ANKZ1_BOVIN
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 03-AUG-2022, entry version 98.
DE RecName: Full=Ankyrin repeat and zinc finger domain-containing protein 1;
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: Plays a role in the cellular response to hydrogen peroxide
CC and in the maintenance of mitochondrial integrity under conditions of
CC cellular stress (By similarity). Involved in the endoplasmic reticulum
CC (ER)-associated degradation (ERAD) pathway (By similarity).
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 -!- 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; Q58CQ5; -.
DR PRIDE; Q58CQ5; -.
DR Ensembl; ENSBTAT00000038173; ENSBTAP00000037989; ENSBTAG00000020610.
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; GESKWDW; -.
DR OrthoDB; 1495271at2759; -.
DR TreeFam; TF313431; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000020610; Expressed in retina and 106 other tissues.
DR ExpressionAtlas; Q58CQ5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR041540; VATC.
DR InterPro; IPR041175; VLRF1/Vms1.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF18826; bVLRF1; 1.
DR Pfam; PF18716; VATC; 1.
DR SMART; SM00248; ANK; 1.
DR SUPFAM; SSF48403; SSF48403; 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; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..728
FT /note="Ankyrin repeat and zinc finger domain-containing
FT protein 1"
FT /id="PRO_0000247277"
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 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
