ZFAN6_MOUSE
ID ZFAN6_MOUSE Reviewed; 223 AA.
AC Q9DCH6; Q9ER79;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=AN1-type zinc finger protein 6;
DE AltName: Full=Associated with PRK1 protein;
DE AltName: Full=Zinc finger A20 domain-containing protein 3;
GN Name=Zfand6; Synonyms=Awp1, Za20d3;
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 [MRNA], AND INTERACTION WITH PKN1.
RC TISSUE=Liver, Mammary gland, and Uterus;
RX PubMed=11054541; DOI=10.1016/s0378-1119(00)00365-6;
RA Duan W., Sun B., Li T.W., Tan B.J., Lee M.K., Teo T.S.;
RT "Cloning and characterization of AWP1, a novel protein that associates with
RT serine/threonine kinase PRK1 in vivo.";
RL Gene 256:113-121(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP FUNCTION, UBIQUITIN-BINDING, INTERACTION WITH PEX6 AND PEX5, AND
RP MUTAGENESIS OF CYS-30 AND CYS-180.
RX PubMed=21980954; DOI=10.1111/j.1600-0854.2011.01298.x;
RA Miyata N., Okumoto K., Mukai S., Noguchi M., Fujiki Y.;
RT "AWP1/ZFAND6 functions in Pex5 export by interacting with cys-
RT monoubiquitinated Pex5 and Pex6 AAA ATPase.";
RL Traffic 13:168-183(2012).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-219, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Involved in regulation of TNF-alpha induced NF-kappa-B
CC activation and apoptosis. Involved in modulation of 'Lys-48'-linked
CC polyubiquitination status of TRAF2 and decreases association of TRAF2
CC with RIPK1 (By similarity). Required for PTS1 target sequence-dependent
CC protein import into peroxisomes and PEX5 stability; may cooperate with
CC PEX6. In vitro involved in PEX5 export from the cytosol to peroxisomes.
CC {ECO:0000250, ECO:0000269|PubMed:21980954}.
CC -!- SUBUNIT: Interacts with PKN1. Interacts with TRAF2 (By similarity).
CC Interacts with mono- and polyubiquitin. Interacts with PEX6. Interacts
CC with PEX5 (Cys-linked ubiquitinated). {ECO:0000250,
CC ECO:0000269|PubMed:11054541, ECO:0000269|PubMed:21980954}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The A20-type zinc finger domain mediates regulation of NF-
CC kappa-B activity. {ECO:0000250}.
CC -!- DOMAIN: The AN1-type zinc finger domain mediates association with
CC TRAF2. {ECO:0000250}.
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DR EMBL; AJ251508; CAC14886.1; -; mRNA.
DR EMBL; AK002775; BAB22349.1; -; mRNA.
DR EMBL; AK144902; BAE26124.1; -; mRNA.
DR EMBL; BC010683; AAH10683.1; -; mRNA.
DR CCDS; CCDS21419.1; -.
DR RefSeq; NP_075361.2; NM_022985.6.
DR RefSeq; XP_006508168.1; XM_006508105.2.
DR RefSeq; XP_006508169.1; XM_006508106.2.
DR RefSeq; XP_006508170.1; XM_006508107.3.
DR RefSeq; XP_006508171.1; XM_006508108.1.
DR AlphaFoldDB; Q9DCH6; -.
DR SMR; Q9DCH6; -.
DR BioGRID; 211125; 4.
DR STRING; 10090.ENSMUSP00000069228; -.
DR iPTMnet; Q9DCH6; -.
DR PhosphoSitePlus; Q9DCH6; -.
DR EPD; Q9DCH6; -.
DR MaxQB; Q9DCH6; -.
DR PaxDb; Q9DCH6; -.
DR PeptideAtlas; Q9DCH6; -.
DR PRIDE; Q9DCH6; -.
DR ProteomicsDB; 298518; -.
DR Antibodypedia; 15226; 107 antibodies from 19 providers.
DR Ensembl; ENSMUST00000069537; ENSMUSP00000069228; ENSMUSG00000030629.
DR Ensembl; ENSMUST00000178385; ENSMUSP00000135968; ENSMUSG00000030629.
DR Ensembl; ENSMUST00000209117; ENSMUSP00000146518; ENSMUSG00000030629.
DR GeneID; 65098; -.
DR KEGG; mmu:65098; -.
DR UCSC; uc009iek.1; mouse.
DR CTD; 54469; -.
DR MGI; MGI:1929510; Zfand6.
DR VEuPathDB; HostDB:ENSMUSG00000030629; -.
DR eggNOG; KOG3173; Eukaryota.
DR GeneTree; ENSGT00940000160833; -.
DR HOGENOM; CLU_057016_1_0_1; -.
DR InParanoid; Q9DCH6; -.
DR OMA; DTTKCFS; -.
DR OrthoDB; 1551371at2759; -.
DR PhylomeDB; Q9DCH6; -.
DR TreeFam; TF313612; -.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 65098; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Zfand6; mouse.
DR PRO; PR:Q9DCH6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DCH6; protein.
DR Bgee; ENSMUSG00000030629; Expressed in metanephric cortical collecting duct and 259 other tissues.
DR ExpressionAtlas; Q9DCH6; baseline and differential.
DR Genevisible; Q9DCH6; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0006625; P:protein targeting to peroxisome; IDA:UniProtKB.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR Gene3D; 4.10.1110.10; -; 1.
DR InterPro; IPR035896; AN1-like_Znf.
DR InterPro; IPR002653; Znf_A20.
DR InterPro; IPR000058; Znf_AN1.
DR Pfam; PF01754; zf-A20; 1.
DR Pfam; PF01428; zf-AN1; 1.
DR SMART; SM00259; ZnF_A20; 1.
DR SMART; SM00154; ZnF_AN1; 1.
DR SUPFAM; SSF118310; SSF118310; 1.
DR PROSITE; PS51036; ZF_A20; 1.
DR PROSITE; PS51039; ZF_AN1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Cytoplasm; Metal-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Zinc; Zinc-finger.
FT CHAIN 1..223
FT /note="AN1-type zinc finger protein 6"
FT /id="PRO_0000245236"
FT ZN_FING 8..42
FT /note="A20-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT ZN_FING 158..204
FT /note="AN1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT REGION 41..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 30
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 33
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6FIF0"
FT MOD_RES 219
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MUTAGEN 30
FT /note="C->S: Abolishes interaction with PEX6 and ubiquitin.
FT Impairs interaction with PEX5."
FT /evidence="ECO:0000269|PubMed:21980954"
FT MUTAGEN 180
FT /note="C->S: Impairs interaction with PEX6."
FT /evidence="ECO:0000269|PubMed:21980954"
FT CONFLICT 99
FT /note="S -> P (in Ref. 1; CAC14886)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="Y -> S (in Ref. 1; CAC14886)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 223 AA; 24001 MW; FFBF1A09EEC39901 CRC64;
MAQETNHSQA PMLCSTGCGF YGNPRTNGMC SVCYKEHLQR QNSSNGRISP PAASVSSLSE
SLPVQCADGS VPDAQSALDS TSSSMQPGPV SNQSLLSESV APSQVDSTSV DKAVSETEDL
QGPRAEGLVP LECDPPSSVS DTTQQPSEEQ SKSLEKPKQK KNRCFMCRKK VGLTGFECRC
GNVYCGVHRY SDVHNCSYNY KADAAEKIRK ENPVVVGEKI QKI
