ID A0A2G8KWS5_STIJA Unreviewed; 1107 AA.
AC A0A2G8KWS5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN ORFNames=BSL78_10622 {ECO:0000313|EMBL:PIK52464.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK52464.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK52464.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK52464.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK52464.1};
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 -!- 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:PIK52464.1}.
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DR EMBL; MRZV01000327; PIK52464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8KWS5; -.
DR STRING; 307972.A0A2G8KWS5; -.
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:0007399; P:nervous system development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 12.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 13.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR PANTHER; PTHR24049:SF22; DROSOPHILA CRUMBS HOMOLOG; 1.
DR Pfam; PF00008; EGF; 9.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR00010; EGFBLOOD.
DR PRINTS; PR01983; NOTCH.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00179; EGF_CA; 12.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 11.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 8.
DR PROSITE; PS00022; EGF_1; 13.
DR PROSITE; PS01186; EGF_2; 7.
DR PROSITE; PS50026; EGF_3; 13.
DR PROSITE; PS01187; EGF_CA; 3.
DR PROSITE; PS50092; TSP1; 1.
PE 4: Predicted;
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1069..1091
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..47
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 49..85
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 87..123
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 125..162
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 164..200
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 202..238
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 239..275
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 277..314
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 316..352
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 354..390
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 392..428
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 627..661
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 663..699
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 37..46
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 75..84
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 113..122
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 152..161
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 190..199
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 228..237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 265..274
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 304..313
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 342..351
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 380..389
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 418..427
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 651..660
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 689..698
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1107 AA; 121183 MW; 0ACA37DDE10FED54 CRC64;
MKSYSINCEI DINECLPNPC LNQASCVDAV ASYACICQPG YTGTNCEVEI DECEDHRCEN
GATCIDLLNR YACECVFGHE GELCDVVTDY CASNPCAEGS SCLARIGGFS CLCPDWLTGD
LCEENVDRCL GSPCQHGSTC VDGVAAGYRC LCTIGYVGLH CQTDLDDCHT QPCHHGGSCV
DLVNGYTCQC PEGYSGTLCE ENIDDCSDHN CINGASCIDG VASYHCNCSQ DWTGQFCEEF
IPCQRNPCNN GGVCGEDGGF RYCSCLLGFS GSLCEENIDD CIGSARCENG GECIDLVNDY
FCECREGFSG DHCEMDGDDC VDEPCYNQAT CVDGVASFAC LCPPAFSGEL CEEFINPCEV
QPCRNGGSCY NFGLTSVCEC RAGFYGDRCE HETNECQSSP CQNSGFCVDH VDGYECLCLP
AFTGTDCQTK LPGDADLKFE TSGGADMLFL DGIYEEFDFT FLKLGYWFRA TGHAGDFVLF
EYTPINATEA DLKVYNVSHI KVELFGNETF ELDRDLSDGQ WHNLVVTAIP DEKIEISLDG
EFVENRTLPV AGIYFKLGGS ARIGFTEGEN VAEVLVSGAH LWSYEVGETF TQCQPDDSGD
VLAWEQILAM SQRGNARLPL TPSVCDDVNS CQENPCGGTC VDTLDGYYCI CPEGYTGDLC
EYWIDFCLEH YCQNDASCVS TANNFTCLCP DHFTGSICEI PIVTGGWSDW SIWSDCSVTC
GNGTHTRERH CNNPIPANGG ADCQGPSSEV KACHNGTCRG CTDMVLPPHT TLDCGKRGEE
RQCGLYCVPP YTFISPPANV YTCGPTTNFS WSDGARFGDD VVLPGCTARI RRSAVKIEVQ
IHLPGLTCES ERDQLEAEDQ LSLQLQKWKK EIPCLFQELC IISEVAVSNC HPETSYPRLF
HSQANVARAV ISLVQNVNNT QGDDNTDTTE DDADQHLQAS IDAIKQLVTS HGLDFGRPDK
ILIQDNSTIF VDGWDVCPPG TIESHQDHFC YPCSEGTYRT YDPLQEDFEC QLCPLNSYQD
EEATDTCKVC PTGGKTIGYG STSLSDCLGE VEYSYWKSLE GEPGINLHLY YWCIATVVVV
VLLLATAFVI VRFQRTKNFQ QKLDVNT
//
