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Database: UniProt
Entry: W5N5F1_LEPOC
LinkDB: W5N5F1_LEPOC
Original site: W5N5F1_LEPOC 
ID   W5N5F1_LEPOC            Unreviewed;       787 AA.
AC   W5N5F1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=Cadherin-20 {ECO:0000256|ARBA:ARBA00040456};
GN   Name=CDH20 {ECO:0000313|Ensembl:ENSLOCP00000015860.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000015860.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000015860.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC       preferentially interact with themselves in a homophilic manner in
CC       connecting cells; cadherins may thus contribute to the sorting of
CC       heterogeneous cell types. {ECO:0000256|ARBA:ARBA00037319}.
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; AHAT01002396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; W5N5F1; -.
DR   Ensembl; ENSLOCT00000015890.1; ENSLOCP00000015860.1; ENSLOCG00000012876.1.
DR   GeneTree; ENSGT00940000158167; -.
DR   Proteomes; UP000018468; Linkage group LG9.
DR   Bgee; ENSLOCG00000012876; Expressed in brain and 4 other cell types or tissues.
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:SF84; CADHERIN-20; 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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
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        610..631
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          74..154
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          155..263
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          264..378
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          379..483
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          483..605
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
SQ   SEQUENCE   787 AA;  88221 MW;  B5A0637A64AAED91 CRC64;
     LKLGNKDNYY NFLQYSTLHI YFQIVSKSEI FKTSTQTDWT EPHNRVKRGW VWNQFFVLEE
     YTGLEPLYVG KLHSDMDKGD GSIKYILSGE GAGTMFTIDD NTGDIHAIQR LDREEKAQYI
     LRAQALHRQT GKPLEPESEF IVKIQDINDN EPKFLDGPYT ASVPEMSVIG TSVMQLTATD
     ADDPTYGNSA RVVYSILQGQ PYFSVEPRTG IIRVSLPNMD REAKEHYEVI IQAKDMGGQL
     GGLAGTTTVN VTLEDVNDNP PRFAQKLYQM SVPESAPVGS IVGRVQAKDL DEGINAEMRY
     AIIDGDGRDT FDISTDPTNQ FGIISIRKKL DFESKRSFTL KVEGANTYLD PRFLNRGPFS
     DVTIIHVSVE DVDEPPQFDS PHYFVEVPED VEIGTVFQTV SAKDPDVANN TVRYSIERKS
     DPGRYFYIDI TSGALMTARP LDREELSWHN ITVLAMEMNN PTQIGSVSVT IKVLDVNDNP
     PELAKYYEAF VCENAKAGQL IQTVTAVDLD DPLGGQHFYY SLAPEAANNP NFTLRDNQDN
     TAWILTRRGG FTQKEQSIYH LPIFITDGDQ PMQSSTSTLT IRVCSCDSDG NVMSCTAEAY
     TLPVSLSRGA LIAILACIFV LLVMILLILS LRSQRKKPYL SDEEENVHEN IVRYDDEGGG
     EEDTEAFDIA AMWNPREVHL GKIRQDMLPE IESLSRYVPQ TCMGDSNVHG YVLAKLYEAD
     ADPCAPPYDS LQTYAYEGEG SVAESLSSLQ SVTSNTDHEY DYLSDWGPRF KKLAEMYGVM
     EANNPLW
//
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