ID H0ZGE0_TAEGU Unreviewed; 797 AA.
AC H0ZGE0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Cadherin 8 {ECO:0000313|Ensembl:ENSTGUP00000009652.2};
GN Name=CDH8 {ECO:0000313|Ensembl:ENSTGUP00000009652.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000009652.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000009652.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000009652.2}
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}.
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DR AlphaFoldDB; H0ZGE0; -.
DR STRING; 59729.ENSTGUP00000009652; -.
DR Ensembl; ENSTGUT00000009756.2; ENSTGUP00000009652.2; ENSTGUG00000009281.2.
DR GeneTree; ENSGT00940000153691; -.
DR HOGENOM; CLU_005284_4_3_1; -.
DR InParanoid; H0ZGE0; -.
DR OMA; IYMAPMA; -.
DR TreeFam; TF329887; -.
DR Proteomes; UP000007754; Chromosome 11.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
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; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF273; CADHERIN-8; 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 Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 611..640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..167
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 168..276
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 277..391
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 392..494
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 494..611
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT REGION 751..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 87855 MW; D8D15EE8DB47B99D CRC64;
MPERLTEMLM DTWTPLIILW ITVLPSIYMA PMNQSQVLPS GSSTGLKRLN EEQRILHRSK
RGWVWNQMFV LEEFSGPEPI LVGRLHTDLD PGSSKIKYIL SGDGAGTIFV INDKTGDIHA
MKRLDREEKA EYTLTAQAVD RDTNQPLEPP SEFIIKVQDI NDNAPEFVEG PYHATVPEMS
VVGTFVTKVT ATDADDPVYG NSAKLVYSIL EGQPYFSIEP HTAIIKTALP NMDREAKEEY
FVVIQAKDMG GHMGGLSGTT TVTITLSDVN DNPPKFAQSL YHFSVMEDVA LGEPIGRVKA
NDLDIGENAK SSYDIIEGDG MDVFEITTDA QTQDGIIRVR KPLDFETKKS YTLKVEAANI
HIDPRFLSGG PFKDTATVKI VVEDADEPPV FSSPTYLLEV HENAALNSVL GQVAAHDPDV
SSSPIRFSID RHTDLERQFN VNAEDGKITL ATPLDRETST WHNITIVATE TSNQVSRVPV
AIKVLDVNDN APEFASEHEA FLCENGKPGQ VIQIVSAVDK DDPKNGHYFL YSLLPEMVNN
PNFTIKKNED NTLSILAKHS GFSRQKQEVY LLPIVISDSG TPPMSSTGTL TIRVCGCSSD
GTVQSCNAEA YVLPIGLSMG ALIAILACII LLLVIVVLFV TLRRHKNEPL IIKDDEDVRE
NIIRYDDEGG GEEDTEAFDI ATLQNPDGIN GFLPRKDIKP DLQFMPRQGL APVPNGVDVD
EFINVRLHEA DNDPTAPPYD SIQIYGYEGK GSAAGSLSSL ESSTSDSDQN FDYLSEWGPR
FKRLGELYSV GESDKET
//
