GenomeNet

Database: UniProt
Entry: F1RAG3_DANRE
LinkDB: F1RAG3_DANRE
Original site: F1RAG3_DANRE 
ID   F1RAG3_DANRE            Unreviewed;      1175 AA.
AC   F1RAG3; A0A8N7UUY5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   27-MAR-2024, entry version 92.
DE   SubName: Full=Nidogen 1a {ECO:0000313|Ensembl:ENSDARP00000090249};
DE   SubName: Full=Nidogen-1 isoform X1 {ECO:0000313|RefSeq:XP_691156.5};
GN   Name=nid1a {ECO:0000313|Ensembl:ENSDARP00000090249,
GN   ECO:0000313|RefSeq:XP_691156.5, ECO:0000313|ZFIN:ZDB-GENE-050302-58};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000090249};
RN   [1] {ECO:0000313|Ensembl:ENSDARP00000090249}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000090249};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000090249, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000090249};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [3] {ECO:0000313|RefSeq:XP_691156.5}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|RefSeq:XP_691156.5};
RG   RefSeq;
RL   Submitted (NOV-2023) 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   EMBL; AL928828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU367849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU651583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_691156.5; XM_686064.8.
DR   STRING; 7955.ENSDARP00000090249; -.
DR   Ensembl; ENSDART00000099475; ENSDARP00000090249; ENSDARG00000068710.
DR   Ensembl; ENSDART00000099475.6; ENSDARP00000090249.4; ENSDARG00000068710.7.
DR   GeneID; 562690; -.
DR   AGR; ZFIN:ZDB-GENE-050302-58; -.
DR   CTD; 562690; -.
DR   ZFIN; ZDB-GENE-050302-58; nid1a.
DR   eggNOG; KOG1214; Eukaryota.
DR   HOGENOM; CLU_003163_1_0_1; -.
DR   OMA; PGTGNQF; -.
DR   OrthoDB; 25347at2759; -.
DR   TreeFam; TF320666; -.
DR   Reactome; R-DRE-1474228; Degradation of the extracellular matrix.
DR   Reactome; R-DRE-3000157; Laminin interactions.
DR   Proteomes; UP000000437; Chromosome 13.
DR   Bgee; ENSDARG00000068710; Expressed in pharyngeal gill and 26 other cell types or tissues.
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:0042813; F:Wnt receptor activity; IBA:GO_Central.
DR   GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 3.
DR   CDD; cd00255; nidG2; 1.
DR   CDD; cd00191; TY; 1.
DR   Gene3D; 2.40.155.10; Green fluorescent protein; 1.
DR   Gene3D; 2.10.25.10; Laminin; 5.
DR   Gene3D; 4.10.800.10; Thyroglobulin type-1; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR026823; cEGF.
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; IPR024731; EGF_dom.
DR   InterPro; IPR006605; G2_nidogen/fibulin_G2F.
DR   InterPro; IPR009017; GFP.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR003886; NIDO_dom.
DR   InterPro; IPR000716; Thyroglobulin_1.
DR   InterPro; IPR036857; Thyroglobulin_1_sf.
DR   PANTHER; PTHR46513:SF6; NIDOGEN-1; 1.
DR   PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF12947; EGF_3; 2.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF07474; G2F; 1.
DR   Pfam; PF00058; Ldl_recept_b; 3.
DR   Pfam; PF06119; NIDO; 1.
DR   Pfam; PF00086; Thyroglobulin_1; 1.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00682; G2F; 1.
DR   SMART; SM00135; LY; 4.
DR   SMART; SM00539; NIDO; 1.
DR   SMART; SM00211; TY; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF54511; GFP-like; 1.
DR   SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1.
DR   SUPFAM; SSF63825; YWTD domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS51120; LDLRB; 3.
DR   PROSITE; PS51220; NIDO; 1.
DR   PROSITE; PS50993; NIDOGEN_G2; 1.
DR   PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE   1: Evidence at protein level;
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:PRU00500};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022869};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:F1RAG3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022869}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1175
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041116794"
FT   DOMAIN          99..252
FT                   /note="NIDO"
FT                   /evidence="ECO:0000259|PROSITE:PS51220"
FT   DOMAIN          374..603
FT                   /note="Nidogen G2 beta-barrel"
FT                   /evidence="ECO:0000259|PROSITE:PS50993"
FT   DOMAIN          602..643
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          644..686
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          691..734
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          735..773
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          778..848
FT                   /note="Thyroglobulin type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51162"
FT   REPEAT          918..960
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          961..1003
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   REPEAT          1004..1048
FT                   /note="LDL-receptor class B"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT   DISULFID        818..825
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ   SEQUENCE   1175 AA;  130100 MW;  5AF20E955A1CAF88 CRC64;
     MGRHGHRHPF WVILFGLTLS VSGITRHELF PFGRNAGDQS LREGNDETQE VNLDKPITFH
     DEQFSKIYIN TNGFVALEKP TGESEYLENM PASFKMIAAL QGDLDTSDGV GKVFFRQDFS
     TALLQQAADH INRAFPEDDL VNPIHALVVT WLDVASHKAE SRGDGLEHSI RRNTFQLVIA
     SVETSSYAIL LYPRDSIQFQ STGSGYTVHA GFSKTQELYY RNTEDTEASV KDLPEQTNSG
     KRGVWVYEIG TFPHFTNIAP GEVPDLPLDS LRRSETQNQQ QQVYPDVQQE NLDGVYHHPE
     HPPPIQVHTV QFTPQDPQVV EIENDDNIQV DVFTYNSGQC GGQKCSKFAE CSGRCCVCKP
     GYYGSGVHCV PEGVPQRMNG KVSGRVFVGN SPVPVDFASN DLHSYVVAND GRAYVAISAI
     PPVIGFSLQP LSSVGGVIGW AFALQQPGFK NGFSIIGGEF KRQADVSFQP GGEKLTISQE
     FRGIDEHDHL MVDTRLEGKI PEVPQGATVQ IDSYSEIYQY SINLITSSST REYVISLPDG
     STQSRSYNFR ETITFQGCQF DEVPSTQMLS VEQVFVMYDM GAQLLRYAMS NKIGDVNGGQ
     SEENACFTGR HGCDTNAVCK PGQGNQFTCE CAAGFTGDGR ACYDIDECRE TPQICGQNSI
     CNNQPGTFRC ECLDGFQFAS DGQTCVEVHR PVDPCRSGTH DCDVPERARC SYTGGSSYIC
     TCAPGFMGDG RRCQDIDECQ VNQCHENAVC FNTPGSFSCQ CNPGFHGDGF YCSTEREKTR
     CELHKESVVG FGPHSARPQP GRFVPTCDAQ GRYEPMQCHA SIGQCWCVDR DGEEISGTRT
     GPGRFPVCRG HDESGPIRPT PNPNISPLPP GSHILFTQSG KIEYIPLDGH NLKKNEAKTA
     LHLPEKVVIG IAYDCVEKMI YWTDISTPAI SRANLQGGEP VQLIKSDIGS PEGIAIDHLG
     RNMFWTDSMK DRIEVSSLDG TQRRVLVNTD LVNPRAILTD STNGYIYWAD WNRESPKIEM
     AYMDGTNRRV LAKDDLSLPN GLTYDPQTSL LCWADAGTHK VECMNPQQGR RTQLMEEIQY
     PFGLTTDGKN FYYTDWTRVS VVVVDRHLRR EVDEFQPQKR TRLYGITTAH ARCPAGQNYC
     SSNNGGCTHL CLATPAGRSC RCPDNAAELG CVERE
//
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