ZFN2A_RAT
ID ZFN2A_RAT Reviewed; 171 AA.
AC Q5U2P3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=AN1-type zinc finger protein 2A;
GN Name=Zfand2a;
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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DR EMBL; BC085928; AAH85928.1; -; mRNA.
DR RefSeq; NP_001008364.1; NM_001008363.1.
DR AlphaFoldDB; Q5U2P3; -.
DR SMR; Q5U2P3; -.
DR STRING; 10116.ENSRNOP00000043105; -.
DR PaxDb; Q5U2P3; -.
DR Ensembl; ENSRNOT00000083814; ENSRNOP00000069561; ENSRNOG00000032917.
DR GeneID; 360772; -.
DR KEGG; rno:360772; -.
DR UCSC; RGD:1310991; rat.
DR CTD; 90637; -.
DR RGD; 1310991; Zfand2a.
DR eggNOG; KOG3183; Eukaryota.
DR GeneTree; ENSGT00940000161571; -.
DR HOGENOM; CLU_061621_3_0_1; -.
DR InParanoid; Q5U2P3; -.
DR OMA; GCRRKEM; -.
DR OrthoDB; 1422113at2759; -.
DR PhylomeDB; Q5U2P3; -.
DR TreeFam; TF314219; -.
DR PRO; PR:Q5U2P3; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000032917; Expressed in jejunum and 20 other tissues.
DR Genevisible; Q5U2P3; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; ISO:RGD.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0045047; P:protein targeting to ER; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..171
FT /note="AN1-type zinc finger protein 2A"
FT /id="PRO_0000269890"
FT ZN_FING 4..52
FT /note="AN1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT ZN_FING 94..142
FT /note="AN1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT REGION 135..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
SQ SEQUENCE 171 AA; 19267 MW; 7494892B67B60EA6 CRC64;
MEFPDLGKHC SEPTCKQLDF LPITCDACKQ DFCKDHFSYS GHKCPFAFKK DVQVPVCPLC
NAPIPVRRGD IPDVVVGEHM DRDCTFHPGR NRNKVFTHRC SKEGCRKKEM LQLACAQCHG
NFCIQHRHPL DHNCQAGSSS VSRGRSSASR AAEQKPSGVS WLAQRLRRTV K
