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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7

DescriptionSubName: Full=Keratin 93 {ECO:0000313|Ensembl:ENSDARP00000006888}; SubName: Full=Zgc:136902 {ECO:0000313|EMBL:AAI15322.1};
MyHits logo
MyHits synonymsQ1RLR3_DANRE , Q1RLR3 , 460B36F96F7773D6
match map segment
ipat:IF ipfam:Filament ismart:Filament  
Legends: 1, COILED {ECO:0000256|SAM:Coils}; 2, ipat:IF [T].
ID   Q1RLR3_DANRE            Unreviewed;       462 AA.
AC   Q1RLR3;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   10-MAY-2017, entry version 88.
DE   SubName: Full=Keratin 93 {ECO:0000313|Ensembl:ENSDARP00000006888};
DE   SubName: Full=Zgc:136902 {ECO:0000313|EMBL:AAI15322.1};
GN   Name=krt93 {ECO:0000313|Ensembl:ENSDARP00000006888,
GN   ECO:0000313|ZFIN:ZDB-GENE-060421-4592};
GN   ORFNames=zgc:136902 {ECO:0000313|EMBL:AAI15322.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI15322.1};
RN   [1] {ECO:0000313|EMBL:AAI15322.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Whole {ECO:0000313|EMBL:AAI15322.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000006888}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000006888};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000006888, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000006888,
RC   ECO:0000313|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   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.,
RA   Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P.,
RA   Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G.,
RA   Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D.,
RA   Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K.,
RA   Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C.,
RA   Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J.,
RA   Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S.,
RA   Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A.,
RA   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.,
RA   Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z.,
RA   Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J.,
RA   Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C.,
RA   Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C.,
RA   Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000256|RuleBase:RU000685, ECO:0000256|SAAS:SAAS00547919}.
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DR   EMBL; BX324177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC115321; AAI15322.1; -; mRNA.
DR   RefSeq; NP_001035449.1; NM_001040359.1.
DR   UniGene; Dr.76263; -.
DR   STRING; 7955.ENSDARP00000006888; -.
DR   Ensembl; ENSDART00000005485; ENSDARP00000006888; ENSDARG00000044976.
DR   GeneID; 678611; -.
DR   KEGG; dre:678611; -.
DR   CTD; 678611; -.
DR   ZFIN; ZDB-GENE-060421-4592; krt93.
DR   eggNOG; ENOG410IFTF; Eukaryota.
DR   eggNOG; ENOG410Y9IV; LUCA.
DR   GeneTree; ENSGT00760000118808; -.
DR   HOGENOM; HOG000230975; -.
DR   HOVERGEN; HBG013015; -.
DR   KO; K07604; -.
DR   OMA; THNANIL; -.
DR   OrthoDB; EOG091G087I; -.
DR   TreeFam; TF332742; -.
DR   Reactome; R-DRE-446107; Type I hemidesmosome assembly.
DR   Reactome; R-DRE-6805567; Keratinization.
DR   Reactome; R-DRE-6809371; Formation of the cornified envelope.
DR   Proteomes; UP000000437; Chromosome 11.
DR   Bgee; ENSDARG00000044976; -.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR23239; PTHR23239; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   PROSITE; PS00226; IF; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|SAAS:SAAS00031873, ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW   Intermediate filament {ECO:0000256|RuleBase:RU000685,
KW   ECO:0000256|SAAS:SAAS00031864};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT   COILED      104    138       {ECO:0000256|SAM:Coils}.
FT   COILED      203    244       {ECO:0000256|SAM:Coils}.
FT   COILED      309    336       {ECO:0000256|SAM:Coils}.
FT   COILED      348    382       {ECO:0000256|SAM:Coils}.
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CC   The following FT lines are automated annotations from the MyHits database.
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FT   MYHIT       397    405       ipat:IF [T]
FT   MYHIT        99    409       ipfam:Filament [T]
FT   MYHIT        99    410       ismart:Filament [T]
SQ   SEQUENCE   462 AA;  50931 MW;  460B36F96F7773D6 CRC64;
     MSLSVRSTTT KGPKTVTSKS IVTKSRGGST SFPHKAYSVY GGGFGGSTRI SSTRIGGGGG
     YGFAGGHCGG YGGGYGGGYS GPLSICVMPS SGLGDFQLNE KATMQNLNDR LASYLDKVRS
     LEAANATLER QIREYYEKKG PVAQRDYSQY WNTIKDLKDK IKNATTHNAN ILLQIDNSKL
     AADDFRLKFE HEVVMRQCVE SDIANLRRLL DQTNLAKNDL QMQIKGLEEE LVFLKKNHQE
     EMAALRCQLT GTVNVEVDAA PQQDLNKVLE EIRTHYENII QKHRREQEAW FKDKTAPLNK
     EVAHSTETIQ TSRSQITELR NTLQSLEIEL QSQLSMKAAL EHSLAETEAR YSAMLAGFQN
     QINNLEAELA QLRASIEQQG RDYALLLDIK TRLEQEIATY RNLLENQDIR TQIPVSISVS
     GGSQSVSSGG SHSVSSGGSH TISTGGPTIQ IKQTTTTSHR TY
//