ID A0A0M3JRJ8_ANISI Unreviewed; 859 AA.
AC A0A0M3JRJ8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN ORFNames=ASIM_LOCUS10094 {ECO:0000313|EMBL:VDK42328.1};
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001036301-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0001036301-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK42328.1, ECO:0000313|Proteomes:UP000267096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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:PRU00076}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; UYRR01030983; VDK42328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M3JRJ8; -.
DR WBParaSite; ASIM_0001036301-mRNA-1; ASIM_0001036301-mRNA-1; ASIM_0001036301.
DR Proteomes; UP000036680; Unplaced.
DR Proteomes; UP000267096; 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:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 4.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 5.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR PANTHER; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR PANTHER; PTHR22722:SF14; MEGALIN, ISOFORM A; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00057; Ldl_recept_a; 4.
DR Pfam; PF00058; Ldl_recept_b; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 5.
DR SMART; SM00135; LY; 4.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF57424; LDL receptor-like module; 4.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 5.
DR PROSITE; PS51120; LDLRB; 2.
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}; Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000267096};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 745..765
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 483..529
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 571..613
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 685..728
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 811..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 62..74
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 69..87
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 81..96
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 111..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 118..136
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 130..145
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 219..231
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 226..244
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 718..727
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 859 AA; 95712 MW; A7E4AACF266B2442 CRC64;
MVIIVQFIVH ASRGCRNETE FDCGYDEGNV HKCIPIEWMC DNLVDCRLNA RDESSCRYIH
YCPRDTLACR NGECLDAIFK CNGFDDCGDG TDERGCTEFY LNGHISAPVR CPPNQFRCNR
GPCITDYAKC DGMKDCPEGD DEENCGPTTN VTMSCSENQF MCDNSCLPLQ WKCDGQKDCD
DGTDEIEEEC GLLHEEEDEL LNLPTREEYH QISLRNSFCS PSEYLCEPGK CIPREKLCDN
HKDCPNGDDE GHRCGECASY GCSYSCVDNP DGAQCLCAEG EELAGDGRTC TDVNECDTHA
AEVCSHKCVN THGSFRCECF DGFDLSSDAR SCRAKPDPYS SILFSLGSEV RHMPLSSLGS
TTSYGIYQHN DQMGTIVRSI VFARSSNQLL MAVSNADHEG HIHSSVNGLQ KCLIGDVNGI
ANLAFDWIAQ NIYYTSQHPS NATGVGVCSL NGRFCSLLVK GIVNNEYYRR QAYRGLVVNP
LRGMMYWIDI PGSFDSPKIM TADMSGNNVR ALVSTKLEHP QGLAMDYIKQ RLYFADIELR
LIERVDVNSL ERVTITSRGV HHPYELAFFD DYIYWTDWST EALVATRVNE QETPHVVHSL
EQMPYGIAVN HSAYWNMTMR NPCEDIQCDH LCVLSVGVKG DVVGRCMCPN LYKNSEEYGC
IPMNSTEIQQ LGGARNVPSL CTTMMVEYCE KGIGCMNGGT CVKQINSHGH VEAISCNCVN
GFNGQYCELG SAWTDDELEI DDSSFLSILF LLVLLILIAI SAYLASEKCP VVRRGVDSLL
AMRLVRLINP SEEDTERIIK PKSMVYESDG FSNPSYEVPE KDKIPLSSGA APTYNTLPEH
HNASLHRTPE PPRFSIDTP
//
