ID Q8MY76_9BIVA Unreviewed; 1222 AA.
AC Q8MY76;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE SubName: Full=Se-cadherin {ECO:0000313|EMBL:BAC06836.1};
DE Flags: Fragment;
GN Name=SeCad {ECO:0000313|EMBL:BAC06836.1};
OS Saccostrea echinata.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Saccostrea.
OX NCBI_TaxID=191078 {ECO:0000313|EMBL:BAC06836.1};
RN [1] {ECO:0000313|EMBL:BAC06836.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12492143; DOI=10.1046/j.1525-142X.2002.02031.x;
RA Oda H., Wada H., Tagawa K., Akiyama-Oda Y., Satoh N., Humphreys T.,
RA Zhang S., Tsukita S.;
RT "A novel amphioxus cadherin that localizes to epithelial adherens junctions
RT has an unusual domain organization with implications for chordate
RT phylogeny.";
RL Evol. Dev. 4:426-434(2002).
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}.
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DR EMBL; AB075367; BAC06836.1; -; mRNA.
DR AlphaFoldDB; Q8MY76; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.40.60; Cadherins; 2.
DR Gene3D; 2.10.25.10; Laminin; 3.
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; 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; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF422; NEURAL-CADHERIN 2-RELATED; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR SMART; SM00112; CA; 3.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR PROSITE; PS50268; CADHERIN_2; 3.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 2: Evidence at transcript level;
KW Calcium {ECO:0000256|PROSITE-ProRule:PRU00043};
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|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1045..1069
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..88
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 98..211
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 228..314
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 466..503
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 504..706
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 709..752
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 755..949
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 990..1030
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 1130..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 493..502
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 723..740
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 742..751
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1020..1029
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAC06836.1"
SQ SEQUENCE 1222 AA; 136244 MW; 68F6F6B762082E5F CRC64;
ATDRDEGING LFDFYVSRKP ISEKPDYYFR IAQNRDNGTV SLKNSLDHET LTKHIVRILA
IDRGIPPNTG TATLTINVKD INDEDPTFRA VPGPVPKVRE NSPPQQVTTL YGVDPDGTPY
GAPFTFEAVC IASICDKFSL DFSPLGDNGN GLATIRSRVN FNREDQKFYY LPIKMTDMRG
HPDQSTLGRT ATSTLTIEIG DENDNPHSPA HQNIHVYNYK GLFGNIDIGQ VSDTDLDDDD
IDDKTFTLLG SQQALQYFTV NKSSGMIRML EHVPATVTGY NLQVDIFDRV FDTLKVVSTV
TVYITDLPEE APYRSGSIRL TGTTPEDFIK KPQNGESPYT KFRLRMKEKL NVRKIDNVQI
ISVQATTVDG VDYTDVRYAA YGSPYFQGSQ LDGIVNQYKD EFQQDTGATI AMVGIDMCYR
EVCEGGGCDN KLVVYDEPNM VTTNGQSVVG VKTGIMAECA CTVSTNVKSC TPDYCMNGGT
CKMNNWDVIS CECLAGFDGP RCQVTKQGFD GTGYAIYEPL KQCENSLTSI EFITTKANGL
ILYSGPVTDD LDPNAPQDFM YLQLTGGYPE LVLDHGSGNV TLTLNGRDSQ GQVKMNPLND
GTWHKIDITR QGKFVTMTVD HCLSADSSEG QDQDRAPCES SGLTRGENIF LNVNAPLQMG
GRYVDTDYPK GVSKEKFKGC VRNMRHNGEL YNLYTKNFYP GSYDGCPDED NACEGSVDQP
KKCGENGKCE LVALPQTTRC ICNPGYRGTS CETATTEKFF LSKSYMDWAL QQQFHASLNT
RKMDVQLMYR TRQKHGMIFH VTGEGIGEFI KLEIVDNVIQ VLYNLGDGNK VLQMVNVTAA
DGYWHTLYFQ RRGRSIVLSQ DGGEGPMFVE TSVDSKYQEL TVKQNQIYAG AEVSYEHSKT
IDQTNSKDLE NSCLNDIRMD MKWFPMTATE NSQNNDIKMV AEAQTTNNCT RDDCAGNICG
MNGKICIPLW GMHKCVCPPH HQEIGGKCVF IDYCQNSPCH HLATCVSDRD NTEFGYYCNC
PPKMSGRLCN VYKEPIVVTE ASSSVWIIVL AVILILLLIV VAIILAYYIR RRKAQDQENI
MNYEKDDYDI RENIVDYDED GAGEDDHEGY DINRLRKPAD LTRMDKPIMA THSRPLKSGP
PGGTVGDFIT DRLDDTNNDP DAPPHDTLHD FEYEGEGSDA GSLSSLNTTS SGGDQDYDFL
NEWGRKFSKL ADMYNNYEDD SD
//
