ZPR1_PAPAN
ID ZPR1_PAPAN Reviewed; 459 AA.
AC A9CB27;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Zinc finger protein ZPR1;
DE AltName: Full=Zinc finger protein 259;
GN Name=ZNF259; Synonyms=ZPR1;
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA Tsipouri V., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as a signaling molecule that communicates proliferative
CC growth signals from the cytoplasm to the nucleus. Plays a role for the
CC localization and accumulation of the survival motor neuron protein SMN1
CC in sub-nuclear bodies, including gems and Cajal bodies. Induces neuron
CC differentiation and stimulates axonal growth and formation of growth
CC cone in spinal cord motor neurons. Plays a role in the splicing of
CC cellular pre-mRNAs. May be involved in H(2)O(2)-induced neuronal cell
CC death (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of an import snRNP complex composed of KPNB1, SNUPN,
CC SMN1 and ZNF259. Interacts (via C-terminal region) with SMN1 (via C-
CC terminal region); the interaction occurs after treatment with serum.
CC Interacts with elongation factor 1-alpha EEF1A1; the interaction occurs
CC in a epidermal growth factor (EGF)-dependent manner. Interacts (via
CC zinc fingers) with EGFR (via C-terminal cytoplasmic kinase domain); the
CC interaction is negatively regulated in response to epidermal growth
CC factor (EGF) stimulation and EGFR kinase activity. May also bind to the
CC PDGFR receptor (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Nucleus, nucleolus {ECO:0000250}. Cytoplasm, perinuclear region
CC {ECO:0000250}. Nucleus, gem {ECO:0000250}. Nucleus, Cajal body
CC {ECO:0000250}. Cell projection, axon {ECO:0000250}. Cell projection,
CC growth cone {ECO:0000250}. Note=Localized predominantly in the
CC cytoplasm in serum-starved cells growth arrested in G0 of the mitotic
CC cell cycle. Localized both in the nucleus and cytoplasm at the G1 phase
CC of the mitotic cell cycle. Accumulates in the subnuclear bodies during
CC progression into the S phase of the mitotic cell cycle. Diffusely
CC localized throughout the cell during mitosis. Colocalized with NPAT and
CC SMN1 in nuclear bodies including gems (Gemini of coiled bodies) and
CC Cajal bodies in a cell cycle-dependent manner. Colocalized with EGFR in
CC the cytoplasm of quiescent cells. Translocates from the cytoplasm to
CC the nucleus in a epidermal growth factor (EGF)-dependent manner.
CC Translocates together with EEF1A1 from the cytoplasm to the nucleolus
CC after treatment with mitogens. Colocalized with SMN1 in Gemini of
CC coiled bodies (gems), Cajal bodies, axon and growth cones of neurons
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ZPR1 family. {ECO:0000305}.
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DR EMBL; DP000486; ABW96811.1; -; Genomic_DNA.
DR RefSeq; NP_001162238.1; NM_001168767.1.
DR AlphaFoldDB; A9CB27; -.
DR SMR; A9CB27; -.
DR STRING; 9555.ENSPANP00000010519; -.
DR PRIDE; A9CB27; -.
DR Ensembl; ENSPANT00000001956; ENSPANP00000010519; ENSPANG00000006431.
DR GeneID; 100137229; -.
DR KEGG; panu:100137229; -.
DR CTD; 8882; -.
DR eggNOG; KOG2703; Eukaryota.
DR GeneTree; ENSGT00390000014500; -.
DR OMA; PVQSQKG; -.
DR OrthoDB; 453044at2759; -.
DR Proteomes; UP000028761; Chromosome 12.
DR Bgee; ENSPANG00000006431; Expressed in pancreas and 66 other tissues.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0015030; C:Cajal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1902742; P:apoptotic process involved in development; ISS:UniProtKB.
DR GO; GO:0061564; P:axon development; ISS:UniProtKB.
DR GO; GO:0030576; P:Cajal body organization; ISS:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0042023; P:DNA endoreduplication; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0045927; P:positive regulation of growth; ISS:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:1990261; P:pre-mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0031641; P:regulation of myelination; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0021510; P:spinal cord development; ISS:UniProtKB.
DR GO; GO:0001834; P:trophectodermal cell proliferation; ISS:UniProtKB.
DR Gene3D; 2.20.25.420; -; 2.
DR Gene3D; 2.60.120.1040; -; 2.
DR InterPro; IPR004457; Znf_ZPR1.
DR InterPro; IPR040141; ZPR1.
DR InterPro; IPR042451; ZPR1_A/B_dom.
DR InterPro; IPR042452; ZPR1_Znf1/2.
DR PANTHER; PTHR10876; PTHR10876; 1.
DR Pfam; PF03367; zf-ZPR1; 2.
DR SMART; SM00709; Zpr1; 2.
DR TIGRFAMs; TIGR00310; ZPR1_znf; 2.
PE 3: Inferred from homology;
KW Cell projection; Cytoplasm; Differentiation; Metal-binding;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..459
FT /note="Zinc finger protein ZPR1"
FT /id="PRO_0000328435"
FT ZN_FING 51..83
FT /note="C4-type 1"
FT ZN_FING 259..291
FT /note="C4-type 2"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 51067 MW; 9A742761D1F96A22 CRC64;
MAASGAVEPG PPGAAVAPSP ALAPPPAPDH LFRPISAEDE EQQPTEIESL CMNCYCNGMT
RLLLTKIPFF REIIVSSFSC EHCGWNNTEI QSAGRVQDQG VRYTLTVRAP EDMNREVVKT
DSATTRIPEL DFEIPAFSQK GALTTVEGLI TRAISGLEQD QPARRANKDA TAERIDEFIV
KLKELKQVAS PFTLIIDDPS GNSFVENPHA PQKDDSLVIT HYNRTQHQKE MLGLQEEAPA
EKPEEEDLRN EVLQFNTNCP ECNAPAQTNM KLVQIPHFKE VIIMATNCEN CGHRTNEVKS
GGAVEPLGTR ITLHITDPSD MTRDLLKSET CSVEIPELEF ELGMAVLGGK FTTLEGLLKD
IRELVTKNPF TLGDSSNPCQ KERLQEFSQK MDQIIEGNMK AHFIMDDPAG NSYLQNVYAP
EDDPEMKVER YKRTFDQNEE LGLNDMKTEG YEAGLASQR
