ZN513_RAT
ID ZN513_RAT Reviewed; 541 AA.
AC Q5FWU5;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Zinc finger protein 513;
GN Name=Znf513; Synonyms=Zfp513;
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=Heart;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcriptional regulator that plays a role in retinal
CC development and maintenance. {ECO:0000250}.
CC -!- SUBUNIT: Binds DNA. Can associate with the proximal promoter regions of
CC PAX6 and SP4, and their known targets including ARR3, RHO, OPN1MW2 and
CC OPN1SW. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; BC089202; AAH89202.1; -; mRNA.
DR RefSeq; NP_001012110.1; NM_001012110.1.
DR AlphaFoldDB; Q5FWU5; -.
DR SMR; Q5FWU5; -.
DR STRING; 10116.ENSRNOP00000040002; -.
DR iPTMnet; Q5FWU5; -.
DR PhosphoSitePlus; Q5FWU5; -.
DR PaxDb; Q5FWU5; -.
DR Ensembl; ENSRNOT00000050102; ENSRNOP00000040002; ENSRNOG00000005298.
DR GeneID; 313913; -.
DR KEGG; rno:313913; -.
DR CTD; 101023; -.
DR RGD; 1310456; Zfp513.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158687; -.
DR HOGENOM; CLU_002678_58_1_1; -.
DR InParanoid; Q5FWU5; -.
DR OMA; SICGYSC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5FWU5; -.
DR PRO; PR:Q5FWU5; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000005298; Expressed in thymus and 20 other tissues.
DR Genevisible; Q5FWU5; RN.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; ISS:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..541
FT /note="Zinc finger protein 513"
FT /id="PRO_0000353094"
FT ZN_FING 150..172
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 178..200
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 206..228
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 360..382
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 388..410
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 416..438
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 444..466
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 472..494
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..57
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PD29"
SQ SEQUENCE 541 AA; 58091 MW; 4C3E23EB3F42B354 CRC64;
MPRRKQSHPQ PVKCEGVKVD TEDSFDEGPG ALVLESDLLL GQDLEFEEEE EEEEGDGHND
QLMGFERDSE GDSQGARPGL PYGLSDDESG GGRALSAESE VEEPARGPGE ARGERPGPAC
QLCGGPTGEG PCCGAGGPGG GPPLPPRLLY SCRLCAFVSH YSSHLKRHMQ THSGEKPFRC
GRCPYASAQL VNLTRHTRTH TGEKPYRCPH CPFACSSLGN LRRHQRTHTG PPTPPCPTCG
FRCCAPRPTR PPSPTEQEGT MPRRSEDALI LPDLSLHVPP GGTSFLPDCG QLRGEGEGLC
GTGSEPLPEL LFPWTCRGCG QELEEGEGSR LGTAMCGRCM RGESGGGGSG GPQGPSDKGF
ACSLCPFATH YPNHLARHMK THSGEKPFRC ARCPYASAHL DNLKRHQRVH TGEKPYKCPL
CPYACGNLAN LKRHGRIHSG DKPFRCSLCN YSCNQSMNLK RHMLRHTGEK PFRCATCAYT
TGHWDNYKRH QKVHGHGGAG GPGLSAPEGW APPHSPPSVL STRGSAALGA TGSRALHTDS
P
