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Database: UniProt
Entry: M7BXR9_CHEMY
LinkDB: M7BXR9_CHEMY
Original site: M7BXR9_CHEMY 
ID   M7BXR9_CHEMY            Unreviewed;       456 AA.
AC   M7BXR9;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Cadherin-11 {ECO:0000313|EMBL:EMP36838.1};
GN   ORFNames=UY3_05921 {ECO:0000313|EMBL:EMP36838.1};
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:EMP36838.1, 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; KB523583; EMP36838.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7BXR9; -.
DR   STRING; 8469.M7BXR9; -.
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; 2.
DR   Gene3D; 2.60.40.60; Cadherins; 2.
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:SF85; CADHERIN-11; 1.
DR   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF00028; Cadherin; 2.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 2.
DR   SUPFAM; SSF49313; Cadherin-like; 2.
DR   PROSITE; PS00232; CADHERIN_1; 1.
DR   PROSITE; PS50268; CADHERIN_2; 2.
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        279..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          82..152
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          152..269
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   456 AA;  50565 MW;  BEF16AE864BF0053 CRC64;
     MVLEKSSDPA FHTAYTSDGQ PAARQGNSLV GHKTVFTLTV HRHGHPQLPL AGNGEPWPLG
     AVDSQCKDCL VVRQWITLTG CRYSIDRHTD LERYFSIDLE DGYIKTIKTL DREEIAWHNI
     SVCANEVRKE HPKAKVPVAI KVLDVNDNAP KFASTYEAFI CENAQSNQPF ITITADDKDD
     TANGPRFIFS LPPEIIHNPN FTLRDNRDNT VSILVRRGGF SRQKQDLYLL PIVISDGGIP
     PMSSTNTLTI RVCGCDSNGS LLSCNAEAYI LNAGLSTGAL IAILACIVIL LVIVVLFVTL
     KRQKKEPLIV FEEEDVRENI ITYDDEGGGE EDTEAFDIAT LQNPDGINGF IPRKDIKPEY
     QYMPRPGLRP APNSVDVDDF INTRIQEADN DPTAPPYDSI QIYGYEGRGS VAGSLSSLES
     ATTDSDLDYD YLQNWGPRFK KLADLYGSKD TFDDDS
//
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