ZFAN6_PONAB
ID ZFAN6_PONAB Reviewed; 208 AA.
AC Q5R7S6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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: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; CR860033; CAH92184.1; -; mRNA.
DR RefSeq; NP_001127520.1; NM_001134048.1.
DR AlphaFoldDB; Q5R7S6; -.
DR SMR; Q5R7S6; -.
DR STRING; 9601.ENSPPYP00000007617; -.
DR Ensembl; ENSPPYT00000007926; ENSPPYP00000007617; ENSPPYG00000006712.
DR GeneID; 100174596; -.
DR KEGG; pon:100174596; -.
DR CTD; 54469; -.
DR eggNOG; KOG3173; Eukaryota.
DR GeneTree; ENSGT00940000160833; -.
DR HOGENOM; CLU_057016_1_0_1; -.
DR InParanoid; Q5R7S6; -.
DR OMA; DTTKCFS; -.
DR OrthoDB; 1551371at2759; -.
DR TreeFam; TF313612; -.
DR Proteomes; UP000001595; Chromosome 15.
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 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 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Cytoplasm; Metal-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Zinc; Zinc-finger.
FT CHAIN 1..208
FT /note="AN1-type zinc finger protein 6"
FT /id="PRO_0000245237"
FT ZN_FING 8..42
FT /note="A20-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT ZN_FING 143..189
FT /note="AN1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT REGION 41..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..135
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 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 181
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 204
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCH6"
SQ SEQUENCE 208 AA; 22599 MW; 331E595F2DDF8E93 CRC64;
MAQETNHSQV PMLCSTGCGF YGNPRTNGMC SVCYKEHLQR QNSSNGRISP PATSVSSLSE
SLPVQCTDGS VPEAQSTLDS TSSSMQPSPV SNQSLLSESV ASSQLDSTSV DKAVPETEDL
QASVSDTAQQ PSEEQSKSLE KPKQKKNRCF MCRKKVGLTG FECRCGNVYC GVHRYSDVHN
CSYNYKADAA EKIRKENPVV VGEKIQKI
