ZFAN1_MOUSE
ID ZFAN1_MOUSE Reviewed; 268 AA.
AC Q8BFR6; Q8R3Y6; Q9D7H5;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=AN1-type zinc finger protein 1 {ECO:0000305};
DE AltName: Full=Zinc finger AN1-type-containing protein 1 {ECO:0000305};
GN Name=Zfand1 {ECO:0000312|MGI:MGI:1913611};
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].
RC STRAIN=C57BL/6J; TISSUE=Forelimb, Pituitary, and Tongue;
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].
RC TISSUE=Mammary gland, Molar, and Olfactory epithelium;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP STRUCTURE BY NMR OF 1-116 IN COMPLEX WITH ZINC IONS.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first and second ZF-AN1 domains of mouse RIKEN
RT cDNA 2310008M20 protein.";
RL Submitted (AUG-2005) to the PDB data bank.
CC -!- FUNCTION: Plays a role in the regulation of cytoplasmic stress granules
CC (SGs) turnover. SGs are dynamic and transient cytoplasmic
CC ribonucleoprotein assemblies important for cellular protein homeostasis
CC when protein production is suspended after acute exogenous stress.
CC Associates with SGs and is involved in the efficient and specific
CC arsenite-induced clearance process of SGs through the recruitment of
CC the ubiquitin-selective ATPase VCP and the 26S proteasome. This process
CC requires both complexes for efficient degradation of damaged
CC ubiquitinated SG proteins during recovery from arsenite stress, and
CC hence avoiding aberrant cytoplasmic SGs degradation via autophagy.
CC {ECO:0000250|UniProtKB:Q8TCF1}.
CC -!- SUBUNIT: Associates with the 26S proteasome; this association occurs
CC upon exposure to arsenite and is reduced in the presence of ATP.
CC Interacts (via AN1-type 1 and 2 zinc fingers) with PSMD1; this
CC interaction is increased upon arsenite treatment and occurs in an ATP-
CC independent manner. Interacts with PSMC4. Interacts with PSMA1.
CC Interacts (via its ubiquitin-like region) with VCP; this interaction
CC occurs in an arsenite-dependent manner and is necessary for the
CC recruitment of the ubiquitin-selective ATPase VCP to stress granules
CC (SGs). {ECO:0000250|UniProtKB:Q8TCF1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, Stress granule
CC {ECO:0000250|UniProtKB:Q8TCF1}. Note=Colocalizes with TIA1, G3BP1, VCP
CC and 26S proteasome in cytoplasmic stress granules (SGs) in response to
CC arsenite-induced stress treatment in a VCP-independent manner. Not
CC localized in SGs in response to other heat- oxidative- or osmotic-
CC induced stress treatments. Colocalizes with VCP in cytoplasmic
CC speckles. {ECO:0000250|UniProtKB:Q8TCF1}.
CC -!- DOMAIN: The ubiquitin-like region is necessary for its localization to
CC stress granules (SGs) in a VCP-independent manner. The AN1-type 1 and 2
CC zinc finger domains are necessary for the recruitment of the 26S
CC proteasome to SGs. Both the AN1-type 1 and 2 zinc finger domains and
CC the ubiquitin-like region are necessary for efficient SGs clearance
CC upon specific arsenite-induced responses.
CC {ECO:0000250|UniProtKB:Q8TCF1}.
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DR EMBL; AK009240; BAB26161.1; -; mRNA.
DR EMBL; AK030472; BAC26977.1; -; mRNA.
DR EMBL; AK077873; BAC37044.1; -; mRNA.
DR EMBL; BC023352; AAH23352.1; -; mRNA.
DR EMBL; BC046585; AAH46585.1; -; mRNA.
DR EMBL; BC089494; AAH89494.1; -; mRNA.
DR CCDS; CCDS17242.1; -.
DR RefSeq; NP_001317942.1; NM_001331013.1.
DR RefSeq; NP_001317943.1; NM_001331014.1.
DR RefSeq; NP_001317944.1; NM_001331015.1.
DR RefSeq; NP_079788.2; NM_025512.3.
DR PDB; 1WFE; NMR; -; A=44-116.
DR PDB; 1WYS; NMR; -; A=1-62.
DR PDBsum; 1WFE; -.
DR PDBsum; 1WYS; -.
DR AlphaFoldDB; Q8BFR6; -.
DR SMR; Q8BFR6; -.
DR STRING; 10090.ENSMUSP00000037459; -.
DR iPTMnet; Q8BFR6; -.
DR PhosphoSitePlus; Q8BFR6; -.
DR EPD; Q8BFR6; -.
DR MaxQB; Q8BFR6; -.
DR PaxDb; Q8BFR6; -.
DR PRIDE; Q8BFR6; -.
DR ProteomicsDB; 275061; -.
DR Antibodypedia; 12557; 25 antibodies from 11 providers.
DR Ensembl; ENSMUST00000037839; ENSMUSP00000037459; ENSMUSG00000039795.
DR GeneID; 66361; -.
DR KEGG; mmu:66361; -.
DR UCSC; uc008ops.1; mouse.
DR CTD; 79752; -.
DR MGI; MGI:1913611; Zfand1.
DR VEuPathDB; HostDB:ENSMUSG00000039795; -.
DR eggNOG; KOG3183; Eukaryota.
DR GeneTree; ENSGT00730000111180; -.
DR HOGENOM; CLU_052358_0_0_1; -.
DR InParanoid; Q8BFR6; -.
DR OMA; EAIGAHC; -.
DR OrthoDB; 1422113at2759; -.
DR PhylomeDB; Q8BFR6; -.
DR TreeFam; TF314219; -.
DR BioGRID-ORCS; 66361; 3 hits in 72 CRISPR screens.
DR EvolutionaryTrace; Q8BFR6; -.
DR PRO; PR:Q8BFR6; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8BFR6; protein.
DR Bgee; ENSMUSG00000039795; Expressed in embryonic brain and 65 other tissues.
DR ExpressionAtlas; Q8BFR6; baseline and differential.
DR Genevisible; Q8BFR6; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1903843; P:cellular response to arsenite ion; ISS:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0035617; P:stress granule disassembly; ISS:UniProtKB.
DR Gene3D; 4.10.1110.10; -; 2.
DR InterPro; IPR035896; AN1-like_Znf.
DR InterPro; IPR000058; Znf_AN1.
DR Pfam; PF01428; zf-AN1; 2.
DR SMART; SM00154; ZnF_AN1; 2.
DR SUPFAM; SSF118310; SSF118310; 2.
DR PROSITE; PS51039; ZF_AN1; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..268
FT /note="AN1-type zinc finger protein 1"
FT /id="PRO_0000066581"
FT ZN_FING 4..52
FT /note="AN1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT ZN_FING 58..106
FT /note="AN1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT REGION 160..260
FT /note="ubiquitin-like"
FT /evidence="ECO:0000250|UniProtKB:Q8TCF1"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:1WFE,
FT ECO:0007744|PDB:1WYS"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:1WFE,
FT ECO:0007744|PDB:1WYS"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:1WFE,
FT ECO:0007744|PDB:1WYS"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:1WFE,
FT ECO:0007744|PDB:1WYS"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:1WFE,
FT ECO:0007744|PDB:1WYS"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:1WFE,
FT ECO:0007744|PDB:1WYS"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:1WFE,
FT ECO:0007744|PDB:1WYS"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449,
FT ECO:0000269|Ref.4, ECO:0007744|PDB:1WFE,
FT ECO:0007744|PDB:1WYS"
FT CONFLICT 102
FT /note="E -> V (in Ref. 1; BAB26161)"
FT /evidence="ECO:0000305"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:1WYS"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1WYS"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1WYS"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1WFE"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:1WFE"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1WFE"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1WFE"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:1WFE"
SQ SEQUENCE 268 AA; 30203 MW; F852DD01553EBAC0 CRC64;
MAELDIGQHC QVQHCRQRDF LPFVCDGCSG IFCLEHRSKD SHGCSEVNVV KERPKTDEHK
SYSCSFKGCT DVELVAVICP YCEKNFCLRH RHQSDHDCEK LEVAKPRMAA TQKLVRDIVD
AKTGGAASKG RKGAKSSGTA AKVALMKLKM HADGDKSLPQ TERTYFQVYL PKGSKEKSKA
MFFCLRWSIG KVVDFAASLA NLRNENNKLT AKKLRLCHVP SGEALPLDHT LERWITKEEC
PLYNGGNVIL EYLNDEEQFL KNVDSYLE
