ID ANKZ1_BOVIN Reviewed; 728 AA.
AC Q58CQ5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 24-JAN-2024, entry version 104.
DE RecName: Full=tRNA endonuclease ANKZF1 {ECO:0000305};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q9H8Y5};
DE AltName: Full=Ankyrin repeat and zinc finger domain-containing protein 1 {ECO:0000305};
GN Name=ANKZF1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Endonuclease that cleaves polypeptidyl-tRNAs downstream of
CC the ribosome-associated quality control (RQC) pathway to release
CC incompletely synthesized polypeptides for degradation. The RQC pathway
CC disassembles aberrantly stalled translation complexes to recycle or
CC degrade the constituent parts. ANKZF1 acts downstream disassembly of
CC stalled ribosomes and specifically cleaves off the terminal 3'-CCA
CC nucleotides universal to all tRNAs from polypeptidyl-tRNAs, releasing
CC (1) ubiquitinated polypeptides from 60S ribosomal subunit for
CC degradation and (2) cleaved tRNAs. ANKZF1-cleaved tRNAs are then
CC repaired and recycled by ELAC1 and TRNT1. Also plays a role in the
CC cellular response to hydrogen peroxide and in the maintenance of
CC mitochondrial integrity under conditions of cellular stress.
CC {ECO:0000250|UniProtKB:Q9H8Y5}.
CC -!- SUBUNIT: Interacts (via VIM motif) with VCP.
CC {ECO:0000250|UniProtKB:Q9H8Y5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H8Y5}.
CC Note=Translocates to the mitochondria upon exposure to hydrogen
CC peroxide. {ECO:0000250|UniProtKB:Q9H8Y5}.
CC -!- DOMAIN: The VLRF1 domain mediates binding to the 60S ribosomal subunit.
CC {ECO:0000250|UniProtKB:Q04311}.
CC -!- SIMILARITY: Belongs to the ANKZF1/VMS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX46739.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BT021892; AAX46739.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001019668.2; NM_001024497.3.
DR RefSeq; XP_005202877.1; XM_005202820.2.
DR AlphaFoldDB; Q58CQ5; -.
DR SMR; Q58CQ5; -.
DR STRING; 9913.ENSBTAP00000037989; -.
DR PaxDb; 9913-ENSBTAP00000037989; -.
DR Ensembl; ENSBTAT00000038173.4; ENSBTAP00000037989.3; ENSBTAG00000020610.6.
DR GeneID; 507867; -.
DR KEGG; bta:507867; -.
DR CTD; 55139; -.
DR VEuPathDB; HostDB:ENSBTAG00000020610; -.
DR VGNC; VGNC:25949; ANKZF1.
DR eggNOG; KOG2505; Eukaryota.
DR GeneTree; ENSGT00390000005911; -.
DR HOGENOM; CLU_014293_0_0_1; -.
DR InParanoid; Q58CQ5; -.
DR OMA; GPHIFMC; -.
DR OrthoDB; 8371at2759; -.
DR TreeFam; TF313431; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000020610; Expressed in retina and 106 other cell types or tissues.
DR ExpressionAtlas; Q58CQ5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0140101; F:catalytic activity, acting on a tRNA; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:RNA endonuclease activity; ISS:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISS:UniProtKB.
DR GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR047139; ANKZ1/VMS1.
DR InterPro; IPR041540; VATC.
DR InterPro; IPR041175; VLRF1/Vms1.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR16036; ANKYRIN REPEAT AND ZINC FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR16036:SF2; ANKYRIN REPEAT AND ZINC FINGER DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF18826; bVLRF1; 1.
DR Pfam; PF18716; VATC; 1.
DR SMART; SM00248; ANK; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Coiled coil; Cytoplasm; Endonuclease; Hydrolase; Metal-binding;
KW Nuclease; Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..728
FT /note="tRNA endonuclease ANKZF1"
FT /id="PRO_0000247277"
FT DOMAIN 216..358
FT /note="VLRF1"
FT /evidence="ECO:0000255"
FT REPEAT 493..526
FT /note="ANK 1"
FT REPEAT 534..563
FT /note="ANK 2"
FT ZN_FING 72..96
FT /note="C2H2-type"
FT REGION 120..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..666
FT /note="VCP/p97-interacting motif (VIM)"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y5"
FT COILED 608..659
FT /evidence="ECO:0000255"
FT COMPBIAS 359..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 254
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y5"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y5"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y5"
FT MOD_RES 607
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y5"
SQ SEQUENCE 728 AA; 81185 MW; F165D3E8221F7598 CRC64;
MSPAPAATQA PVSVSLFDLS TDAPVLQGLR LVSHFPEEAL AQSLQTSCPG SEEQISPERR
PFQGALDISE KLFCSTCDQV FQNHQEQREH YKLDWHRFNL KQRLKDKPLL SALDFEKQSS
TGDLSSISGS EDSDSDSEED LQILDEERAD LEKPTRPQGF HPHRVLFQNA QGQFLYAYRC
VLGPRHASAS TYCVVPLEES ELLLQNLQTG GPRDCVVLMA AAGHFAGAIF QGREVLTHKT
FHRYTVRAKR GTAQGLRDAR GAAAHSAGAS LRRYNEAALY KEVRDLLAGP AWAKALEEAG
TILLRAPRSG RSLFFGGREA PLRRGDPRLW DIPLATRRPT FQELQRVVHK LTTLHIHGED
PRETSRLDLP QTHRKRVRER KVIEEESKVP SDENEALGQN KEAPTQGSES EGGDGSQVEL
ELVEVTLGTL DLREFDVFPK QRRRKRNKRE RKQDLESGAQ MTLSQQPKED EALSGSAPLR
PPLDEATSPC QSELWDVLLA ACRAGDVGML KDRLTASPLH PGVLPLLSAP LGSGGFTLLH
AAAAAGRGSV VRLLLEAGAD PTVQDSRARP PYTVAADRST RNEFRRFMEK NPDAYDYSKA
QVPGPLTAEM EARQATRRRE QKAARRHREE QQRKQQEQEK QEQEEQQRFA ALSDREKRAL
AAERRLAAQL GALNPQTPDP AITVSNIPRC WSCGMSLQGL VPFHYLDFSF CSTRCLRDHR
CQAGKPSS
//
