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 25-MAY-2022, entry version 76.
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; 612611at2759; -.
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; 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; 3.
DR SMART; SM00451; ZnF_U1; 3.
DR SUPFAM; SSF57667; SSF57667; 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
