TXB1A_DANRE
ID TXB1A_DANRE Reviewed; 781 AA.
AC Q1LWB0;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Tax1-binding protein 1 homolog A {ECO:0000303|PubMed:18638469};
GN Name=tax1bp1a {ECO:0000303|PubMed:18638469,
GN ECO:0000312|ZFIN:ZDB-GENE-060503-587};
GN Synonyms=si:ch211-204j16.2 {ECO:0000312|ZFIN:ZDB-GENE-060503-587};
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;
RN [1]
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:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=18638469; DOI=10.1016/j.ydbio.2008.06.032;
RA Ahn D., Ho R.K.;
RT "Tri-phasic expression of posterior Hox genes during development of
RT pectoral fins in zebrafish: implications for the evolution of vertebrate
RT paired appendages.";
RL Dev. Biol. 322:220-233(2008).
CC -!- FUNCTION: May have anti-apoptotic activity. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Little expression is observed during pectoral fin
CC development, except for an elevated level of expression in the distal
CC mesenchyme cells of some samples. {ECO:0000269|PubMed:18638469}.
CC -!- DOMAIN: The C-terminal UBZ-type zinc fingers function as ubiquitin-
CC binding domains. {ECO:0000250|UniProtKB:Q86VP1}.
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DR EMBL; BX601646; CAK04430.2; -; Genomic_DNA.
DR AlphaFoldDB; Q1LWB0; -.
DR SMR; Q1LWB0; -.
DR STRING; 7955.ENSDARP00000095151; -.
DR PaxDb; Q1LWB0; -.
DR ZFIN; ZDB-GENE-060503-587; tax1bp1a.
DR eggNOG; ENOG502QQ1D; Eukaryota.
DR HOGENOM; CLU_021315_1_0_1; -.
DR InParanoid; Q1LWB0; -.
DR PhylomeDB; Q1LWB0; -.
DR Reactome; R-DRE-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-DRE-936440; Negative regulators of DDX58/IFIH1 signaling.
DR PRO; PR:Q1LWB0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR InterPro; IPR012852; CALCOCO1-like.
DR InterPro; IPR041641; CALCOCO1/2_Zn_UBZ1.
DR InterPro; IPR041611; SKICH.
DR Pfam; PF07888; CALCOCO1; 1.
DR Pfam; PF17751; SKICH; 1.
DR Pfam; PF18112; Zn-C2H2_12; 2.
DR PROSITE; PS51905; ZF_UBZ1; 2.
PE 2: Evidence at transcript level;
KW Apoptosis; Coiled coil; Metal-binding; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..781
FT /note="Tax1-binding protein 1 homolog A"
FT /id="PRO_0000379495"
FT ZN_FING 716..742
FT /note="UBZ1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT ZN_FING 743..769
FT /note="UBZ1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT REGION 441..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 148..453
FT /evidence="ECO:0000255"
FT COILED 488..581
FT /evidence="ECO:0000255"
FT COMPBIAS 441..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..510
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 719
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 722
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 738
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 742
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 746
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 749
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 765
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 769
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
SQ SEQUENCE 781 AA; 89584 MW; 952CEA309344C338 CRC64;
MSSSCNVGAS AGGGGSVVME TSNFAHVIFQ NVGKSFLPQA ALECHYTLTP FITPHPKDWV
GIFKVGWSSA RDYYTFLWSP MPENYTEGST VHRTIIFQGY YVPRSDGEFY QFCYVTHTGE
IRGASTPFQF RPATPTGEEL LTVEDDGNSD ILVRVEEVQQ ECKELQKALR LLTQERDQLQ
EKQRQQNQEL QKSLIEEKEE AQSRVRQLEQ DLLKITQKAV LKETELDCLR DKLQKVISER
DSLQTQLKNE RDERELYKSH VRSAELENTK LSAELQMLKA VELNREVTIA QYQEELHRLR
TERDTHPAET GLKEQLRQAE EQLQATRQQA AMLGSELRDA SGGRDRTMTE LYRVRQEAEE
LRAHLAEAQE ECRHAQDQLD RMKNQTSQEM GRAGGGVGVA SELEAELQKE VEELKLRLNM
AAEHYKEKYR ECQRLRRQVT KLTQQQETQQ GDANRNDAST ETTLELHTPD AETPSESYPA
EIKTVARDVE KSRDEEGNEQ EEEDEEEEEC SLSVEAELAC MEEKWREQCT INENLKLLLA
NEEKRFKTQV AEKDREVSAL RESLVVVTKE KERLEKQYMR EGTTRSRRLE VREPVVLRYP
LPYPQDPPPL PLVPQQPAEL QFGNPYLEQE TRDGADGALS PEQTCRPPPL APPPWGGPVV
CSQPSRSLSP PDGLENPTEE RPTGGDGEAP AVCEHQSLES NESHTSFCFD TRPDVHKQCP
LCEVIFPPHF EQSSFERHVE SHWRVCPVCS EQFPLDCQQQ LYEKHVHTHF DGNVLNFDNF
D
