EST1A_DANRE
ID EST1A_DANRE Reviewed; 1544 AA.
AC A0A0R4IZ84; C5J7W9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Telomerase-binding protein EST1A {ECO:0000305};
DE EC=3.1.-.-;
DE AltName: Full=Ever shorter telomeres 1A {ECO:0000250|UniProtKB:Q86US8};
DE AltName: Full=Nonsense mediated mRNA decay factor SMG6 {ECO:0000312|ZFIN:ZDB-GENE-081107-52};
DE AltName: Full=Smg-6 homolog {ECO:0000250|UniProtKB:Q86US8};
GN Name=smg6 {ECO:0000312|ZFIN:ZDB-GENE-081107-52};
GN Synonyms=est1a {ECO:0000250|UniProtKB:Q86US8};
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 {ECO:0000312|Proteomes:UP000000437};
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:CAX18775.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 93-519, FUNCTION, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=19414594; DOI=10.1128/mcb.00177-09;
RA Wittkopp N., Huntzinger E., Weiler C., Sauliere J., Schmidt S.,
RA Sonawane M., Izaurralde E.;
RT "Nonsense-mediated mRNA decay effectors are essential for zebrafish
RT embryonic development and survival.";
RL Mol. Cell. Biol. 29:3517-3528(2009).
CC -!- FUNCTION: Component of the telomerase ribonucleoprotein (RNP) complex
CC that is essential for the replication of chromosome termini (By
CC similarity). Required for normal embryonic development
CC (PubMed:19414594). {ECO:0000250|UniProtKB:Q86US8,
CC ECO:0000269|PubMed:19414594}.
CC -!- FUNCTION: Plays a role in nonsense-mediated mRNA decay.
CC {ECO:0000250|UniProtKB:Q86US8}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q86US8};
CC -!- SUBUNIT: May form homooligomers (By similarity). Associated component
CC of the telomerase holoenzyme complex (By similarity).
CC {ECO:0000250|UniProtKB:Q86US8}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q86US8}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q86US8}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q86US8}.
CC -!- DEVELOPMENTAL STAGE: Expressed during early cleavage, gastrulation and
CC at 1 day post-fertilization. {ECO:0000269|PubMed:19414594}.
CC -!- DOMAIN: The PINc domain confers endonuclease activity and is expected
CC to bind the catalytic metal ion. {ECO:0000250|UniProtKB:Q86US8}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown leads to a phenotype ranging
CC in severity from weak to severe that are developmentally delayed with
CC disturbed brain patterning, necrosis in areas of the brain, aberrant
CC eye development, impaired somitogenesis resulting in stacked somites,
CC perturbed yolk sac extension and posterior axis extension with a high
CC mortality rate of 93% at 5 days post-fertilization.
CC {ECO:0000269|PubMed:19414594}.
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DR EMBL; BX663516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR925771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; FM986822; CAX18775.1; -; mRNA.
DR AlphaFoldDB; A0A0R4IZ84; -.
DR SMR; A0A0R4IZ84; -.
DR STRING; 7955.ENSDARP00000116550; -.
DR PaxDb; A0A0R4IZ84; -.
DR Ensembl; ENSDART00000158537; ENSDARP00000140752; ENSDARG00000100481.
DR ZFIN; ZDB-GENE-081107-52; smg6.
DR eggNOG; KOG2162; Eukaryota.
DR GeneTree; ENSGT00940000155300; -.
DR OMA; KDFMPPQ; -.
DR OrthoDB; 556396at2759; -.
DR Reactome; R-DRE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 10.
DR Bgee; ENSDARG00000100481; Expressed in mature ovarian follicle and 21 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005697; C:telomerase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0070034; F:telomerase RNA binding; IBA:GO_Central.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0043009; P:chordate embryonic development; IMP:ZFIN.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IDA:ZFIN.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR018834; DNA/RNA-bd_Est1-type.
DR InterPro; IPR045153; Est1/Ebs1-like.
DR InterPro; IPR019458; Est1_N.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR002716; PIN_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR15696; PTHR15696; 1.
DR Pfam; PF10374; EST1; 1.
DR Pfam; PF10373; EST1_DNA_bind; 1.
DR Pfam; PF13638; PIN_4; 1.
DR SMART; SM00670; PINc; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF88723; SSF88723; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Cytoplasm; Endonuclease; Hydrolase;
KW Nonsense-mediated mRNA decay; Nuclease; Nucleus; Reference proteome;
KW Telomere.
FT CHAIN 1..1544
FT /note="Telomerase-binding protein EST1A"
FT /id="PRO_0000454183"
FT DOMAIN 1369..1522
FT /note="PINc"
FT /evidence="ECO:0000255"
FT REGION 25..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 936..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 976..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..247
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 177
FT /note="G -> E (in Ref. 2; CAX18775)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="P -> L (in Ref. 2; CAX18775)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="H -> N (in Ref. 2; CAX18775)"
FT /evidence="ECO:0000305"
FT CONFLICT 258..265
FT /note="RQDDTNQI -> GQDDSNQS (in Ref. 2; CAX18775)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="P -> A (in Ref. 2; CAX18775)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="K -> R (in Ref. 2; CAX18775)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="A -> S (in Ref. 2; CAX18775)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="I -> M (in Ref. 2; CAX18775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1544 AA; 172241 MW; 60918E6DEC914E84 CRC64;
MADELERVRI SAAELRAQAS SFNIHGDDVK DLREEGKKQR QRDSKRPDLQ LYKPGVGHPN
RRMDSVEGAG SDTLIQPDGF GNDPKMSDES PTSPGCSYMP GTGNEDYLND HSKPETNHKT
DGHIGGDKHK LVDENAVKII ERAGTPKSPK QSRKMRKPDR QIYQPGGRRS QGNKEVGASK
ELDRDRSREE EVDGKSIETP LKCEKEEKRK NRRGKNDRKK QASVETPSAN KTENAVENIS
NKVSNLHLET VESKDRDRQD DTNQIKHSEE GRKIQTGGAN RGMGEDKKKE RGNGKSRPGK
EKGNNQVFDK KEEGEAGGKA SEAPHLEGRK QRNFGAKEAS RDQNLNHEKQ QGNRPKEKGK
PSERTDSKRV NAASKRYSQS DIRRPRNRTY STSSASSGTS MDGLAEAERL KAEGQQFSAR
TLERATGQRE FVRGGQTRSR RRTARTLSST DSLEENEVWE REGRRSRAAE EAKSSTRKEG
GILRVSLDKR EEQASRKSTR GRGRGILVLP AHTDLTQTPD PAPPLGGMRG GMGLGRGRGG
RGGGTRRLWD PNNPDKKPAL VSSQQSQHAS QHQALYLQQG GCGPLHFLDT DDETVGSPPV
RQGEFFQNQQ AAAMAYYKFQ NSDNPYCYPV SANSPNTPPR YPYPYQIPYQ IPGSNGMYPA
SAMTSFYGPY GQGGPGYPSP TVSALTPEEA EVQTRGELGK FLRLADSQEL QLSNLLSRER
LSQEGLERMA QLRAELLTIY ERVILTDIEF SDSQNVDQTL WKNVFYQVIE RFRQLLKDQN
SDTAPQIKTM LMTILEEGAV FFDSLLQKLQ SVFQFKLQDY MDCMAIRARP LRKTVKYALI
SAQRCMICQG DIARYREQAS ESANYGKARS WYLKAQQIAP KNGRPYNQLA LLAVYTKRKL
DAVYYYMRSL AASNPILTAK ESLMSLFEEA KRKADQVERR LKQDSDGSAH GPKGHTGGRR
GEDAARVEIW IRPSEVSGTS RPTGSESGKD SEQDGELGAL SASDLNKRFI LSFLHAHGKL
FTKVGMESFP AVANRVLLEF RALLQHSPSP LGSTRMLQII TINMFTIYNA QIRAKGQGET
RSALEEQAIS LGLAMFGLLV QRCTELLKET PTEPIPAEEL GEFDEMDDEE GMVRVSVFPH
DLRELLPSMK VWSDWMLGHP EKWNPPPCSM QGSPDVWQCL ADLCNSFSRV YHGEVLLYKA
DADGEGDEEL RVLQLEEDKM LSGFVPLLAA PQDACYTDQG TDAAIAADCK RVTVLKYFLE
ALCGQEEPLL AFKGGKYISM AAPLTPSINT ENKAQEQEDD VIVEESSLSA SEGEIDGEME
GDGSEDDIRE LRARRHALAH KLAQQQKRRD KIQAVLQTGG QLEIEVRPFY LVPDTNGFID
HLEGLRKLLA CGTYILVVPL IVITELDGLA KGQDSREGVG NGAHARQVQD RARAAVMFLE
KAFESRDPSI RALTSRGNTL ESIAFRSEDT SGQKGNNDDV ILSCCLHYCQ DKAKDFMPAE
RNGPVRLRRE VVLLTDDRNL RVKALTRNVP VRDIPAFLIW AKVG
