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Database: UniProt
Entry: A0A2G8LNX4_STIJA
LinkDB: A0A2G8LNX4_STIJA
Original site: A0A2G8LNX4_STIJA 
ID   A0A2G8LNX4_STIJA        Unreviewed;       756 AA.
AC   A0A2G8LNX4;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   22-FEB-2023, entry version 17.
DE   SubName: Full=Ap-cadherin {ECO:0000313|EMBL:PIK61969.1};
GN   ORFNames=BSL78_01113 {ECO:0000313|EMBL:PIK61969.1};
OS   Stichopus japonicus (Sea cucumber).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC   Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX   NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK61969.1, ECO:0000313|Proteomes:UP000230750};
RN   [1] {ECO:0000313|EMBL:PIK61969.1, ECO:0000313|Proteomes:UP000230750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shaxun {ECO:0000313|EMBL:PIK61969.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PIK61969.1};
RX   PubMed=29023486;
RA   Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA   Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA   Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA   Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT   "The sea cucumber genome provides insights into morphological evolution and
RT   visceral regeneration.";
RL   PLoS Biol. 15:E2003790-E2003790(2017).
CC   -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC       {ECO:0000256|RuleBase:RU004357}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIK61969.1}.
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DR   EMBL; MRZV01000021; PIK61969.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8LNX4; -.
DR   STRING; 307972.A0A2G8LNX4; -.
DR   Proteomes; UP000230750; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   CDD; cd00110; LamG; 2.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR   InterPro; IPR039808; Cadherin.
DR   InterPro; IPR000233; Cadherin_Y-type_LIR.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR001791; Laminin_G.
DR   PANTHER; PTHR24027:SF422; CADHERIN DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF02210; Laminin_G_2; 2.
DR   SMART; SM00282; LamG; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        587..608
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          104..306
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          309..346
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          349..525
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          695..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..731
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        279..306
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT   DISULFID        336..345
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   756 AA;  83125 MW;  146695BCDEC362B6 CRC64;
     MGGPSAMEKL LKLLSTITGA KEENIDIFTV LPVPDMENTV DVRYSAHGSP YYSAERLNGD
     AESKIALIES TLTGVTVEAI YIDECGSAEC EADCSNVLTI DPDPVVINSV EASMVGINAF
     ISPFCGCAAR DGDVGTCIGH YCHNGGTCED TFSGPKPQDY ILLQLRAGKP HSNGLRCWDL
     TLEVTNNGAL NDGKWHKVDI FRNGLDVELV IDDCASASVF ENHTTSVFSN SDLCKASATL
     PGDETVFHAN KPLQLGGVNP NLEYPQTLGL DSVDGFNGCI RNVDQDSTLY DLYDVDEASP
     GSQPGCPDAD KHCDALRPPC INGVCDADFS GAVCICNPGW FGDGCDQELD AYDFLDSSYV
     TYQLKTNLPL PDRESSYKIM IRTRQQTGRV WQITNANTFE HVTMQLQDGY LMSSWHLGDN
     TISVTLDKYP LDNGEWHSIF FYRYDNYIQI KVDGGGGVRQ AENRDSSFRV LQVDRDNLVV
     GAELLYGVTV SSDFVGCMKD PRIGDNYLGV TETSEFASPM AVNMCHGVYL IGRCLCGRTG
     LQQQSMPERC EVYDKFDDYE CCVRRDFTGK DCDLKSEAVF LTIRAGGIIP IVACLLLLLL
     LLLLFIVYKR TEDKKNALAF AVDPEDDMRE NFINYDEEGG EKDQTAYDIT MLRKPVQPSP
     IVPRPVKTLE DVPQRSIPRD GVNVGDFLEE RLGDLTTTRG SPYDTLHTYD YEGEGSTSGS
     LSSLNSNSSD GSQDYDYLKG LGPPFKRLAD MYGGVE
//
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