ID A0A2I3SIV3_PANTR Unreviewed; 820 AA.
AC A0A2I3SIV3;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Cadherin 24 {ECO:0000313|Ensembl:ENSPTRP00000076986.1};
GN Name=CDH24 {ECO:0000313|Ensembl:ENSPTRP00000076986.1,
GN ECO:0000313|VGNC:VGNC:7436};
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:ENSPTRP00000076986.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000076986.1, 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:ENSPTRP00000076986.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AACZ04059393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I3SIV3; -.
DR PaxDb; 9598-ENSPTRP00000052774; -.
DR Ensembl; ENSPTRT00000088162.1; ENSPTRP00000076986.1; ENSPTRG00000006158.6.
DR VGNC; VGNC:7436; CDH24.
DR GeneTree; ENSGT00940000159567; -.
DR InParanoid; A0A2I3SIV3; -.
DR Proteomes; UP000002277; Chromosome 14.
DR Bgee; ENSPTRG00000006158; Expressed in cerebellar cortex and 17 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; 4.
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; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF272; CADHERIN-24; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 4.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 4.
DR SUPFAM; SSF49313; Cadherin-like; 5.
DR PROSITE; PS00232; CADHERIN_1; 1.
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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..820
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014124245"
FT TRANSMEM 642..663
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..150
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 151..259
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 260..374
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 375..518
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 518..631
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 769..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 87761 MW; 83289301364DFF56 CRC64;
MWGLVRLLLA WLGGWGCMGR LAAPARAWAG SRGHPGPALL RTRRSWVWNQ FFVIEEYAGP
EPVLIGKLHS DVDRGEGRTK YLLTGEGAGT VFVIDEATGN IHVTKSLDRE EKAQYVLLAQ
AVDRASNRPL EPPSEFIIKV QDINDNPPIF PLGPYHATVP EMSNVGTSVI QVTAHDADDP
SYGNSAKLVY TVLDGLPFFS VDPQTGVVRT AIPNMDRETQ EEFLVVIQAK DMGGHMGGLS
GSTTVTVTLS DVNDNPPKFP QSLYQFSVVE TAGPGTLVGR LRAQDPDVGD NALMAYSILD
GEGSEAFSIS TDSQGRDGLL TVRKPLDFES RRSYSFRVEA TNTLIDPAYL RRGPFKDVAS
VRVAVQDAPE PPAFTQAAYH LTVPENKAPG TLVGQISAAD LDSPASPIRY SILPHSDPER
CFSIQPEEGT IHTAAPLDRE ARVWHNLTVL ATELGWSWGP ERGWVPPLVA EWSAPAAPPQ
RSPVGSPVGI PQVGDSAQAS RVQVAIQTLD ENDNAPQLAE PYDTFVCDSA APGQLIQVIQ
ALDRDEVGNS SHVSFQGPLG PDANFTVRDN RDGSASLLLP SRPAPPRHAP YLVPIELWDW
GQPALSSTAT VTVSVCRCQP DGSVASCWPE AHLSAAGLST GALLAIITCV GALLALVVLF
AALRRQKREA LMVLEEDDVR ENIITYDDEG GGEEDTEAFD ITALQNPDGA APPAPGPPAR
RDVLPRARVS RQPRPPGPAD VAQLLALRLR EADEDPGVPP YDSVQVYGYE GRGSSCGSLS
SLGSGSEAGG APGPAEPLDD WGPLFRTLAE LYGAKEPPAP
//
