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Database: UniProt
Entry: F1QT18_DANRE
LinkDB: F1QT18_DANRE
Original site: F1QT18_DANRE 
ID   F1QT18_DANRE            Unreviewed;       435 AA.
AC   F1QT18; A0A8M1P4L6;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Tubulin--tyrosine ligase-like protein 9 {ECO:0000256|ARBA:ARBA00030445};
GN   Name=ttll9 {ECO:0000313|Ensembl:ENSDARP00000108447,
GN   ECO:0000313|RefSeq:NP_001243693.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-030131-1582};
GN   Synonyms=fb75c08 {ECO:0000313|RefSeq:NP_001243693.1}, si:dkey-211h10.2
GN   {ECO:0000313|RefSeq:NP_001243693.1}, wu:fb75c08
GN   {ECO:0000313|RefSeq:NP_001243693.1};
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:ENSDARP00000108447};
RN   [1] {ECO:0000313|RefSeq:NP_001243693.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21262966; DOI=10.1074/jbc.M110.209817;
RA   Pathak N., Austin C.A., Drummond I.A.;
RT   "Tubulin tyrosine ligase-like genes ttll3 and ttll6 maintain zebrafish
RT   cilia structure and motility.";
RL   J. Biol. Chem. 286:11685-11695(2011).
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000108447}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000108447};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000108447, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000108447};
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   [4] {ECO:0000313|RefSeq:NP_001243693.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26469318;
RA   Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA   Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA   Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA   Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA   Reith W., Hertzano R.;
RT   "RFX transcription factors are essential for hearing in mice.";
RL   Nat. Commun. 6:8549-8549(2015).
RN   [5] {ECO:0000313|RefSeq:NP_001243693.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=27189481;
RA   Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I.,
RA   Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y.,
RA   Bobe J.;
RT   "Gene evolution and gene expression after whole genome duplication in fish:
RT   the PhyloFish database.";
RL   BMC Genomics 17:368-368(2016).
RN   [6] {ECO:0000313|RefSeq:NP_001243693.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC       {ECO:0000256|ARBA:ARBA00006820}.
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DR   EMBL; AL929345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001243693.1; NM_001256764.1.
DR   STRING; 7955.ENSDARP00000108447; -.
DR   PaxDb; 7955-ENSDARP00000127671; -.
DR   Ensembl; ENSDART00000128551; ENSDARP00000108447; ENSDARG00000062806.
DR   Ensembl; ENSDART00000128551.4; ENSDARP00000108447.2; ENSDARG00000062806.8.
DR   GeneID; 556794; -.
DR   KEGG; dre:556794; -.
DR   AGR; ZFIN:ZDB-GENE-030131-1582; -.
DR   CTD; 164395; -.
DR   ZFIN; ZDB-GENE-030131-1582; ttll9.
DR   eggNOG; KOG2157; Eukaryota.
DR   OMA; IWIMKPP; -.
DR   OrthoDB; 7265at2759; -.
DR   PhylomeDB; F1QT18; -.
DR   TreeFam; TF313087; -.
DR   Proteomes; UP000000437; Chromosome 23.
DR   Bgee; ENSDARG00000062806; Expressed in testis and 9 other cell types or tissues.
DR   GO; GO:0005929; C:cilium; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR   GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IBA:GO_Central.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR004344; TTL/TTLL_fam.
DR   PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1.
DR   PANTHER; PTHR12241:SF39; TUBULIN POLYGLUTAMYLASE TTLL9-RELATED; 1.
DR   Pfam; PF03133; TTL; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   435 AA;  51140 MW;  69F0F71F1D6AA819 CRC64;
     MSKNKQTTGH KAAHSSQRKK EVEARSCIRY RCGLTNTIQD VLNHRPGWVE VKDDAEWDFN
     WCDVGWLREN FDHSYMEEHV RICHFRNHYE LTRKNLMVKN LKRYRKTLER EVGRLEAAKC
     DFFPRTFELP SEYHIFVEEF KKSPGNTWIM KPVARSQGKG IFLFRKLKDI IDWRKDGSRS
     EEQKDEAQVE SYVAQRYIEN PYLIAGRKFD LRVYVLVTSY IPLKAWLYRD GFARFSNTRF
     SLSSIDDQYV HLTNVAVQKT APDYDPEKGC KWQMQQLRWY LTAKHGFETV QTLFKEIDNV
     FIRSLLSVQK TIINDKHCFE LYGYDILLDQ DLKPWLIEVN ASPSLTASSQ EDYDLKYRLL
     EDTLHIVDME GRLTGKEKRI GGFDLMWNDG PVYTDVGLEA LGSSCLVANT HLGCVNDREK
     QLQQLLKPFP GQKKT
//
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