ID H2QQP7_PANTR Unreviewed; 788 AA.
AC H2QQP7; A0A2J8KU52;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE SubName: Full=Cadherin 10 {ECO:0000313|Ensembl:ENSPTRP00000028743.3};
GN Name=CDH10 {ECO:0000313|Ensembl:ENSPTRP00000028743.3,
GN ECO:0000313|VGNC:VGNC:6838};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000028743.3, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000028743.3, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000028743.3}
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; AACZ04062287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_009447643.1; XM_009449368.2.
DR AlphaFoldDB; H2QQP7; -.
DR SMR; H2QQP7; -.
DR STRING; 9598.ENSPTRP00000028743; -.
DR PaxDb; 9598-ENSPTRP00000028743; -.
DR Ensembl; ENSPTRT00000031119.4; ENSPTRP00000028743.3; ENSPTRG00000016758.4.
DR GeneID; 461942; -.
DR KEGG; ptr:461942; -.
DR CTD; 1008; -.
DR VGNC; VGNC:6838; CDH10.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000154187; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; H2QQP7; -.
DR OMA; CSPEITF; -.
DR OrthoDB; 3667774at2759; -.
DR TreeFam; TF329887; -.
DR Proteomes; UP000002277; Chromosome 5.
DR Bgee; ENSPTRG00000016758; Expressed in Brodmann (1909) area 10 and 9 other cell types or tissues.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd11304; Cadherin_repeat; 5.
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; IPR000233; Cadherin_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027:SF290; CADHERIN-10; 1.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 5.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
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 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:UP000002277};
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..788
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015092975"
FT TRANSMEM 603..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..160
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 161..269
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 270..384
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 385..489
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 489..603
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
SQ SEQUENCE 788 AA; 88451 MW; E92908F9C19270B2 CRC64;
MTIHQFLLLF LFWVCLPHFC SPEIMFRRTP VPQQRILSSR VPRSDGKILH RQKRGWMWNQ
FFLLEEYTGS DYQYVGKLHS DQDKGDGSLK YILSGDGAGT LFIIDEKTGD IHATRRIDRE
EKAFYTLRAQ AINRRTLRPV EPESEFVIKI HDINDNEPTF PEEIYTASVP EMSVVGTSVV
QVTATDADDP SYGNSARVIY SILQGQPYFS VEPETGIIRT ALPNMNRENR EQYQVVIQAK
DMGGQMGGLS GTTTVNITLT DVNDNPPRFP QNTIHLRVLE SSPVGTAIGS VKATDADTGK
NAEVEYRIID GDGTDMFDIV TEKDTQEGII TVKKPLDYES RRLYTLKVEA ENTHVDPRFY
YLGPFKDTTI VKISIEDVDE PPVFSRSSYL FEVHEDIEVG TIIGTVMARD PDSISSPIRF
SLDRHTDLDR IFNIHSGNGS LYTSKPLDRE LSQWHNLTVI AAEINNPKET TRVAVFVRIL
DVNDNAPQFA VFYDTFVCEN ARPGQLIQTI SAVDKDDPLG GQKFFFSLAA VNPNFTVQDN
EDNTARILTR KNGFNRHEIS TYLLPVVISD NDYPIQSSTG TLTIRVCACD SQGNMQSCSA
EALLLPAGLS TGALIAILLC IIILLVIVVL FAALKRQRKK EPLILSKEDI RDNIVSYNDE
GGGEEDTQAF DIGTLRNPAA IEEKKLRRDI IPETLFIPRR TPTAPDNTDV RDFINERLKE
HDLDPTAPPY DSLATYAYEG NDSIAESLSS LESGTTEGDQ NYDYLREWGP RFNKLAEMYG
GGESDKDS
//
