ID A0A3B4T3F9_SERDU Unreviewed; 1654 AA.
AC A0A3B4T3F9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=von Willebrand factor D and EGF domains {ECO:0000313|Ensembl:ENSSDUP00000000610.1};
GN Name=VWDE {ECO:0000313|Ensembl:ENSSDUP00000000610.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000000610.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000000610.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR STRING; 41447.ENSSDUP00000000610; -.
DR Ensembl; ENSSDUT00000000652.1; ENSSDUP00000000610.1; ENSSDUG00000000481.1.
DR GeneTree; ENSGT00940000160835; -.
DR OMA; GNLCTCA; -.
DR Proteomes; UP000261420; Unplaced.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR CDD; cd00054; EGF_CA; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.10.25.10; Laminin; 12.
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; IPR013111; EGF_extracell.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001846; VWF_type-D.
DR PANTHER; PTHR14949:SF50; 3-PHYTASE; 1.
DR PANTHER; PTHR14949; EGF-LIKE-DOMAIN, MULTIPLE 7, 8; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF12661; hEGF; 3.
DR Pfam; PF00094; VWD; 1.
DR SMART; SM00181; EGF; 15.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 6.
DR PROSITE; PS01186; EGF_2; 5.
DR PROSITE; PS50026; EGF_3; 8.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS51233; VWFD; 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 Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 295..475
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 1023..1062
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1064..1099
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1101..1140
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1424..1456
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1457..1488
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1520..1552
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1584..1616
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1617..1648
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 576..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1229..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1052..1061
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1068..1078
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1089..1098
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1428..1438
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1446..1455
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1460..1470
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1478..1487
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1524..1534
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1542..1551
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1588..1598
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1606..1615
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1620..1630
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1638..1647
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1654 AA; 179465 MW; 88030C62E2D3FCA4 CRC64;
MLAPNSQSPL CHEYSCMLIN LDLQLTVITA LFALSEMSDT LPTTPCGPDE VNVDGTCKNK
HPPAPSVPVI VSQLTGNTVY LKCSFDSSSR SSLGYVVAWS RLSPEGRKEE LKQETTIQTS
VFIELDGFNL RLGDKIYCSS SSFFLDSPDV RGASVESQEF FAGIRLRPEV SSVPEDGRLY
ELVVESTVPV PCLEESSSSM EQCTLSLQLS TSSRDEGVLG ADLSLSSCVV ELSRSPCRDG
VCGRAGIHFS PITDFVKDGN RTTQVSVKAI VTQNFLWSGY SPEPVEITVK DVPSAYCYSF
TDPHIITFDG RHYESYQIGT FVLYKSTVWP FEVHVRQWEC GSVMHAASCV CGFVARDGGD
VIAFDMCSGE MGETKPHLSV KNRDLSKSGI RITESYQGRK VTMTFSSGAF VRADVSNWGM
SLTLRAPSSD WSHTEGLCGT YDGQSDNDFH SARGATLEDL HAFISEWRLP PGSSLFDTVP
SHLSTLSPRK YCTCQTEPHL SSPRVRSQPV TSSDSTCSHY GNVHLLSVIP TLDVTAEYIG
SVELLRGNER QSLPPGHSTQ NTQDQGVDAQ LREKGFSFRA SRDEALTSAQ HRRRRGRRQT
HRYISNSPHQ SLSQSDLEGF TYFFPEDHEP AVQPDSSPTW PTPSGLTEQQ ARDQCQQTVA
HSGIAIGCGR LLEESLVSHA VTMCVTDLQL KDETSWLNAT LPLLENECER RLVEERRREE
EHQDVLAVLK CPNLCNGNGQ CSEWGCVCFP GFGSYDCSVL SDQIPEITEL EKEGLCDVRQ
GDCSAIQVYG QGFKDSYELK CEFVKEKFVD GDWVLDEPQF VLATFLDVTA LECQLPLEDG
RTPSSLDLET VINRPLARWQ IKVSNDGYSY SNAKILTLYD GACQICSLNT EILCTLREKT
CNIDGLCYSE GESNPSSPCL TCRPDSSKHT WSIAEKNAPP VLQSLPFGLR SFKGENFIYQ
LQAEDPEGSA VLFTLISSPE GASLSAAGLL MWKATAETTD THTFHFTVTD DCNAETRASV
QVSVRSCECL NGASCVTNVN LPVGSGEYLC VCLDGFRGER CEVDIDDCKP NPCRLGRCID
GPNSFSCICP PGMTGRTCRE DVDECVSQPC FPGVSCNNTL GSFICGVCPH GYSGDGKHCT
RNTDSTVKAG TTPPRIPQVS LKPKPSGGSP CSRRPCHPGV QCFESIHVSA GFVCGPCPPG
LHGNGRTCSA TPGQGTVADG ADGHIHITRS NSSKEMTPTT SSSSSSSSPT SPRRTSDRRT
RPEATISTTR RVSSSDRKAT ATPQNQTAAS VFAPTVLRGQ PSGVELTPDL TTGVKWGPPP
HRITCADSPC FPGVPCEPTA TGSFRCGRCP YGYTGDGVTC KAVCRYQCGR NMECSLPNTC
SCKEGYTGYN CHIAVCRPDC KNQGKCVKPD VCECPAGYRG PTCEEASCEP PCRHGGTCLA
RNLCTCPYGY VGPRCEIMVC NRHCENGGEC VSPDVCRCKP GWYGPTCNSA LCQPVCLNGG
TCMKPNVCAC PSGFYGSQCQ IAVCSPPCKN GGQCMRNNVC SCPEGYTGKR CQKSVCEPMC
MNKGKCVGPN TCSCASGWRG RRCNIPVCLQ KCKNGGECVG PNTCHCPSGW EGLQCQTPVC
KQRCLNGGRC VLPDYCHCRK GYKGLTCTVK ASQA
//
