ID A0A183A931_9TREM Unreviewed; 2355 AA.
AC A0A183A931;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Laminin EGF-like domain-containing protein {ECO:0000313|WBParaSite:ECPE_0000346901-mRNA-1};
GN ORFNames=ECPE_LOCUS3466 {ECO:0000313|EMBL:VDP69595.1};
OS Echinostoma caproni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC Echinostoma.
OX NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0000346901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ECPE_0000346901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP69595.1, ECO:0000313|Proteomes:UP000272942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Egypt {ECO:0000313|EMBL:VDP69595.1,
RC ECO:0000313|Proteomes:UP000272942};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
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DR EMBL; UZAN01040418; VDP69595.1; -; Genomic_DNA.
DR WBParaSite; ECPE_0000346901-mRNA-1; ECPE_0000346901-mRNA-1; ECPE_0000346901.
DR Proteomes; UP000050740; Unplaced.
DR Proteomes; UP000272942; Unassembled WGS sequence.
DR CDD; cd00055; EGF_Lam; 6.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF365; NETRIN-A-RELATED; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00053; Laminin_EGF; 6.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00180; EGF_Lam; 6.
DR SUPFAM; SSF57196; EGF/Laminin; 5.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01248; EGF_LAM_1; 2.
DR PROSITE; PS50027; EGF_LAM_2; 4.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000272942}.
FT DOMAIN 1..38
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 39..92
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 442..489
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 547..593
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT REGION 1715..1736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1876..1896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 929..1003
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1049..1122
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1718..1733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 11..20
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 66..75
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 461..470
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 473..487
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 547..559
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 549..566
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 568..577
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 2355 AA; 261941 MW; 4FF00C53FF21C394 CRC64;
MCDPNTGKCN CGQNVIGDSC DQCRSGHYWN VTGPNCLPCD CGIGTELSET VGRASSCNME
TGQCECAPHV TGRQCTECEP GYFGVSPAGC QPCPMCPNGQ VCDQITGKCI CPPYTQGDRC
EECAPGSYDY NPITGCKIIS SDRESVPGGS LIQLSVGLGA EASTDLSIGV NQFDWRFSTH
RPTFMEIPEL KGSLVRYRTM RNYGSVVIAI STECLRTGDC RLNAPDSRYP MELMTTGPAV
NRDEAGGFIV RMPYRIDAKM TALNGTLQLE YQPAVSRYSF TECSFSTSVI QEAWKDDTQT
TMVDGFRHIW LRESDWVLTK VVGHDTRVRP SRNELMLALL NVTSFSVRLF MPEANPKMVS
VRYRIYEALT ETTTVSGTPI RSIEKCDCTN TASGDHCEIA SPGFYFPQLI PKPGPSIVPP
APGAEPPKWP ENIIWTGGVE KCRCNGMSSH CDPVTGVCES CTGNTMGPDC GQCATGYMGD
PKQGLPCVKC HCPTEQTDYA ITCIPAPDRP YVSHQCICKP GYSGARCEVC APGYYGDPTS
LIACQPCDCD MAGSLSPNCA QDTGQCRCAP GVHGRRCDQC EPDHVVDAGR CIDCRGPCTG
ELFTKADEVM MQIDNLNVTS LAYRGLARLG QQVETVRKRF SPAREQAERE LIARTQQVAK
QTVQLREQVD RAQVTADAIQ TTRCVTLGNG TELREDVASF RRRVSDWIQE VREAPTGRPD
QATLQRWREE ARRVLTELGT INLNSTEEWV NQLLSSAERA MEAANALLKS VKPGKSAVDL
ERLVTYQEEQ ARLLDFQQSQ IYRIGNATQS TIRELNAAKA KSDKLEKAAQ EAIDPAVMRA
FENSIKNVND QLGEWDQSEV TKVEQKLAES KSALKQLNGV VLIELKDVEI PTTLRMKVVE
PMEREVDSIV RTLRPNSRLN RTMEALEAYQ TIVDNMQAAE NATEEAEEAL KKSTAGQDQT
WQSMMNEVAA KGTKIETVLD QEEERLAQRN ETLNEALRKL DKVSIDLTMI GKTAEESLTY
SKETIDKVKK VTQVLEVTEP LAQNASDRSE TQRVKLDDLA DRLQQMENRY AQLQGTAQSM
VDQANSTQLN LVKLIGDAEN SIKQLDSKLL NLRRLADEAR SMLDVTYGAL AQDPVPIELG
RSCVYSLVPY ALTKSRVFDI EFWFKVHDLQ TAMNSVIMVG RRAFAGRTQM FAFTLEAPAP
TLRFSWNVMG GKVEIGPIRE AIWYQVRVTS VLGETRMMLT ARPEDDEVPI EPRTREATTL
AGADHPESAL MLDRQMELRV GGVIQAGTRL VSPESWGDNA AEAFWSRLLS MGSPEVCMLN
LRLGGMRMSM VDLATATPSC LRPKRLRCQM AGKLNQVTTR MRPAQSTQPQ YVLQLLFYYD
FAGTGGYARL GSSTDLQFCK DFLQFQLTPL DEARKERMMG FTFFDYRKDF GVTIEWVDGR
PRATRWAGDE LYRSIHSSDL LEAGETMRRR VLRATVASPN NYGHSRWRRN AFMESGKDKV
VESISLNYPQ QKVWRLDKLL TPECHEDTIL FIGSIPPGHY SLRRRVAEGR IGLGKDKTGG
DGDLYLDDYV MTPVNQFGDS YFTDLRQRGE SFVVENTKPD SQYCLRLTPH DAYTQLELDH
AKMGSPFNPG VSMTIRFNPL RTITEDVDLL RVQLSSAEWF RVYLTNDHRL GILIPGGRKE
LITREPLSYR PLEDPSFALR DLELAEARMI NASTRAWKEQ DRTSEEESKL PTESLRTDAW
SSSGEIEVAV TLHFGGSDSR QLYVLYDQRV VQSWTIPRQM SDAQVQQILV GPHTKISQPI
TINYLVIGRK LVDFSTELTG TDDLNGSHVG FCGGQLHPRF FERQGLVGPV WIEQGLDLAP
PPGGRRLRFV EPGSPEANVT LPGVSPPTPV KPTGRLRREE RTTVLLSPSF LSIHTPFLFS
DGPFVFKIGF RAQLSRGTSG TANSGSPLPT FRYSLLAAFN FGPNVENLYL IVSESQIFLT
NSQNVLWSSP HLTIADTNWH QLILTSPAET NGNGAPAGAA TANELNGPAV ESGIHMLFDG
RDLWLPPLQS DLKPILAFIG GLPSGQKLNL DPDTNIAPIT GLFGCVDELE INGVQIDPKQ
SGRPACYDCF SLDPNIVHIP QSIEQYLDNN LIPLEIPKAF LEPDTPQITF DFSIFYDREI
LPAASLFVLS FEGEQNGDPV THRIWIHLAD AEVKMSPAPY DEPLTDLGHT APLLTLPRYA
NTWQFIKLQM FFDYGNVVLQ LQSQVVITPE EQKTIVLGST SHTFTGCIRD MRLTSSTGVE
TIWIRPVPDH VDWCHTNGTQ TKESTVEESN LVDGHGTAKE FTKPVDPQSR QLMVPGIAVL
VSLRRNIERP VKLPG
//
