIAAB05127 Cadm3,Cell adhesion molecule 3,IgSF4B,Igsf4b,Immunoglobulin superfamily member 4B,Necl1,NECL-1,Nectin-like protein 1,Rat,Rattus norvegicus
EIAAB05123 Cadm2,Cell adhesion molecule 2,IgSF4D,Igsf4d,Immunoglobulin superfamily member 4D,Necl3,NECL-3,Nectin-like protein 3,Rat,Rattus norvegicus
EIAAB05124 Cadm2,Cell adhesion molecule 2,IgSF4D,Igsf4d,Immunoglobulin superfamily member 4D,Mouse,Mus musculus,Necl3,NECL-3,Nectin-like protein 3
EIAAB05128 Cadm4,Cell adhesion molecule 4,IgSF4C,Igsf4c,Immunoglobulin superfamily member 4C,Necl4,NECL-4,Nectin-like protein 4,Rat,Rattus norvegicus
EIAAB05122 CADM2,Cell adhesion molecule 2,Homo sapiens,Human,IgSF4D,IGSF4D,Immunoglobulin superfamily member 4D,NECL3,NECL-3,Nectin-like protein 3
EIAAB05129 Cadm4,Cell adhesion molecule 4,IgSF4C,Igsf4c,Immunoglobulin superfamily member 4C,Mouse,Mus musculus,Necl4,NECL-4,Nectin-like protein 4,TSLC1-like protein 2,Tsll2
EIAAB05130 CADM4,Cell adhesion molecule 4,Homo sapiens,Human,IgSF4C,IGSF4C,Immunoglobulin superfamily member 4C,NECL4,NECL-4,Nectin-like protein 4,TSLC1-like protein 2,TSLL2
EIAAB06691 Bgp2,BGP-2,Biliary glycoprotein 2,Carcinoembryonic antigen-related cell adhesion molecule 2,Ceacam2,CEA-related cell adhesion molecule 2,Mouse,Mus musculus
EIAAB33207 Homo sapiens,Human,NECL-5,Nectin-like protein 5,Poliovirus receptor,PVR,PVS


 

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