ID A0A0M3JW23_ANISI Unreviewed; 1625 AA.
AC A0A0M3JW23;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Nidogen-1 {ECO:0000313|WBParaSite:ASIM_0001246001-mRNA-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_0001246001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0001246001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Secreted, extracellular space, extracellular matrix, basement membrane
CC {ECO:0000256|ARBA:ARBA00004302}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR WBParaSite; ASIM_0001246001-mRNA-1; ASIM_0001246001-mRNA-1; ASIM_0001246001.
DR Proteomes; UP000036680; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 3.
DR CDD; cd00255; nidG2; 1.
DR Gene3D; 2.40.155.10; Green fluorescent protein; 1.
DR Gene3D; 2.10.25.10; Laminin; 10.
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; IPR006605; G2_nidogen/fibulin_G2F.
DR InterPro; IPR009017; GFP.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR003886; NIDO_dom.
DR PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR PANTHER; PTHR24049:SF22; DROSOPHILA CRUMBS HOMOLOG; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF07474; G2F; 1.
DR Pfam; PF00058; Ldl_recept_b; 1.
DR Pfam; PF06119; NIDO; 1.
DR SMART; SM00181; EGF; 13.
DR SMART; SM00179; EGF_CA; 7.
DR SMART; SM00682; G2F; 1.
DR SMART; SM00135; LY; 3.
DR SMART; SM00539; NIDO; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF54511; GFP-like; 1.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 8.
DR PROSITE; PS50026; EGF_3; 10.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS51120; LDLRB; 2.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS50993; NIDOGEN_G2; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
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}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022869};
KW Secreted {ECO:0000256|ARBA:ARBA00022869}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1625
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007417887"
FT DOMAIN 137..279
FT /note="NIDO"
FT /evidence="ECO:0000259|PROSITE:PS51220"
FT DOMAIN 522..747
FT /note="Nidogen G2 beta-barrel"
FT /evidence="ECO:0000259|PROSITE:PS50993"
FT DOMAIN 820..858
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 923..962
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 977..1018
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1028..1072
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1092..1133
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1149..1191
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1192..1235
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1239..1282
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1285..1322
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1323..1364
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 1411..1453
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1454..1498
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DISULFID 987..1004
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1102..1119
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1159..1176
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1204..1221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1250..1267
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1625 AA; 180993 MW; 13D522B624C12C6D CRC64;
LPCKVIFSLF FLLPLAYSTK LYRFGPDEAD QDKCHFKEIS YSSEPSAVTL DVPIVYFEET
QNAIYISSNG IVSFGKPIED DQESVRNLDD ERINAIAVFY VPTSGGTIYY RSIFLNAYKN
LMEFFLQIIA IDRAEPYYIT NVRKYLMKID PARATSSDND LLNDLSDRIN RNFPTGDSGE
FRALHAILIT WDDVSASDAD GLNQYQLAIA TDGLNSYAVF IYNRIDWTTS HDKIAQAGLY
FSDGRRQSMV NSGTPNIREL INYSNNQKEG SYIFRISGGS PEDPRVSDVD EDYSYNDYEA
EYNPDEEFRR PQQPSANCPP DPYRYSCPTE CEVLTDDRGC SLCICTQSPA YQPSTAQQSP
NDITNSIATP VQSYQYVPVA YPGESPTQPE DAINRVDEAP RVSYGGQQGS VSGSDIHQFQ
PNKPIYSSVD HPIPQPRQPP SDIEQHIEIA DTPSRVDSLS HSTSNFGQDR DMALSCAQAS
ETIQPCHDHA RCIDYNPGYC CQCLDGYYGN GKECLRNGNP CDPQRINGYF EGVINGEEIG
RTDLHTYVMT AEGRAYMALS QIPAHLGRSL LLLNPIGSAM GWLFAKVESP SSYNGFQLTG
GLFNRTINVH IGDRSAVTIK QQFSGRDIHH YFKANIFVTG TLPQLAEGVQ VIYPDHEEEY
RREGPGFVRS YSSLDVLVNE HGQERTIRLT IDQQIHFAEC PYKTFSKDSI VVVKVTRPHV
VYDTEERIVR YASANAATSE RSHIVVEEAT DEGQEQQQQI SASGRHLAHE ARDPCAEGHH
LCTLPNMFCT RVDPSYRCEC QKGYQTMPDA STHLGWKCID LNECDRGDHT CDRNAVCTNT
DGSFKCDCRP GYEGDGFQCY SSEQPSKGGC HSHQECHQWG ECVFGHNGHP GHCKCRGWYV
GDGVKHCGPP EEQPRVPERE EIDENLCGGY TCDANADCIT VQSGGEQCVC RRGFYGNGVQ
CEQVADTMRP AVHTVSVGSV CRSHDECGEH GNCVYGNDVG FYRCVCVPPY KSDGTRCVQD
ETQDIESVQM SCDLENICDL NADCVFERGP DDEGYYRCIC RPGFTGDGIR CIRTTIDHIP
FDTSEQEEVL VEQQYCDTLH NCDVNAECIF DPQIGHYICR CMPNFEGDGY SCPPIHPHLV
TQPPQPTDVR RSCHDASDCH RNAHCVVREN SFEYFCECLP GFKGDGVNVC KSADECNPTD
PQTCHEHAEC VYGQVESAFV CKCIQGYVGD GLTCTPQARP PSCDQEPTVC HMNAQCIYNT
EQDKHICICQ PGSIGDGYNS CEIQDAPRCG RCSTFARCVQ QENGAWSCEC NPGYQGNGHV
CSALSSCLDD PSICDPNAEC VPGGHGQYVC NCHYGYHGNG RTCTPDTEGR EQGLLIGRGM
TVIQRGTNPD IHGKQSELQS PEGIVVDWSS RNVYYADSVK DEIGVATLDG KYQKALITEG
LVNPRALAID LRDRHLYYSD WHRENPLIGR VDLDGRNNKV FINTDLNLPN GLTILQERRE
LCWVDAGMQR LSCIGLDGHN RRVVFAPLEY PFGLTNHNEQ RFYWTDWKDN QIHSVSIYGD
GYTSFPPTMG GTGRLYGIMS VPLQCKGTAN GCAVNNGGCQ YMCLPGTTQV RCACPDNVQD
LEGCS
//
