ANKZ1_RAT
ID ANKZ1_RAT Reviewed; 722 AA.
AC Q66H85;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ankyrin repeat and zinc finger domain-containing protein 1;
GN Name=Ankzf1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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}.
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DR EMBL; BC081973; AAH81973.1; -; mRNA.
DR RefSeq; NP_001014241.1; NM_001014219.1.
DR AlphaFoldDB; Q66H85; -.
DR SMR; Q66H85; -.
DR STRING; 10116.ENSRNOP00000036500; -.
DR iPTMnet; Q66H85; -.
DR PhosphoSitePlus; Q66H85; -.
DR PaxDb; Q66H85; -.
DR GeneID; 363255; -.
DR KEGG; rno:363255; -.
DR UCSC; RGD:1359242; rat.
DR CTD; 55139; -.
DR RGD; 1359242; Ankzf1.
DR VEuPathDB; HostDB:ENSRNOG00000019052; -.
DR eggNOG; KOG2505; Eukaryota.
DR HOGENOM; CLU_014293_0_0_1; -.
DR InParanoid; Q66H85; -.
DR OMA; GESKWDW; -.
DR OrthoDB; 1495271at2759; -.
DR PhylomeDB; Q66H85; -.
DR PRO; PR:Q66H85; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000019052; Expressed in cerebellum and 19 other tissues.
DR Genevisible; Q66H85; RN.
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; 2.
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..722
FT /note="Ankyrin repeat and zinc finger domain-containing
FT protein 1"
FT /id="PRO_0000247280"
FT REPEAT 489..519
FT /note="ANK 1"
FT REPEAT 530..559
FT /note="ANK 2"
FT ZN_FING 70..94
FT /note="C2H2-type"
FT REGION 109..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..650
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 602..655
FT /evidence="ECO:0000255"
FT COMPBIAS 110..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y5"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y5"
FT MOD_RES 529
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y5"
FT MOD_RES 603
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y5"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y5"
SQ SEQUENCE 722 AA; 80585 MW; A6517030713C2212 CRC64;
MLPAPRAAPV PASVSLLTLN GEAPLVRGLS LVSQAPGEAL AWAPRTSCPG ENTSSGRKVS
PCSLDISDKL FCSACDQVFQ NHQEQREHYK LDWHRFNLKQ RLKNKPLLSA SDFERQSSRG
DLSSISGSED SDSASEEDLL TLDEERAESE KPNRPPGFYP HRVLFRNAQG QFLYAYRCVL
GPHQIPPEKA ELLLQNLQNG GPRHYVVLMA AAGHFAGAIF QGREVVAHKT FHRYTVRAKR
GTAQGLQDAQ GRASRSAGAN LRRYNEAMLY KDVRDLLAGP TWSKALGEAE TILLHAPRSG
RSLFFGGQGA PLQRSDFRLW DIPLTTRRPT FGELQRVLHK LTTLQVYDED PREMVRFHSP
ETHCKPVREE RKRDTEKEKT KVPSDANKAL GQDEEPLKQG SESQEEDGSE VELELVELTL
GTLDLREFEV LPKRRKKRKK KERSQKQQCG AHGPLLQQPQ DEPFSQPTQV VATPLDTLVD
EAKAPGQPEL WDMLLAACRA GEVEVLKLQL ATGPVDPGVM SLLSAPLGSG GFTLLHAAAA
AGRGLVVRLL LEAGADPTVH DSRARPPYTV AADRSTRNEF RRFMEKNLDA YDYSKARVPG
PLTQEMEARQ ATRKKEQKAA RRQREQQQRK QREQEEQEQE ERRRFAALSD REKRALAAER
RLAAQLGAPS PPVPDSAVVN AGRCWSCGVS LQGLIPFHYL DFSFCSTRCL RDHRSQAGRP
SS
