ID M7BVU9_CHEMY Unreviewed; 742 AA.
AC M7BVU9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Cadherin-8 {ECO:0000313|EMBL:EMP36208.1};
DE Flags: Fragment;
GN ORFNames=UY3_06539 {ECO:0000313|EMBL:EMP36208.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP36208.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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 EMBL; KB525803; EMP36208.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BVU9; -.
DR STRING; 8469.M7BVU9; -.
DR eggNOG; KOG3594; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
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 561..590
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..115
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 116..224
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 225..339
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 340..444
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 444..566
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMP36208.1"
FT NON_TER 742
FT /evidence="ECO:0000313|EMBL:EMP36208.1"
SQ SEQUENCE 742 AA; 81915 MW; 761823AABC995948 CRC64;
QKVLNRSKRG WVWNQMFVLE EFSGPEPILV GRLHTDLDPG SSKIKYILSG DGAGTIFVIN
DKTGDIHAMK RLDREEKAEY TLTAQAVDRD TNKPLEPPSE FIIKVQDIND NAPEFLDGPY
HATVPEMSIV GTFVTKVTAT DADDPVYGNS AKLVYSILEG QPYFSIEPHT AIIRTALPNM
DREAKEEYFV VIQAKDMGGH MGGLSGTTTV TITLTDVNDN PPKFAQSLYH FSVMEDIALG
EPIGRVKAND LDIGENAKSS YDIIEGDGMD IFEITSEAQT QDGIIRLRKP LDFETKKSYT
LKVEAANVHI DPRFISGGPF KDTATVKIVV EDADEPPVFS SPTYLLEVHE NAAINSVIGQ
VTSHDPDVSS SPIRFSIDRH TDLERQFNIN ADDGKITLAT PLDRETNIWH NITIVATETR
NHSQVSRVPV AIKVLDVNDN APEFASEHDA FLCENGKPGQ VIQTVSAIDK DDPKNGHFFL
YSLLPEMVNN PNFTIKKNED NTLSILAKHS AFSRQKQEVY LLPIIISDSG NPPMSSTSTL
TIRVCGCSSD GVVQSCNVEA YVLPIGLSMG ALIAILACII LLLVIVVLFV TLRRHKNEPL
IIKDEEDVRE NIIRYDDEGG GEEDTEAFDI ATLQNPDGIN GFLPRKDIKP DLQFMPRQGL
APVPNGVDVD EFINVRLHEA DNDPTAPPYD SIQIYGYEGR GSVAGSLSSL ESSTSDSDQN
FDYLSEWGPR FKRLGELYSV GE
//
