ZFR_RAT
ID ZFR_RAT Reviewed; 1073 AA.
AC Q562A2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Zinc finger RNA-binding protein;
GN Name=Zfr;
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 MRNA] OF 848-1073.
RC TISSUE=Brain;
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 [3]
RP FUNCTION, IDENTIFICATION IN A CYTOPLASMIC MRNP COMPLEX WITH STAU2,
RP INTERACTION WITH STAU2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16277607; DOI=10.1111/j.1471-4159.2005.03523.x;
RA Elvira G., Massie B., DesGroseillers L.;
RT "The zinc-finger protein ZFR is critical for Staufen 2 isoform specific
RT nucleocytoplasmic shuttling in neurons.";
RL J. Neurochem. 96:105-117(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1053, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1053, 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: Involved in postimplantation and gastrulation stages of
CC development (By similarity). Binds to DNA and RNA (By similarity).
CC Involved in the nucleocytoplasmic shuttling of STAU2. {ECO:0000250,
CC ECO:0000269|PubMed:16277607}.
CC -!- SUBUNIT: Interacts with STAU2. Found in a cytoplasmic mRNP complex with
CC STAU2. Does not interact with STAU1. {ECO:0000269|PubMed:16277607}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16277607}. Cytoplasm
CC {ECO:0000269|PubMed:16277607}. Cytoplasmic granule
CC {ECO:0000269|PubMed:16277607}. Chromosome {ECO:0000250}. Note=Localizes
CC in somatodendritic compartment of primary hippocampal neurons.
CC Colocalizes with STAU2 in several cytosolic RNA granules. Associated
CC with chromosome foci in meiotic cells (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in hippocampus.
CC {ECO:0000269|PubMed:16277607}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AABR03015519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03021812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03017146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03016281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03012204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC092648; AAH92648.1; -; mRNA.
DR AlphaFoldDB; Q562A2; -.
DR SMR; Q562A2; -.
DR STRING; 10116.ENSRNOP00000016196; -.
DR iPTMnet; Q562A2; -.
DR PhosphoSitePlus; Q562A2; -.
DR jPOST; Q562A2; -.
DR PaxDb; Q562A2; -.
DR PRIDE; Q562A2; -.
DR RGD; 1311890; Zfr.
DR VEuPathDB; HostDB:ENSRNOG00000011627; -.
DR eggNOG; KOG3792; Eukaryota.
DR HOGENOM; CLU_012026_1_0_1; -.
DR InParanoid; Q562A2; -.
DR PhylomeDB; Q562A2; -.
DR PRO; PR:Q562A2; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011627; Expressed in Ammon's horn and 20 other tissues.
DR ExpressionAtlas; Q562A2; baseline and differential.
DR Genevisible; Q562A2; RN.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR006561; DZF_dom.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF07528; DZF; 1.
DR SMART; SM00572; DZF; 1.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS51703; DZF; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Cytoplasm; Developmental protein; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..1073
FT /note="Zinc finger RNA-binding protein"
FT /id="PRO_0000312722"
FT DOMAIN 702..1072
FT /note="DZF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01040"
FT REGION 120..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 508
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96KR1"
FT MOD_RES 515
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O88532"
FT MOD_RES 1053
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT CROSSLNK 508
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96KR1"
FT CROSSLNK 540
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96KR1"
FT CROSSLNK 622
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96KR1"
FT CONFLICT 983
FT /note="N -> S (in Ref. 2; AAH92648)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1073 AA; 116818 MW; 95D356D3B61549FF CRC64;
MIPICPVVSF TYVPSRLGED AKMATGNYFG FTHSGAAAAA AAAQYSQQPA SGVAYSHPTT
VASYTVHQAP VAAHTVTAAY APAAATVAVA RPAPVAVAAA ATAAAYGGYP TAHTATDYGY
TQRQQEAPPP PPPATTQNYQ DSYSYVRSTA PAVAYDSKQY YQQPTATAAA VAAAAQPQPS
VAETYYQTAP KAGYSQGATQ YTQAQQARQV TAIKPATPSP ATTTFSIYPV SSTVQPVAAA
ATVVPSYTQS ATYSTTAVTY SGTSYSGYEA AVYSAASSYY QQQQQQQKQA AAAAAAAAAT
AAWTGTTFTK KTPFQNKQLK PKQPPKPPQI HYCDVCKISC AGPQVFILCI YHESQCTFTS
VYSVLCNSPI DQKDACGKLH LCRLCDVSCT GADAYAAHIR GAKHQKVVKL HTKLGKPIPS
TEPNVVSQAT SSTAVSASKP TASPSSIGAS NCTLNTSSIA TTSVKGLSTT GNSSLNSTSN
TKVSAVPTNM AAKKTSTPKI NFVGGGNKLQ STGNKAEDLK GTDCIKNNPA ASAVQIPEVK
QDAVSEPVTP ASLAALQSDV QPVGHDYVEE VRNDEGKVIR FHCKLCECSF NDPNAKEMHL
KGRRHRLQYK KKVNPDLQVE VKPSIRARKI QEEKMRKQMQ KEEYWRRREE EERWRMEIRR
YEEDMYWRRM EEEQHHWDDR RRMPDGGYPH GPPGPLGLLG VRPGMPPQPQ GPAPLRRPDS
SDDRYVMTKH ATIYPTEEEL QAVQKIVSIT ERALKLVSDS LSEHEKSKNK EGDDKKEGGK
DRSLKGVLRV GVLAKGLLLR GDRNVNLVLL CSEKPSKSLL SRIAENLPKQ LAVISPEKYD
IKCAVSEAAI ILNSCVEPKM QVTITLTSPI IREENMREGD VTSGMVKDPP DVLDRQKCLD
ALAALRHAKW FQARANGLQS CVIIIRILRD LCQRVPTWSD FPSWAMELLV EKAISSASSP
QSPGDALRRV FECISSGIIL KGNPGLLDPC EKDPFDTLAT MTDQQREDIT SSAQFALRLL
AFRQIHKVLG MDPLPQMNQR FNIHNNRKRR RDSDGVDGFE AEGKKDKKDY DNF
