ANKZ1_MOUSE
ID ANKZ1_MOUSE Reviewed; 748 AA.
AC Q80UU1; B9EKG0; Q9CZF5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Ankyrin repeat and zinc finger domain-containing protein 1;
GN Name=Ankzf1; Synonyms=D1Ertd161e;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6NCr; TISSUE=Brain, and Hematopoietic stem cell;
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 -!- INTERACTION:
CC Q80UU1; Q01853: Vcp; NbExp=2; IntAct=EBI-9510971, EBI-80597;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80UU1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80UU1-2; Sequence=VSP_019961, VSP_019962;
CC -!- SIMILARITY: Belongs to the ANKZF1/VMS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK157405; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK012672; BAB28398.1; -; mRNA.
DR EMBL; AK156255; BAE33643.1; -; mRNA.
DR EMBL; AK157405; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC051449; AAH51449.1; -; mRNA.
DR EMBL; BC057896; AAH57896.1; -; mRNA.
DR EMBL; BC150879; AAI50880.1; -; mRNA.
DR CCDS; CCDS56632.1; -. [Q80UU1-1]
DR RefSeq; NP_001254549.1; NM_001267620.1.
DR AlphaFoldDB; Q80UU1; -.
DR SMR; Q80UU1; -.
DR IntAct; Q80UU1; 1.
DR STRING; 10090.ENSMUSP00000136163; -.
DR iPTMnet; Q80UU1; -.
DR PhosphoSitePlus; Q80UU1; -.
DR EPD; Q80UU1; -.
DR MaxQB; Q80UU1; -.
DR PaxDb; Q80UU1; -.
DR PRIDE; Q80UU1; -.
DR ProteomicsDB; 296249; -. [Q80UU1-1]
DR ProteomicsDB; 296250; -. [Q80UU1-2]
DR DNASU; 52231; -.
DR GeneID; 52231; -.
DR KEGG; mmu:52231; -.
DR UCSC; uc029qpf.2; mouse. [Q80UU1-1]
DR CTD; 55139; -.
DR MGI; MGI:1098746; Ankzf1.
DR eggNOG; KOG2505; Eukaryota.
DR InParanoid; Q80UU1; -.
DR OrthoDB; 1495271at2759; -.
DR BioGRID-ORCS; 52231; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Ankzf1; mouse.
DR PRO; PR:Q80UU1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80UU1; protein.
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 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 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Coiled coil; Cytoplasm; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..748
FT /note="Ankyrin repeat and zinc finger domain-containing
FT protein 1"
FT /id="PRO_0000247279"
FT REPEAT 515..545
FT /note="ANK 1"
FT REPEAT 556..585
FT /note="ANK 2"
FT ZN_FING 96..120
FT /note="C2H2-type"
FT REGION 135..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..677
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 628..681
FT /evidence="ECO:0000255"
FT COMPBIAS 135..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y5"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y5"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y5"
FT MOD_RES 629
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y5"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8Y5"
FT VAR_SEQ 211..225
FT /note="IPPEKAELLLQNLQN -> ASNSPDCVLTPNF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019961"
FT VAR_SEQ 226..748
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019962"
FT CONFLICT 4
FT /note="P -> S (in Ref. 2; AAH51449)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="P -> S (in Ref. 2; AAH51449)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="S -> T (in Ref. 2; AAH51449)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 748 AA; 82976 MW; 38E877B35B4A7594 CRC64;
MAKPAGDAAV GSRSGELFLP SVSSSATSPA PSAAPAPASV SLLSLNGEAP LIRGLSLVSQ
APGEALAWAP RTSCPGENTS SGGKVSPYSL EISEKLFCSA CDQIFQNHQE QREHYKLDWH
RFNLKQRLKN KPLLSASDFE QQSSTGDLSS ISGSDDTDSS SEEDLLPLDE GRAESEKPNR
PPGFYPHRVL FKNAQGQFLY AYRCVLGPHQ IPPEKAELLL QNLQNGGPRY YVVLMAAAGH
FAGAIFQGRE VVAHKTFHRY TVRAKRGTAQ GLQDAHGRAS RSAGANLRRY NEAMLYKDVR
NLLAGPIWSK ALGEAETVLF RAPRSGRSLF FGGQGAPLQR DDPRLWDIPL TTRRPTFGEL
QRVLHKLTTL QVYDEDPREM VRFHSPETHW KPVREERKKD TEKEKTKVPS DANKPLGQDE
EPLKQGSESQ EEDGSEVELE LVELTLGTLD LREFEVLPKR RRRRKKKERS QEQQCGAHGP
LPQQPQDEPF SQPTQEVETP LDTLVYEAKA PGQPELWDTL LAACRAGEVE VLKLQLATGL
VDPGVKSLLN APLGSGGFTL LHAAAAAGRG LVVRLLLEAG ADPTVQDSRA RPPYTVAADK
STRNEFRRFM EKNLDAYDYN KARVPGPLTQ EMEARQATRK KEQKAARRQR EQQQRKQREQ
EEQEQEEQRR FAALSDREKR ALAAERRLAA QLGAPSPPVP DSAVASAGRC WSCGVSLQGL
IPFHYLDFSF CSTRCLRDHR SQAGRPSS
