ID   A0A3Q3XDG5_MOLML        Unreviewed;      1033 AA.
AC   A0A3Q3XDG5;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
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:ENSMMOP00000023839.1, ECO:0000313|Proteomes:UP000261620};
RN   [1] {ECO:0000313|Ensembl:ENSMMOP00000023839.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A3Q3XDG5; -.
DR   STRING; 94237.ENSMMOP00000023839; -.
DR   Ensembl; ENSMMOT00000024237.1; ENSMMOP00000023839.1; ENSMMOG00000018144.1.
DR   OMA; CYVPDRI; -.
DR   Proteomes; UP000261620; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
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; 6.
DR   Gene3D; 2.60.40.60; Cadherins; 6.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   PANTHER; PTHR24028; CADHERIN-87A; 1.
DR   PANTHER; PTHR24028:SF41; PROTOCADHERIN-17; 1.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; Cadherin-like; 6.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 6.
PE   4: Predicted;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261620};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        699..721
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..142
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          143..253
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          254..361
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          363..467
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          468..577
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          583..689
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          902..952
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..922
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1033 AA;  113966 MW;  A082F5DFFF6C111D CRC64;
     GDTTRPHSNT TMLGMYLSIF FFFLLWANAL TLKNLNYSVP EEQGPGTVIG NIAKDARLGP
     EQTGQGGQGK KANFRVLENS APHLIDVDPQ SGLLYTKQRI DRETLCKRNP KCQLSMEVFA
     NDKEICMIKI DIQDINDNSP TFPSDQIDID ISENAVPGTR FPLTSAHDAD AGENGLKTYQ
     ITRDDYNLFS LEVKSRGDGT KFPELVIQRP LDREERSHHT LILSATDGGE YPRSGTMQIN
     VKVIDSNDNS PVFDQPSYVV EIPENSPPGK VLIDLNATDP DEGNNGQVVY SFSGYAPERI
     RELFSIDSRT GVIKIQGEID YEESPVIEID VQAKDLGPNP IPGHCKVTVK VLDRNDNLPS
     IGFVSVRQGA ISEAAPPGTV IALVRVTDKD SGRNGQLQCR VLGSVPFKLE ENYDNFYTVV
     TDRPLDREVQ DEYNVTIVAK DNGIPPLNST KSFTVKILDE NDNVPRFTKS VYLLQIPENN
     IPGEYLGSVL AHDPDLGQNG TVYYSIINSN VSGGDVNTYV NVNAANGAIY AVRSFNYEQI
     KYFDFKVLAK DAGSPHLESN TTVRISVLDV NDNIPVIVLP ILLNDTAEIH VPRNVGVGYI
     VTTVRAVDND YGESGRLTYE ISDGNEEHLF EIDPVTGEVR TAHPFWDDVS PIVELIIRVS
     DHGKPMLTAA ARLIIKASDG RPPDGLPHTK DNQNWDMSLP LIVTLSIISI MLLAAMVTIA
     IKCKRENKEI RTYNCRIAEY SHPQLGKGKK KKINKNDIML VQSEVEERDA MNVMNVVSSP
     SLATSPMYFD YQTRLPLSSP RSEDCVNCTE ECRVLGHSDR CWMPQFPAGG NQAEGVDYRN
     NMFVPAGMET VPEMETYETV NPNGKKTFCT FGKERRDHTI LVANVKPYLK AKRALSPLLQ
     EIPSASSSPT KGCSTMSPCS SVKSPADGAE GKPPPATCSG HYGPPDGQYL SPAKHTREQG
     MYQAMPASDP VAKMLAEARS RISQEATAET ECVLEQVEPD ANRDRMDADQ VVRDIDKLLQ
     DCRGSEATGT LRK
//