ZFAN6_RAT
ID ZFAN6_RAT Reviewed; 223 AA.
AC Q6DGF4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=AN1-type zinc finger protein 6;
DE AltName: Full=Zinc finger A20 domain-containing protein 3;
GN Name=Zfand6; Synonyms=Za20d3;
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).
RN [2]
RP PROTEIN SEQUENCE OF 26-40; 153-158; 181-201 AND 212-219, AND SUBCELLULAR
RP LOCATION.
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).
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. Required for PTS1 target sequence-dependent protein import
CC into peroxisomes and PEX5 stability; may cooperate with PEX6. In vitro
CC involved in PEX5 export from the cytosol to peroxisomes (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PKN1. Interacts with TRAF2. Interacts with
CC mono- and polyubiquitin. Interacts with PEX6. Interacts with PEX5 (Cys-
CC linked ubiquitinated) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21980954}.
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; BC076394; AAH76394.1; -; mRNA.
DR RefSeq; NP_001007631.1; NM_001007630.1.
DR RefSeq; XP_006229561.1; XM_006229499.2.
DR RefSeq; XP_006229562.1; XM_006229500.3.
DR RefSeq; XP_006229564.1; XM_006229502.3.
DR RefSeq; XP_006229566.1; XM_006229504.2.
DR RefSeq; XP_017444432.1; XM_017588943.1.
DR AlphaFoldDB; Q6DGF4; -.
DR SMR; Q6DGF4; -.
DR STRING; 10116.ENSRNOP00000018098; -.
DR iPTMnet; Q6DGF4; -.
DR PhosphoSitePlus; Q6DGF4; -.
DR PaxDb; Q6DGF4; -.
DR PRIDE; Q6DGF4; -.
DR Ensembl; ENSRNOT00000018098; ENSRNOP00000018098; ENSRNOG00000013506.
DR GeneID; 293067; -.
DR KEGG; rno:293067; -.
DR UCSC; RGD:1359317; rat.
DR CTD; 54469; -.
DR RGD; 1359317; Zfand6.
DR eggNOG; KOG3173; Eukaryota.
DR GeneTree; ENSGT00940000160833; -.
DR HOGENOM; CLU_057016_1_0_1; -.
DR InParanoid; Q6DGF4; -.
DR OMA; DTTKCFS; -.
DR OrthoDB; 1551371at2759; -.
DR PhylomeDB; Q6DGF4; -.
DR TreeFam; TF313612; -.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR PRO; PR:Q6DGF4; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000013506; Expressed in esophagus and 20 other tissues.
DR Genevisible; Q6DGF4; RN.
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; ISS: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; ISS:UniProtKB.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; ISO:RGD.
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; Direct protein sequencing;
KW Metal-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Transport; Zinc; Zinc-finger.
FT CHAIN 1..223
FT /note="AN1-type zinc finger protein 6"
FT /id="PRO_0000245238"
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:0000250|UniProtKB:Q9DCH6"
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
