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Database: UniProt
Entry: A0A3Q3X8L9_MOLML
LinkDB: A0A3Q3X8L9_MOLML
Original site: A0A3Q3X8L9_MOLML 
ID   A0A3Q3X8L9_MOLML        Unreviewed;       945 AA.
AC   A0A3Q3X8L9;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Cadherin domain-containing protein {ECO:0000259|PROSITE:PS50268};
OS   Mola mola (Ocean sunfish) (Tetraodon mola).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Molidae; Mola.
OX   NCBI_TaxID=94237 {ECO:0000313|Ensembl:ENSMMOP00000024600.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000024600.1}
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|RuleBase:RU003318};
CC       Single-pass type I membrane protein {ECO:0000256|RuleBase:RU003318}.
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DR   AlphaFoldDB; A0A3Q3X8L9; -.
DR   STRING; 94237.ENSMMOP00000024600; -.
DR   Ensembl; ENSMMOT00000025011.1; ENSMMOP00000024600.1; ENSMMOG00000018698.1.
DR   OMA; MTGQEMG; -.
DR   Proteomes; UP000261620; Unplaced.
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; 4.
DR   Gene3D; 2.60.40.60; Cadherins; 5.
DR   Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
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; PTHR24025; DESMOGLEIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR24025:SF1; DESMOGLEIN-2; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF00028; Cadherin; 3.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 4.
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:ARBA00022989};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003318};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          30..111
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          111..221
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          222..341
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          342..453
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          469..557
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          693..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        693..708
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   945 AA;  103484 MW;  875D2CD6BE23D181 CRC64;
     KKREWITAPR QLKENHDYTG LQSIARIRSD KENHTQIMYF LSGPGVDETP KNVFGVDRVT
     GFVKIYSILD REKIAFYYLQ GIAKYADGSY AEKIIGLNIT VVDENDCPPV IKAQQVGSVN
     ESSATGTVVM KVIATDDDQV NTLHTKIFYS IVEQANTAGF FRINSQTGDV TVQRNTLDRE
     KQDTYKLTIK AADLDGRAGG NTGTGEILIK ILDINDNIPT LEKESYEGSV EENTINVEVL
     KIKAIDMDLI HTDNWLAVFK IISGNEAGYF SITTDSKTNE GIIMIRKALD YEELKVVHLE
     VTVSNKAQYN FGSGSTAGGT ITQKSYTIKI NVVNQKEGPR FQPSVKVVII SEDQTSISLN
     KIITRYAAID TDTLQTVTDV RYAKIRDDDN WLIIDEKTAD IKLNKLPDRE SKFLVNGTYY
     AKIICITNDH PSKTATGTIA IQVEDYNDHC PTLTTRTQTM CYEDNFVYVT AIDQDEFPNA
     APFDFTVIQE SNQGNWKVEP LNETTVILRG QDNLWPGNYK VTVEVKDQQG KSCTDVQVME
     VIVCACHETT KTCVPRSAKT TTLGASGYKC EISVLVIPLL LLFCLCGGAA SAGDFKPIPY
     DTKQQLISYH TEGQGEDKKS NHAAQQSQQK DSMLIYDYEG QESLAGSVGC CSLLENDNDL
     SFLNDLGPKF KTLAEICQGS TIVTKSLSAG VSISPPRSLS PVRPSTSTHT HVHTHRETIR
     DRDRVDINTL NTSKVAAGSF STVQEKQFTD RTQGLATTSK IHVQDNIMIP SQTMLVQQPT
     MFYAATPMYV VEPNPQVVLV AGGTQQAVGQ VGVSQGLVQV SGLQGSQGVV LVDRQVGGLT
     GKVSQGLIQG TGSGSRQVWV ENGSSGGGQA ISQGFVRIQQ GSAEQGLESR IHSKQVKTQS
     ISHASTGLNK GFAQKATPKV HGSQKVVVQH KKVSLTERNV ESSSA
//
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