CADH3_MOUSE
ID CADH3_MOUSE Reviewed; 822 AA.
AC P10287; Q61465; Q8BSL6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Cadherin-3;
DE AltName: Full=Placental cadherin;
DE Short=P-cadherin;
DE Flags: Precursor;
GN Name=Cdh3; Synonyms=Cdhp;
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].
RX PubMed=3428270; DOI=10.1002/j.1460-2075.1987.tb02698.x;
RA Nose A., Nagafuchi A., Takeichi M.;
RT "Isolation of placental cadherin cDNA: identification of a novel gene
RT family of cell-cell adhesion molecules.";
RL EMBO J. 6:3655-3661(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Forelimb;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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).
RN [5]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=1886768; DOI=10.1093/nar/19.16.4437;
RA Hatta M., Miyatani S., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA Takeichi M.;
RT "Genomic organization and chromosomal mapping of the mouse P-cadherin
RT gene.";
RL Nucleic Acids Res. 19:4437-4441(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
RX PubMed=8515462; DOI=10.1006/jmbi.1993.1341;
RA Faraldo M.L., Cano A.;
RT "The 5' flanking sequences of the mouse P-cadherin gene. Homologies to 5'
RT sequences of the E-cadherin gene and identification of a first 215 base-
RT pair intron.";
RL J. Mol. Biol. 231:935-941(1993).
RN [7]
RP NUCLEOTIDE SEQUENCE OF 1-55.
RC STRAIN=C57BL/6J;
RA Hatta M., Takeichi M.;
RT "Complex cell type-specific transcriptional regulation by the promoter and
RT an intron of the mouse P-cadherin gene.";
RL Dev. Growth Differ. 36:509-519(1994).
RN [8]
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=8879495; DOI=10.1095/biolreprod55.4.822;
RA Munro S.B., Blaschuk O.W.;
RT "A comprehensive survey of the cadherins expressed in the testes of fetal,
RT immature, and adult mice utilizing the polymerase chain reaction.";
RL Biol. Reprod. 55:822-827(1996).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells; cadherins may thus contribute to the sorting of
CC heterogeneous cell types.
CC -!- SUBUNIT: Interacts with CDCP1 and CTNNB1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- DEVELOPMENTAL STAGE: Expression is high in both fetal and newborn
CC testis but minimal in testis of 7-day-old animals. Not detected in
CC testis of 21-day-old or adult. {ECO:0000269|PubMed:8879495}.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain. {ECO:0000250}.
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DR EMBL; X06340; CAA29646.1; -; mRNA.
DR EMBL; X68057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK031265; BAC27327.1; -; mRNA.
DR EMBL; CH466525; EDL11370.1; -; Genomic_DNA.
DR EMBL; BC098459; AAH98459.1; -; mRNA.
DR EMBL; D12688; BAA02186.1; -; Genomic_DNA.
DR CCDS; CCDS22637.1; -.
DR PIR; S03163; IJMSCP.
DR RefSeq; NP_001032898.1; NM_001037809.5.
DR PDB; 4NQQ; X-ray; 3.20 A; A/B/C/D=100-312.
DR PDBsum; 4NQQ; -.
DR AlphaFoldDB; P10287; -.
DR SMR; P10287; -.
DR STRING; 10090.ENSMUSP00000079613; -.
DR GlyGen; P10287; 2 sites.
DR iPTMnet; P10287; -.
DR PhosphoSitePlus; P10287; -.
DR MaxQB; P10287; -.
DR PaxDb; P10287; -.
DR PeptideAtlas; P10287; -.
DR PRIDE; P10287; -.
DR ProteomicsDB; 265499; -.
DR Antibodypedia; 942; 927 antibodies from 41 providers.
DR DNASU; 12560; -.
DR Ensembl; ENSMUST00000080797; ENSMUSP00000079613; ENSMUSG00000061048.
DR GeneID; 12560; -.
DR KEGG; mmu:12560; -.
DR UCSC; uc009ngh.2; mouse.
DR CTD; 1001; -.
DR MGI; MGI:88356; Cdh3.
DR VEuPathDB; HostDB:ENSMUSG00000061048; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000154848; -.
DR HOGENOM; CLU_005284_2_1_1; -.
DR InParanoid; P10287; -.
DR OMA; EAQNQHT; -.
DR OrthoDB; 182239at2759; -.
DR PhylomeDB; P10287; -.
DR TreeFam; TF316817; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR BioGRID-ORCS; 12560; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Cdh3; mouse.
DR PRO; PR:P10287; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P10287; protein.
DR Bgee; ENSMUSG00000061048; Expressed in ectoplacental cone and 145 other tissues.
DR Genevisible; P10287; MM.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0022405; P:hair cycle process; ISO:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0031424; P:keratinization; ISO:MGI.
DR GO; GO:0051796; P:negative regulation of timing of catagen; ISO:MGI.
DR GO; GO:0032912; P:negative regulation of transforming growth factor beta2 production; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; ISO:MGI.
DR GO; GO:0048023; P:positive regulation of melanin biosynthetic process; ISO:MGI.
DR GO; GO:1902910; P:positive regulation of melanosome transport; ISO:MGI.
DR GO; GO:0032773; P:positive regulation of tyrosinase activity; ISO:MGI.
DR GO; GO:0060901; P:regulation of hair cycle by canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0001895; P:retina homeostasis; ISO:MGI.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 4.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..99
FT /id="PRO_0000003747"
FT CHAIN 100..822
FT /note="Cadherin-3"
FT /id="PRO_0000003748"
FT TOPO_DOM 100..647
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..822
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 100..207
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 208..320
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 321..432
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 433..538
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 539..645
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 351
FT /note="S -> W (in Ref. 1; CAA29646)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="A -> P (in Ref. 1; CAA29646)"
FT /evidence="ECO:0000305"
FT CONFLICT 771
FT /note="L -> M (in Ref. 1; CAA29646)"
FT /evidence="ECO:0000305"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:4NQQ"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:4NQQ"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:4NQQ"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:4NQQ"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 225..228
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 246..254
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:4NQQ"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:4NQQ"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 284..294
FT /evidence="ECO:0007829|PDB:4NQQ"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:4NQQ"
FT STRAND 301..311
FT /evidence="ECO:0007829|PDB:4NQQ"
SQ SEQUENCE 822 AA; 90612 MW; 7C653D58210A595A CRC64;
MELLSGPHAF LLLLLQVCWL RSVVSEPYRA GFIGEAGVTL EVEGTDLEPS QVLGKVALAG
QGMHHADNGD IIMLTRGTVQ GGKDAMHSPP TRILRRRKRE WVMPPIFVPE NGKGPFPQRL
NQLKSNKDRG TKIFYSITGP GADSPPEGVF TIEKESGWLL LHMPLDREKI VKYELYGHAV
SENGASVEEP MNISIIVTDQ NDNKPKFTQD TFRGSVLEGV MPGTSVMQVT ATDEDDAVNT
YNGVVAYSIH SQEPKEPHDL MFTIHKSTGT ISVISSGLDR EKVPEYRLTV QATDMDGEGS
TTTAEAVVQI LDANDNAPEF EPQKYEAWVP ENEVGHEVQR LTVTDLDVPN SPAWRATYHI
VGGDDGDHFT ITTHPETNQG VLTTKKGLDF EAQDQHTLYV EVTNEAPFAV KLPTATATVV
VHVKDVNEAP VFVPPSKVIE AQEGISIGEL VCIYTAQDPD KEDQKISYTI SRDPANWLAV
DPDSGQITAA GILDREDEQF VKNNVYEVMV LATDSGNPPT TGTGTLLLTL TDINDHGPIP
EPRQIIICNQ SPVPQVLNIT DKDLSPNSSP FQAQLTHDSD IYWMAEVSEK GDTVALSLKK
FLKQDTYDLH LSLSDHGNRE QLTMIRATVC DCHGQVFNDC PRPWKGGFIL PILGAVLALL
TLLLALLLLV RKKRKVKEPL LLPEDDTRDN VFYYGEEGGG EEDQDYDITQ LHRGLEARPE
VVLRNDVVPT FIPTPMYRPR PANPDEIGNF IIENLKAANT DPTAPPYDSL LVFDYEGSGS
DAASLSSLTT SASDQDQDYN YLNEWGSRFK KLADMYGGGE DD
