ID B3SC70_TRIAD Unreviewed; 281 AA.
AC B3SC70;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN ORFNames=TRIADDRAFT_61862 {ECO:0000313|EMBL:EDV19668.1};
OS Trichoplax adhaerens (Trichoplax reptans).
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV19668.1, ECO:0000313|Proteomes:UP000009022};
RN [1] {ECO:0000313|EMBL:EDV19668.1, ECO:0000313|Proteomes:UP000009022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV19668.1,
RC ECO:0000313|Proteomes:UP000009022};
RX PubMed=18719581; DOI=10.1038/nature07191;
RA Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA Rokhsar D.S.;
RT "The Trichoplax genome and the nature of placozoans.";
RL Nature 454:955-960(2008).
CC -!- SIMILARITY: Belongs to the CRELD family.
CC {ECO:0000256|ARBA:ARBA00005897}.
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; DS985268; EDV19668.1; -; Genomic_DNA.
DR RefSeq; XP_002117825.1; XM_002117789.1.
DR AlphaFoldDB; B3SC70; -.
DR STRING; 10228.B3SC70; -.
DR EnsemblMetazoa; TriadT61862; TriadP61862; TriadG61862.
DR GeneID; 6759056; -.
DR KEGG; tad:TRIADDRAFT_61862; -.
DR CTD; 6759056; -.
DR eggNOG; KOG4260; Eukaryota.
DR HOGENOM; CLU_038974_0_1_1; -.
DR InParanoid; B3SC70; -.
DR OMA; ECEANAC; -.
DR OrthoDB; 337149at2759; -.
DR PhylomeDB; B3SC70; -.
DR Proteomes; UP000009022; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR InterPro; IPR021852; DUF3456.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24038:SF12; INTEGRIN BETA-LIKE PROTEIN E; 1.
DR PANTHER; PTHR24038; STABILIN; 1.
DR Pfam; PF11938; DUF3456; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01248; EGF_LAM_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000009022};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..281
FT /note="EGF-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002798570"
FT DOMAIN 158..192
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 207..246
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 246..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 182..191
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 281 AA; 31404 MW; C2E96154002E996E CRC64;
MAGRKHWPRF GSFFAFLLVL LLCNRIVNAK EEDEDNGKDR VMKRCIDCRK LAVSFEIGLD
LTNRKGYGGG DVVWEEKKLG KYENSEMRLL DITEKTCKRK DFQCNTMLEN YEDEIEKWFF
KLRQDETDFA EWFCEKTLKV CCPFNTFGPD CQACPGNGEF SCSQHGKCHG NGTRSGNGSC
ICETGYSGSV CENCTTGYVQ KGSECNDINE CEANACDVSL ENCENTEGSF ICTCKEGFQK
EGDVCVPAEP TEGTESSTDD SAATNAVEEE KAAEVDSHEE L
//
