ID A0A2U9C428_SCOMX Unreviewed; 844 AA.
AC A0A2U9C428;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Cadherin domain-containing protein {ECO:0000259|PROSITE:PS50268};
GN ORFNames=SMAX5B_016356 {ECO:0000313|EMBL:AWP11354.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP11354.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP11354.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of intercellular desmosome junctions. Involved in
CC the interaction of plaque proteins and intermediate filaments mediating
CC cell-cell adhesion. {ECO:0000256|RuleBase:RU004358}.
CC -!- SUBCELLULAR LOCATION: Cell junction, desmosome
CC {ECO:0000256|ARBA:ARBA00004568}. Cell membrane
CC {ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane protein
CC {ECO:0000256|RuleBase:RU003318}.
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DR EMBL; CP026254; AWP11354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9C428; -.
DR STRING; 52904.ENSSMAP00000030442; -.
DR Proteomes; UP000246464; Chromosome 12.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
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 InterPro; IPR009122; Desmosomal_cadherin.
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 PRINTS; PR01818; DESMOCADHERN.
DR SMART; SM00112; CA; 4.
DR SUPFAM; SSF49313; Cadherin-like; 5.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 4.
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 junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..844
FT /note="Cadherin domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015916962"
FT TRANSMEM 596..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..143
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 142..254
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 255..367
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 368..479
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
SQ SEQUENCE 844 AA; 92520 MW; 02DA8B2C5E72FF8B CRC64;
MGNDEMGLLL LLVLALMLST EARQKRPQTL KRQKREWILP PAKLLENTDY THKEFIAKIR
SDKDKGAKVE YYLSGPGADK PPFNLFVVDQ YTGFVTVTGI LDREKYPSFN LTGIAKHIDG
TLAEDSIPMM VTVLDQNDNA PTFELHTGNI TEASKKGTFV MQIEGKDNDQ AGTSNSEISY
SIVSQEPEGT GHMFTIDKKT GNLYVNEPTL DRETYDSYKL VIKGIDLGGA AGGLTGTGTV
EIKVLDINDN IPTLEKSEYS GTVDENVMDV VVMRIKALDK DLENTDNWVT VFSIAKGNED
NIFSIETDKE TNEGILKLIK PLDFEEIQNL ELGLLIENVA PFLEGGAILM DVDVKISVNN
VPEVPAFIPD TKTVPVSEDP NEATEDGVIT VFAAVDPDTG KPAEDVSYAK GYDPDSWLTI
NAETAEIKLN KIPDRESSFL VNGTYIAKIL VMTKDIPSKT ATGTIAIQVT DSNDHCPTLI
TKHNSLCSNE KTVFVTGCDE DVSPNSAPFT FRIITDGTQG NWVVEVINET SAALHSQEPL
WPGSYELQLE VLDAQGLSCS ANEVVIVDVC TCVETEACSL MAARLGTTSP KLSAPAIGLL
LMAMCLLLFI PLLLLLCHCG GKDTIFPEKF NDLPFDAKEH LISYRTEGRG DDKAVPLQNV
PITLGTQTFF GTAPASNFTQ HQTPTTFQTA TIYNKFEESS QSLREVNDAY RFSREAFNHG
NGKALQFSRK RLGIQNRTVL FEDIALPDTF LDDYYSQKVV CALPVKDGLL EYDFEGHGSF
AGSVGCCSFL ESDNDLQFLN DLGTKFKTLA DICSPPISKP SLTCKEGDVL LYLSSSQFTT
PPAL
//
