ID A0A0V0WG54_9BILA Unreviewed; 1640 AA.
AC A0A0V0WG54;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Multiple epidermal growth factor-like domains protein 11 {ECO:0000313|EMBL:KRX74565.1};
GN Name=Megf11 {ECO:0000313|EMBL:KRX74565.1};
GN ORFNames=T06_520 {ECO:0000313|EMBL:KRX74565.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX74565.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX74565.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX74565.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR601577-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR601577-2};
CC -!- SIMILARITY: Belongs to the peptidase M8 family.
CC {ECO:0000256|ARBA:ARBA00005860}.
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:KRX74565.1}.
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DR EMBL; JYDK01000143; KRX74565.1; -; Genomic_DNA.
DR STRING; 92179.A0A0V0WG54; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00055; EGF_Lam; 4.
DR Gene3D; 3.10.170.20; -; 1.
DR Gene3D; 3.90.132.10; Leishmanolysin , domain 2; 1.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 5.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR011489; EMI_domain.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR042635; MEGF10/SREC1/2-like.
DR InterPro; IPR001577; Peptidase_M8.
DR PANTHER; PTHR24043:SF8; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24043; SCAVENGER RECEPTOR CLASS F; 1.
DR Pfam; PF07974; EGF_2; 2.
DR Pfam; PF00053; Laminin_EGF; 5.
DR Pfam; PF01457; Peptidase_M8; 1.
DR PRINTS; PR00011; EGFLAMININ.
DR PRINTS; PR00782; LSHMANOLYSIN.
DR SMART; SM00181; EGF; 16.
DR SMART; SM00180; EGF_Lam; 16.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS00022; EGF_1; 10.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 7.
DR PROSITE; PS51041; EMI; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR601577-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|PIRSR:PIRSR601577-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR601577-2}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 895..914
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..111
FT /note="EMI"
FT /evidence="ECO:0000259|PROSITE:PS51041"
FT DOMAIN 148..183
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 191..226
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 233..268
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 456..486
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 580..615
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 623..661
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 718..749
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT ACT_SITE 1239
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-1"
FT BINDING 1238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 1242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT BINDING 1321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR601577-2"
FT DISULFID 173..182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 216..225
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 258..267
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 476..485
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 605..614
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 651..660
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 739..748
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1640 AA; 181401 MW; FF035B26E728952C CRC64;
MQLRIMFVHV GGSIWTICFV FLILFVTESF SLSGPNVCSK LVGVEKWHVV EYQRPYMYRT
HDFCWDFYKG FRCEKNKVAF KTSQRNESYI SEELQSVCCD GYDEMNDTCI PVCSQPCSHG
HCSSPESCTC LPGWGGKQCN KSCPHNHYGD QCEMDCKCEN GASCDPVSGE CFCRAGYRGR
HCTLACSEGT YGENCAQLCH CLNGGSCDHR NGKCSCLPGF EGVLCEKKCA GRHGQDCQWE
CQCKNNGQCD HITGICECTP GWTGILCDQP CPPGKYGSNC SLTCECQNEA VCDPINGTCH
CQIGFSGFKC EQPCQPGYFG LNCTQVCDCE NAKYCRPSDG KCICNDGFHG DKCENRVCPH
DRHGLNCSSM CPCVMENTKM CHPVTGKCYC KAGWTGLTCN EICPTYMYGE NCRNLCQCKN
DAYCDAKTGA CICQPGFHGD KCELPCKTGK FGRNCLMNCT CQNDGICIGT TGECSCKPGW
TGIDCDLPCP AGRYGDRCNQ TCPCGTPPNG CTPVDGVCHC AAGYVGKHCE LVCQPGKYGL
SCMQNCSCQP VSCNPFTGMC ICDAGKYGLD CSSACKDGFY GEDCSKQCHC SEHGTCDELT
GDCICQPGYM GAQCERSCPV GMYGKNCEMK CQNCVHSDGQ NCHPDTGQCL CLPGYQGVHC
EHACSAEYYG RKCSERCRCN LAFSFCHHVT GECQCFPGKT GADCSEDCPE GTFGRSCAQQ
CLECFNGGQC DAIDGTCICR AGFAGPRCET PCPAGTWGVG CVNQCNCTVG AFCNGTNGNC
HCPAGLHGVF CDEYCPFGKY GPNCAKSCKC SAFAKGCHPI TGVCVCPSGF IGSKCETVCQ
PNTYGTNCKE ICQCKPDEIC HPSIGCCKGA ACPSGIMLPF VYDGSSSTTG LSTTVAIVVT
VLILVVFLLV LLVGHYRKKY MLERDPPLPS VRYSNNQQCV QASERSGVDN PLYDPFAQKS
QKMMMQNNTS EDYPWTRPIN SGGSGVGGSF TKASSFDDGP SVNHEKMKLK FDDEDDYDDE
IQSEQSGVYA VPDYERMRYN YGVVGDNLNA PTAEKKEKAW VKEGSDRHQG TAPQSSFVQK
SSVMTEKEES VFIERQFKPI RIRMVVSDAF KAAYNNEQMA VLEEAFNETL NFLQTTIRVR
RLKIPIDLES YNCFNYTHFP IESDWLKKGV LHTDLIIFVD SKHTASCSNP DITLAFAATC
PPKLNFINRP VFGYVAICRN STAAKQWNVY SISNTVIHEI LHVMVFNDFS MHTITTMIHN
AYNSFGIEQQ WKVNDNVTVT QQTNFVSTPR VLKFVREHFN CPDLIGAQLE DNGGPGTIRS
HWKKRLFGNE IMTGKLSNQI VLSPLTSAFM EDSGWYMVNY SNVGQLEYGK GAGCTFAQKS
CSEYVDSVKD EPFAAYPYCN WADFVTRENF GATKLARCTK DRTRYIYCNF VVNKTISDKY
GYFRDKTAIL DDGEIVSGVH VTGGEELFNH CPVWQELQWK WWQNHFEDSI CHHTIGDTNP
DLNFGAESRG PNTICVEQIS AFAILRSMGF SIFSFSTTSY DTKFGAGCYR YKCYKGRLMV
HAASNLMDTI PQAEYKICWY AGALLRFARH FRSNDGRYQV HRGSLICPPC EEICTKNDKN
FQCEPDIIGI ESRDLMLPNY
//
