ID A0A0V0ZK56_9BILA Unreviewed; 1095 AA.
AC A0A0V0ZK56;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Multiple epidermal growth factor-like domains protein 11 {ECO:0000313|EMBL:KRY12670.1};
GN Name=MEGF11 {ECO:0000313|EMBL:KRY12670.1};
GN ORFNames=T12_1843 {ECO:0000313|EMBL:KRY12670.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY12670.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY12670.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY12670.1};
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 -!- 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:KRY12670.1}.
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DR EMBL; JYDQ01000159; KRY12670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZK56; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR CDD; cd00055; EGF_Lam; 2.
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 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; 4.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 14.
DR SMART; SM00180; EGF_Lam; 13.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS51041; EMI; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 906..925
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 REGION 1066..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 1095 AA; 119076 MW; A3C1C916415CABA1 CRC64;
MQLRIMFVHA GGSIWTMCFV FLILFVTESF SLSGPNVCSK LVGVEKWRVV EYKRPYMYRT
HDFCWDFYKG FRCERNKVAF KTSQRNESYI SAELQSVCCD GYDEMNDTCI PVCSQPCSHG
HCSSPESCTC LPGWGGKQCN KSCPHNHYGD QCEMDCKCEN GASCDPVSGE CFCRAGYRGR
HCTLACSEGT YGENCAQLCH CLNGGSCDHR NGKCSCLPGF EGVLCEKKCA GRHGQDCQWE
CQCKNNGQCD HITGVCECTP GWTGILCDQP CPPGKYGSNC SLTCECQNEA VCDPINGTCH
CQIGFSGFKC EQPCQPGYFG LNCTQVCDCD NAKYCQPSDG KCICNDGFHG DKCENRVCPH
DRHGVNCSSM CPCVMENTKM CHPVTGKCYC KAGWTGLTCN EICPTYMYGE NCRNLCQCKN
DAYCDAKTGA CICQPGFHGD KCELPCETGK FGRNCLMNCT CQNDGICIGT TGECSCKPGW
TGIDCDLPCP AGRYGDRCNQ TCPCGTPPNG CTPVDGVCHC AAGYVGKHCE LVCQPGKYGL
SCMQNCSCQP VSCNPFTGMC ICDAGKYGLD CSSACKDGFY GEDCSKQCHC SEHGTCDELT
GDCICQPGYM GAQCERSCPV GMYGKNCEMK CQNCVHSDGQ NCHPDTGQCL CLPGYQGPVR
PNITAENVLN GVGAIWRSVS VTTSPENVSA FLERPGLTAV KTVLKEHLDE VVLSSVWNAS
TAVSVMRSMV LAFVEPALPD QDAKHLVQLE HGILYNKHIF LLKIFLPRGV GCVNQCNCTV
GAFCNGTNGN CHCPAGLHGV FCDEYCPFGK YGPNCAKSCK CSAFAKGCHP ITGVCVCPSG
FIGSKCETVC QPNTYGTNCK EICQCKPDEI CHPSIGCCKG AACPSGIMLP FVYDGSSSTT
GLSTTVAIVV TVLILVVFLL VLLVGHYRKK YMLERDPPLP SVRYSNNQQC VQASERSGVD
NPLYDPFAQK SQKMMMQNNT SEDYPWTRPI NSGGSGVGGS FTKASSFDDG PSVNHEKMKL
KFDDEDDYDD EIQSEQSGVY AVPDYERMRY NYGVVGDNLN APTAEKKEKA WVKEGSDRHQ
GTAPQSSFVQ KSSVM
//
