ID A0A2R9BYH8_PANPA Unreviewed; 829 AA.
AC A0A2R9BYH8;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Cadherin 3 {ECO:0000313|Ensembl:ENSPPAP00000031572.1};
GN Name=CDH3 {ECO:0000313|Ensembl:ENSPPAP00000031572.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000031572.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000031572.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000031572.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC {ECO:0000256|RuleBase:RU004357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU003318}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
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DR EMBL; AJFE02047334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02047335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02047336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02047337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02047338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02047339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003814609.1; XM_003814561.2.
DR AlphaFoldDB; A0A2R9BYH8; -.
DR STRING; 9597.ENSPPAP00000031572; -.
DR Ensembl; ENSPPAT00000054437.1; ENSPPAP00000031572.1; ENSPPAG00000038719.1.
DR GeneID; 100982523; -.
DR KEGG; pps:100982523; -.
DR CTD; 1001; -.
DR GeneTree; ENSGT00940000154848; -.
DR OMA; EAQNQHT; -.
DR OrthoDB; 5306553at2759; -.
DR Proteomes; UP000240080; Chromosome 16.
DR Bgee; ENSPPAG00000038719; Expressed in adult mammalian kidney and 4 other cell types or tissues.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0022405; P:hair cycle process; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0031424; P:keratinization; IEA:Ensembl.
DR GO; GO:0051796; P:negative regulation of timing of catagen; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0048023; P:positive regulation of melanin biosynthetic process; IEA:Ensembl.
DR GO; GO:1902910; P:positive regulation of melanosome transport; IEA:Ensembl.
DR GO; GO:0001895; P:retina homeostasis; IEA:Ensembl.
DR CDD; cd11304; Cadherin_repeat; 3.
DR Gene3D; 2.60.40.60; Cadherins; 5.
DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR000233; Cadherin_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF444; CADHERIN-3; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 4.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 4.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; Cadherin-like; 5.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU003318};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..829
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015359593"
FT TRANSMEM 655..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 108..215
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 216..328
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 329..440
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 441..548
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 547..660
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
SQ SEQUENCE 829 AA; 91389 MW; 483775FDF25DE58C CRC64;
MGLPRGPLAS LLLLQVCWLQ CAASEPCRAV FREAEVTLEA GGAEQEPGQA LGKVFMGCPG
QEPALFSTDN DDFTVRNGET VQERRSLKER NPLKIFPSKR ILRRHKRDWV VAPISVPENG
KGPFPQRLNQ LKSNKDRDTK IFYSITGPGA DSPPEGVFAV EKETGWLLLN KPLDREEIAK
YELFGHAVSE NGASVEDPMN ISIIVTDQND HKPKFIQDTF RGSVLEGVLP GTSVMQVTAT
DEDDAIYTYN GVVAYSIHSQ EPKDPHDLMF TIHRSTGTIS VISSGLDREK VPEYTLTIQA
TDMDGDGSTT TAVAVVEILD ANDNAPVFDP QKYEAHVPEN AVGHEVQRLT VTDLDAPNSP
AWRATYLIMG GDDGDHFTIT THPESNQGIL TTRKGLDFEA KNQHTLYVEV TNEAPFVLKL
PTSTATIVVH VEDVNEAPVF VPPSKVVEVQ EGIPTGEPVC VYTAEDPDKE NQKISYRILR
DPAGWLAMDP DSGQVTAVGT LDREDEQFVR NNIYEVMVLA MDNGSPPTTG TGTLLLTLID
VNDHGPVPEP RQITICNQSP VHQVLNITDK DLSPHTSPFQ AQLTDDSDIY WTAEVNEEGD
TVVLSLKKFL KQDTYDVHLS LSDHGNKEQL TVIRATVCDC HGHVETCPGP WKGGFILPVL
GAILALLFLL LVLLLLVRKK RKIKEPLLLP EDDTRDNVFY YGEEGGGEED QDYDITQLHR
GLEARPEVVL RNDVAPTIIP TPMYRPRPAN PDEIGNFIIE NLKAANTDPT APPYDSLLVF
DYEGSGSDAA SLSPLTSSAS DQDQDYDYLN EWGSRFKKLA DMYGGGEDD
//
