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Database: UniProt
Entry: ZFR_PONAB
LinkDB: ZFR_PONAB
Original site: ZFR_PONAB 
ID   ZFR_PONAB               Reviewed;        1074 AA.
AC   Q5REX3;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 79.
DE   RecName: Full=Zinc finger RNA-binding protein;
GN   Name=ZFR;
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 postimplantation and gastrulation stages of
CC       development. Involved in the nucleocytoplasmic shuttling of STAU2.
CC       Binds to DNA and RNA (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Found in a cytoplasmic RNP complex with STAU2. Interacts with
CC       STAU2. Does not interact with STAU1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasmic granule.
CC       Chromosome. Note=Associated with chromosome foci in meiotic cells.
CC       Localizes in somatodendritic compartment of primary hippocampal
CC       neurons. Colocalizes with STAU2 in several cytosolic RNA granules (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; CR857391; CAH89684.1; -; mRNA.
DR   RefSeq; NP_001124762.1; NM_001131290.1.
DR   AlphaFoldDB; Q5REX3; -.
DR   SMR; Q5REX3; -.
DR   STRING; 9601.ENSPPYP00000017176; -.
DR   GeneID; 100171613; -.
DR   KEGG; pon:100171613; -.
DR   CTD; 51663; -.
DR   eggNOG; KOG3792; Eukaryota.
DR   InParanoid; Q5REX3; -.
DR   OrthoDB; 4565640at2759; -.
DR   Proteomes; UP000001595; Unplaced.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 1.10.1410.40; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 3.
DR   InterPro; IPR006561; DZF_dom.
DR   InterPro; IPR049402; DZF_dom_C.
DR   InterPro; IPR049401; DZF_dom_N.
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   PANTHER; PTHR45762; ZINC FINGER RNA-BINDING PROTEIN; 1.
DR   PANTHER; PTHR45762:SF3; ZINC FINGER RNA-BINDING PROTEIN; 1.
DR   Pfam; PF20965; DZF_C; 1.
DR   Pfam; PF07528; DZF_N; 1.
DR   Pfam; PF12874; zf-met; 3.
DR   SMART; SM00572; DZF; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SMART; SM00451; ZnF_U1; 3.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS51703; DZF; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PE   2: Evidence at transcript 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..1074
FT                   /note="Zinc finger RNA-binding protein"
FT                   /id="PRO_0000312721"
FT   DOMAIN          703..1073
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          349..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..723
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..781
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1040..1074
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        363..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1048..1074
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         509
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q96KR1"
FT   MOD_RES         516
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O88532"
FT   MOD_RES         1054
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96KR1"
FT   CROSSLNK        509
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q96KR1"
FT   CROSSLNK        541
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96KR1"
FT   CROSSLNK        623
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96KR1"
SQ   SEQUENCE   1074 AA;  117139 MW;  63AAFE4A1D465461 CRC64;
     MIPICPVVSF TYVPSRLGED AKMATGNYFG FTHSGAAAAA AAAQYSQQPA SGVAYSHPTT
     VASYTVHQAP VAAHTVTAAY APAAATVAVA RPAPVAVAAA ATAAAYGGYP TAHTATDYGY
     TQRQQEAPPP PPPATTQNYQ DSYSYVRSTA PAVAYDSKQY YQQPTATAAA VAAAAQPQPS
     VAETYYQTAP KAGYSQGATQ YTQAQQTRQV TAIKPATPSP ATTTFSIYPV SSTVQPVAAA
     ATVVPSYTQS ATYSTTAVTY SGTSYSGYEA AVYSAASSYY QQQQQQQKQA AAAAAAAAAT
     AAWTGTTFTK KAPFQNKQLK PKQPPKPPQI HYCDVCKISC AGPQTYKEHL EGQKHKKKEA
     ALKASQNASS SNNSTRGTQN QLRCELCDVS CTGADAYAAH IRGAKHQKVV KLHTKLGKPI
     PSTEPNVVSQ ATSSTAVSAS KPTASPSSIA ANNCTVNTSS IATSSMKGLT TTGNSSLNST
     SNTKVSAVPT NMAAKKTSTP KINFVGGNKL QSTGNKTEDI KGTECVKSTP VTSAVQIPEV
     KQDTVSEPVT PASLAVLQSD VQPVGHDYVE EVRNDEGKVI RFHCKLCECS FNDPNAKEMH
     LKGRRHRLQY KKKVNPDLQV EVKPSIRARK IQEEKMRKQM QREEYWRRRE EEERWRMEMR
     RYEEDMYWRR MEEEQHHWDD RRRMPDGGYP HGPPGPLGLL GVRPGMPPQP QGPAPLRRPD
     SSDDRYVMTK HATIYPTEEE LQAVQKIVSI TERALKLVSD SLSEHEKNKN KEGDDKKEGS
     KDRALKGVLR VGVLAKGLLL RGDRNVNLVL LCSEKPSKTL LSRIAENLPK QLAVISPEKY
     DIKCAVSEAA IILNSCVEPK MQVTITLTSP IIREENMREG DVTSGMVKDP PDVLDRQKCL
     DALAALRHAK WFQARANGLQ SCVIIIRILR DLCQRVPTWS DFPSWAMELL VEKAISSASS
     PQSPGDALRR VFECISSGII LKGSPGLLDP CEKDPFDTLA TMTDQQREDI TSSAQFALRL
     LAFRQIHKVL GMDPLPQMSQ RFNIHNNRKR RRDSDGVDGF EAEGKKDKKD YDNF
//
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