EST1A_PONAB
ID EST1A_PONAB Reviewed; 1419 AA.
AC Q5RAK6;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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:0000250|UniProtKB:Q86US8};
DE AltName: Full=Smg-6 homolog {ECO:0000250|UniProtKB:Q86US8};
GN Name=SMG6 {ECO:0000250|UniProtKB:Q86US8};
GN Synonyms=EST1A {ECO:0000250|UniProtKB:Q86US8},
GN KIAA0732 {ECO:0000250|UniProtKB:Q86US8};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the telomerase ribonucleoprotein (RNP) complex
CC that is essential for the replication of chromosome termini. May have a
CC general role in telomere regulation. Promotes in vitro the ability of
CC TERT to elongate telomeres. Overexpression induces telomere uncapping,
CC chromosomal end-to-end fusions (telomeric DNA persists at the fusion
CC points) and did not perturb TRF2 telomeric localization. Binds to the
CC single-stranded 5'-(GTGTGG)(4)GTGT-3' telomeric DNA, but not to a
CC telomerase RNA template component (TER).
CC {ECO:0000250|UniProtKB:Q86US8}.
CC -!- FUNCTION: Plays a role in nonsense-mediated mRNA decay. Is thought to
CC provide a link to the mRNA degradation machinery as it has endonuclease
CC activity required to initiate NMD, and to serve as an adapter for UPF1
CC to protein phosphatase 2A (PP2A), thereby triggering UPF1
CC dephosphorylation. Degrades single-stranded RNA (ssRNA), but not ssDNA
CC or dsRNA. {ECO:0000250|UniProtKB:Q86US8}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC -!- SUBUNIT: May form homooligomers. Associated component of the telomerase
CC holoenzyme complex. Interacts with TERT, independently of the
CC telomerase RNA. Interacts with SMG1, SMG5, SMG7, UPF1, UPF2, UPF3B and
CC the PP2A catalytic subunits. Also interacts with the exon junction
CC complex (EJC) composed at least of CASC3, EIF4A3, MAGOH and RBM8A;
CC required for the process of nonsense-mediated mRNA decay. Interacts
CC with DHX34; the interaction is RNA-independent (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}. Note=Particularly enriched in the
CC nucleolus. {ECO:0000250|UniProtKB:Q86US8}.
CC -!- DOMAIN: The PINc domain confers endonuclease activity and is expected
CC to bind the catalytic metal ion. {ECO:0000250|UniProtKB:Q86US8}.
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DR EMBL; CR859009; CAH91204.1; -; mRNA.
DR RefSeq; NP_001125708.1; NM_001132236.2.
DR AlphaFoldDB; Q5RAK6; -.
DR SMR; Q5RAK6; -.
DR STRING; 9601.ENSPPYP00000008776; -.
DR GeneID; 100172632; -.
DR KEGG; pon:100172632; -.
DR CTD; 23293; -.
DR eggNOG; KOG2162; Eukaryota.
DR InParanoid; Q5RAK6; -.
DR OrthoDB; 556396at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:endoribonuclease activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
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; Coiled coil; Cytoplasm; DNA-binding; Endonuclease; Hydrolase;
KW Manganese; Metal-binding; Methylation; Nonsense-mediated mRNA decay;
KW Nuclease; Nucleus; Phosphoprotein; Reference proteome; Telomere.
FT CHAIN 1..1419
FT /note="Telomerase-binding protein EST1A"
FT /id="PRO_0000233088"
FT DOMAIN 1246..1397
FT /note="PINc"
FT REGION 26..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..59
FT /note="EJC-binding motif 1; mediates interaction with the
FT EJC"
FT /evidence="ECO:0000250"
FT REGION 99..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..153
FT /note="EJC-binding motif 2; mediates interaction with the
FT EJC"
FT /evidence="ECO:0000250"
FT REGION 179..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 166..190
FT /evidence="ECO:0000255"
FT COILED 575..600
FT /evidence="ECO:0000255"
FT COMPBIAS 30..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 1353
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 1392
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86US8"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61406"
FT MOD_RES 406
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P61406"
FT MOD_RES 433
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P61406"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P61406"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86US8"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86US8"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86US8"
FT MOD_RES 870
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86US8"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86US8"
SQ SEQUENCE 1419 AA; 160801 MW; E002F6EA2CC967D0 CRC64;
MAEGLERVRI SASELRGILA TLAPQAGSRE NMKELKEARP RKDNRRPDLE IYKPGLSRLR
NKPKIKEPSG SEEFKDEIVN DRDCSAVENG TQPFKDVCKE LNNQQQNGPI DPENNRGQES
FPRTAGQEDR SLKMIKRTKK PDLQIYQPGR RLQTVSKESA SRVEEEEILN QVEQLRVEED
ECRGNVVKEE VVNKPDRAEI EKSPGGDRVR AAKGEKGKRI EKGEGMRKTN DDPAQGKPGS
AKRYSRSDKR RNRYRTCSTS SAGSNNSAEG AGLTDNGCRR RRQDRTKERP RLKKQVSVSS
TDSLDEDRID EPDGLEPRRS SERKKHLERN WSGRGEGEQK SNGKENRGTL RVTFDAEAMN
KESPMVRSAR DDMDRGKPDK GLSSGGKGSE KQESKNPKQE LRGRGRGILI LPAHTTLSVN
SAGSPESAPL GPRLLFGSGS KGPRSWGRGG TTRRLWDPNN PDQKPALKTQ TPQLHFLDTD
DEVSPTSWGD SRQAQASYYK FQNSDNPYYY PRTPGPASQY PYTGYNPLQY PVGPTNGVYP
GPYYPGYPTP SGPYVCSPLP ASTMSPEEVE QHMRNLQQQE LHRLLRVADN QELQLSNLLS
RDRISPEGLE KMAQLRAELL QLYERCILLD IEFSDNQNVD QILWKNAFYQ VIEKFRQLVK
DPNVENPEQI RNRLLELLDE GSDFFDSLLQ KLQVTYKFKL EDYIDGLAIR SKPLRKTVKY
ALISAQRCMI CQGDIARYRE QARDTANYGK ARSWYLKAQH IAPKNGRPYN QLALLAVYTR
RKLDAVYYYM RSLAASNPIL TAKESLMSLF EETKRKAEQM EKKQHEEFEL SPDQWRKGKK
STFRHVGDDT TRLEIWIHPS HPRSSQGTES GKDSEQENGL GSLSPSDLNK RFILSFLHAH
GKLFTRIGME TFPAVAEKVL KEFQVLLQHS PSPIGSTRML QLMTINMFAV HNSQLKDCFS
EECRSVIQEQ AAALGLAMFS LLVCRCTYLL KESAKAQLSS PEDQDDQDDI KVSSFVPDLK
ELLPSVKVWS DWMLGYPDTW NPPPTSLDLP SHVAVDVWST LADFCNILTA VNQSEVPLYK
DPDDDLTLLI LEEDRLLSGF VPLLAAPQDP CYVEKTSDKV IAADCKRVTV LKYFLEALCG
QEEPLLAFKD GKYVSVAPAP DTMGKEMVSQ EGTRLEDEEE DVVIEDFEED SEAEGSGGED
DIRELRAKKL ALARKIAEQQ RRQEKIQAVL EDHSQMRQME LEIRPLFLVP DTNGFIDHLA
SLARLLESRK YILVVPLIVI NELDGLAKGQ ETDHRAGGYA RVVQEKARKS IEFLEQRFES
RDSCLRALTS RGNELESIAF RSEDITGQLG NNDDLILSCC LHYCKDKAKD FMPTSKEEPI
RLLREVVLLT DDRNLRVKAL TRNVPVRDIP AFLTWAQVG
