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KERA_DANRE
ID   KERA_DANRE              Reviewed;         348 AA.
AC   Q5RI43; Q0PZF1;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Keratocan {ECO:0000303|PubMed:17965408};
DE   Flags: Precursor;
GN   Name=kera {ECO:0000303|PubMed:17965408};
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:0000312|Proteomes:UP000000437};
RN   [1] {ECO:0000312|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
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., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., 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   [2] {ECO:0000312|EMBL:AAI15059.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000312|EMBL:ABG72686.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-348, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, GLYCOSYLATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17965408; DOI=10.1074/jbc.m707656200;
RA   Yeh L.K., Liu C.Y., Chien C.L., Converse R.L., Kao W.W., Chen M.S.,
RA   Hu F.R., Hsieh F.J., Wang I.J.;
RT   "Molecular analysis and characterization of zebrafish keratocan (zKera)
RT   gene.";
RL   J. Biol. Chem. 283:506-517(2008).
CC   -!- FUNCTION: May be important in developing and maintaining corneal
CC       transparency and for the structure of the stromal matrix.
CC       {ECO:0000250|UniProtKB:O60938}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000305|PubMed:17965408}.
CC   -!- TISSUE SPECIFICITY: Expressed in eye, where it is found in the corneal
CC       epithelial layer and to a lesser extent in the stromal layer (at
CC       protein level). {ECO:0000269|PubMed:17965408}.
CC   -!- DEVELOPMENTAL STAGE: At 2-3 days post-fertilization, detected in eye,
CC       forebrain, midbrain, hindbrain and anterior spinal cord.
CC       {ECO:0000269|PubMed:17965408}.
CC   -!- PTM: Glycosylated. Contains keratan sulfate chains.
CC       {ECO:0000269|PubMed:17965408}.
CC   -!- DISRUPTION PHENOTYPE: Morpolino knockdown of the protein results in
CC       increased apoptosis in eye, forebrain and midbrain, and reduced
CC       survival rate in embryos. {ECO:0000269|PubMed:17965408}.
CC   -!- SIMILARITY: Belongs to the small leucine-rich proteoglycan (SLRP)
CC       family. SLRP class II subfamily. {ECO:0000305}.
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DR   EMBL; BX322608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC115058; AAI15059.1; -; mRNA.
DR   EMBL; DQ667686; ABG72686.1; -; Genomic_DNA.
DR   RefSeq; NP_001020719.1; NM_001025548.2.
DR   RefSeq; XP_005164822.1; XM_005164765.2.
DR   AlphaFoldDB; Q5RI43; -.
DR   SMR; Q5RI43; -.
DR   STRING; 7955.ENSDARP00000073976; -.
DR   PaxDb; Q5RI43; -.
DR   Ensembl; ENSDART00000079521; ENSDARP00000073976; ENSDARG00000056938.
DR   GeneID; 567017; -.
DR   KEGG; dre:567017; -.
DR   CTD; 11081; -.
DR   ZFIN; ZDB-GENE-041210-165; kera.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000158968; -.
DR   HOGENOM; CLU_000288_186_4_1; -.
DR   InParanoid; Q5RI43; -.
DR   OMA; MECFCPP; -.
DR   OrthoDB; 826997at2759; -.
DR   PhylomeDB; Q5RI43; -.
DR   TreeFam; TF334562; -.
DR   Reactome; R-DRE-2022854; Keratan sulfate biosynthesis.
DR   Reactome; R-DRE-2022857; Keratan sulfate degradation.
DR   PRO; PR:Q5RI43; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 4.
DR   Bgee; ENSDARG00000056938; Expressed in head and 19 other tissues.
DR   ExpressionAtlas; Q5RI43; baseline and differential.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; -; 2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR000372; LRRNT.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF01462; LRRNT; 1.
DR   SMART; SM00369; LRR_TYP; 5.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS51450; LRR; 8.
PE   1: Evidence at protein level;
KW   Disulfide bond; Extracellular matrix; Glycoprotein; Leucine-rich repeat;
KW   Reference proteome; Repeat; Secreted; Sensory transduction; Signal; Vision.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..348
FT                   /note="Keratocan"
FT                   /id="PRO_5010844546"
FT   DOMAIN          40..69
FT                   /note="LRRNT"
FT                   /evidence="ECO:0000255"
FT   REPEAT          70..92
FT                   /note="LRR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          93..118
FT                   /note="LRR 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          119..140
FT                   /note="LRR 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          141..163
FT                   /note="LRR 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          165..189
FT                   /note="LRR 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          190..213
FT                   /note="LRR 6"
FT                   /evidence="ECO:0000255"
FT   REPEAT          215..234
FT                   /note="LRR 7"
FT                   /evidence="ECO:0000255"
FT   REPEAT          235..260
FT                   /note="LRR 8"
FT                   /evidence="ECO:0000255"
FT   REPEAT          262..280
FT                   /note="LRR 9"
FT                   /evidence="ECO:0000255"
FT   REPEAT          281..303
FT                   /note="LRR 10"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:O42235"
FT   CARBOHYD        259
FT                   /note="N-linked (GlcNAc...) (keratan sulfate) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:O42235"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        41..47
FT                   /evidence="ECO:0000250|UniProtKB:P21793"
FT   DISULFID        45..57
FT                   /evidence="ECO:0000250|UniProtKB:P21793"
FT   DISULFID        302..339
FT                   /evidence="ECO:0000250|UniProtKB:P21793"
SQ   SEQUENCE   348 AA;  38938 MW;  2872AB178511645F CRC64;
     MSRLNLTMEV LLVAFVAVFL TSQVHSDEIP YEHLMSQLQA CPKECNCPPN FPNAVYCDNK
     GLKSIPVIPP YTWYLYLQNN LIDVLSANAL RNATQLKWIN LNRNKITTEG LEVDALRAMS
     NLVHLYMEDN LLSSIPSPLP AKLEQLRLSR NKISKIPPGV FSGMGHLTLL DLQSNKLQDD
     AVTEVSLKGL NNLIQINLAK NQLNSMPLGL PPTTTQIFLD GNNIEKIPAE YFKGLPKVAS
     LRLNRNKLAN GGIPKNVFNL SSILDLQLSH NQLTEVPVIS SGLEHLHLDH NKIKSVNSSD
     ICPPGVLDDH LEEKSPRLRY LRLDGNEIQP PIPRELMTCF RLLRAVVI
 
 
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