ZFAN5_RAT
ID ZFAN5_RAT Reviewed; 213 AA.
AC B5DF11;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=AN1-type zinc finger protein 5;
DE AltName: Full=Zinc finger protein 216;
GN Name=Zfand5; Synonyms=Zfp216, Znf216;
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP STRUCTURE BY NMR OF 1-60 IN COMPLEX WITH UBIQUITIN, IDENTIFICATION IN A
RP COMPLEX WITH SQSTM1 AND UBIQUITIN, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=21923101; DOI=10.1021/bi201137e;
RA Garner T.P., Strachan J., Shedden E.C., Long J.E., Cavey J.R., Shaw B.,
RA Layfield R., Searle M.S.;
RT "Independent interactions of ubiquitin-binding domains in a ubiquitin-
RT mediated ternary complex.";
RL Biochemistry 50:9076-9087(2011).
CC -!- FUNCTION: Involved in protein degradation via the ubiquitin-proteasome
CC system. May act by anchoring ubiquitinated proteins to the proteasome.
CC Plays a role in ubiquitin-mediated protein degradation during muscle
CC atrophy. Plays a role in the regulation of NF-kappa-B activation and
CC apoptosis. Inhibits NF-kappa-B activation triggered by overexpression
CC of RIPK1 and TRAF6 but not of RELA. Inhibits also tumor necrosis factor
CC (TNF), IL-1 and TLR4-induced NF-kappa-B activation in a dose-dependent
CC manner. Overexpression sensitizes cells to TNF-induced apoptosis. Is a
CC potent inhibitory factor for osteoclast differentiation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer and/or heterooligomer. Interacts (via A20-type
CC domain) with IKBKG and RIPK1 and with TRAF6 (via AN1-type domain) (By
CC similarity). Interacts with ubiquitin and polyubiquitinated proteins.
CC Identified in a heterotrimeric complex with ubiquitin and SQSTM1, where
CC ZFAND5 and SQSTM1 both interact with the same ubiquitin molecule.
CC {ECO:0000250, ECO:0000269|PubMed:21923101}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21923101}.
CC -!- DOMAIN: The A20-type zinc finger directly binds polyubiquitin chains
CC and associates with the 26S proteasome. The zinc-finger A20-type domain
CC is essential for inhibition of NF-kappa-B activation (By similarity).
CC {ECO:0000250}.
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DR EMBL; CH473953; EDM13001.1; -; Genomic_DNA.
DR EMBL; BC168882; AAI68882.1; -; mRNA.
DR RefSeq; XP_008758519.1; XM_008760297.2.
DR PDB; 2KZY; NMR; -; A=1-60.
DR PDB; 2L00; NMR; -; A=1-60.
DR PDBsum; 2KZY; -.
DR PDBsum; 2L00; -.
DR AlphaFoldDB; B5DF11; -.
DR BMRB; B5DF11; -.
DR SMR; B5DF11; -.
DR STRING; 10116.ENSRNOP00000024583; -.
DR PhosphoSitePlus; B5DF11; -.
DR PaxDb; B5DF11; -.
DR PeptideAtlas; B5DF11; -.
DR PRIDE; B5DF11; -.
DR Ensembl; ENSRNOT00000024583; ENSRNOP00000024583; ENSRNOG00000018107.
DR GeneID; 293960; -.
DR CTD; 7763; -.
DR RGD; 1310776; Zfand5.
DR eggNOG; KOG3173; Eukaryota.
DR GeneTree; ENSGT00940000156165; -.
DR HOGENOM; CLU_057016_1_0_1; -.
DR InParanoid; B5DF11; -.
DR OMA; AHGCSFD; -.
DR OrthoDB; 1551371at2759; -.
DR PhylomeDB; B5DF11; -.
DR TreeFam; TF313612; -.
DR EvolutionaryTrace; B5DF11; -.
DR PRO; PR:B5DF11; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Proteomes; UP000234681; Chromosome 1.
DR Bgee; ENSRNOG00000018107; Expressed in Ammon's horn and 20 other tissues.
DR Genevisible; B5DF11; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0060324; P:face development; ISO:RGD.
DR GO; GO:0010761; P:fibroblast migration; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0003016; P:respiratory system process; ISO:RGD.
DR GO; GO:0048705; P:skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0048745; P:smooth muscle tissue development; ISO:RGD.
DR GO; GO:0001944; P:vasculature development; 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 3D-structure; Acetylation; Cytoplasm; Metal-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..213
FT /note="AN1-type zinc finger protein 5"
FT /id="PRO_0000415373"
FT ZN_FING 8..42
FT /note="A20-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00451"
FT ZN_FING 148..194
FT /note="AN1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT REGION 39..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..142
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 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 168
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="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 175
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="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O76080"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88878"
FT MOD_RES 209
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O88878"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2KZY"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:2KZY"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:2KZY"
SQ SEQUENCE 213 AA; 23088 MW; B293DB1A55E79B9B CRC64;
MAQETNQTPG PMLCSTGCGF YGNPRTNGMC SVCYKEHLQR QQNSGRMSPM GTASGSNSPT
SDSASVQRAD ATLNNCEGAA GSTSEKSRNV PVAALPVTQQ MTEMSISRED KITSPKTEVS
EPVVTQPSPS VSQPSSSQSE EKAPELPKPK KNRCFMCRKK VGLTGFDCRC GNLFCGLHRY
SDKHNCPYDY KAEAAAKIRK ENPVVVAEKI QRI
