ZOP1_ARATH
ID ZOP1_ARATH Reviewed; 242 AA.
AC Q7XA66; Q94AV7; Q9FX87;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Zinc finger protein ZOP1 {ECO:0000305};
DE AltName: Full=Zinc-finger and OCRE domain-containing protein 1 {ECO:0000303|PubMed:23524848};
GN Name=ZOP1 {ECO:0000303|PubMed:23524848};
GN OrderedLocusNames=At1g49590 {ECO:0000312|Araport:AT1G49590};
GN ORFNames=F14J22.17 {ECO:0000312|EMBL:AAG13045.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, INTERACTION WITH STA1, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP IN PRE-MRNA SPLICING COMPLEX.
RX PubMed=23524848; DOI=10.1038/emboj.2013.49;
RA Zhang C.J., Zhou J.X., Liu J., Ma Z.Y., Zhang S.W., Dou K., Huang H.W.,
RA Cai T., Liu R., Zhu J.K., He X.J.;
RT "The splicing machinery promotes RNA-directed DNA methylation and
RT transcriptional silencing in Arabidopsis.";
RL EMBO J. 32:1128-1140(2013).
RN [5]
RP INTERACTION WITH PRP31, AND SUBCELLULAR LOCATION.
RX PubMed=25684655; DOI=10.1016/j.molp.2015.02.003;
RA Du J.L., Zhang S.W., Huang H.W., Cai T., Li L., Chen S., He X.J.;
RT "The splicing factor PRP31 is involved in transcriptional gene silencing
RT and stress response in Arabidopsis.";
RL Mol. Plant 8:1053-1068(2015).
CC -!- FUNCTION: Nucleic acid-binding protein that promotes Pol IV-dependent
CC small interfering RNA (siRNA) accumulation, DNA methylation and
CC transcriptional silencing. May possess both RNA-directed DNA
CC methylation (RdDM)-dependent and -independent roles in transcriptional
CC silencing. Acts as a pre-mRNA splicing factor that associates with
CC several typical components of the splicing machinery as well as with
CC Pol II. {ECO:0000269|PubMed:23524848}.
CC -!- SUBUNIT: Component of a pre-mRNA splicing complex. Interacts with STA1.
CC Interacts with PRP31 (PubMed:25684655). {ECO:0000269|PubMed:23524848,
CC ECO:0000269|PubMed:25684655}.
CC -!- INTERACTION:
CC Q7XA66; Q9ZT71: STA1; NbExp=2; IntAct=EBI-4429233, EBI-6921761;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130,
CC ECO:0000269|PubMed:23524848, ECO:0000269|PubMed:25684655}. Nucleus,
CC Cajal body {ECO:0000269|PubMed:23524848, ECO:0000269|PubMed:25684655}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q7XA66-1; Sequence=Displayed;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG13045.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC011807; AAG13045.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32445.1; -; Genomic_DNA.
DR EMBL; AY045687; AAK74045.1; -; mRNA.
DR EMBL; BT010196; AAQ22665.1; -; mRNA.
DR PIR; E96532; E96532.
DR RefSeq; NP_175382.1; NM_103847.5. [Q7XA66-1]
DR AlphaFoldDB; Q7XA66; -.
DR SMR; Q7XA66; -.
DR IntAct; Q7XA66; 28.
DR MINT; Q7XA66; -.
DR STRING; 3702.AT1G49590.1; -.
DR PaxDb; Q7XA66; -.
DR PRIDE; Q7XA66; -.
DR ProteomicsDB; 242978; -. [Q7XA66-1]
DR EnsemblPlants; AT1G49590.1; AT1G49590.1; AT1G49590. [Q7XA66-1]
DR GeneID; 841383; -.
DR Gramene; AT1G49590.1; AT1G49590.1; AT1G49590. [Q7XA66-1]
DR KEGG; ath:AT1G49590; -.
DR Araport; AT1G49590; -.
DR TAIR; locus:2012222; AT1G49590.
DR eggNOG; KOG0150; Eukaryota.
DR HOGENOM; CLU_072188_0_0_1; -.
DR InParanoid; Q7XA66; -.
DR OMA; RLNTMRQ; -.
DR PhylomeDB; Q7XA66; -.
DR PRO; PR:Q7XA66; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q7XA66; baseline and differential.
DR GO; GO:0015030; C:Cajal body; IDA:TAIR.
DR GO; GO:0071011; C:precatalytic spliceosome; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:TAIR.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0080188; P:gene silencing by RNA-directed DNA methylation; IMP:TAIR.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0008380; P:RNA splicing; IMP:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR CDD; cd16165; OCRE_ZOP1_plant; 1.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR041591; OCRE.
DR InterPro; IPR013085; U1-CZ_Znf_C2H2.
DR InterPro; IPR040023; WBP4.
DR InterPro; IPR035622; ZOP1_OCRE.
DR PANTHER; PTHR13173; PTHR13173; 1.
DR Pfam; PF17780; OCRE; 1.
DR Pfam; PF06220; zf-U1; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; DNA-binding; Metal-binding;
KW mRNA processing; mRNA splicing; Nucleus; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Spliceosome; Zinc; Zinc-finger.
FT CHAIN 1..242
FT /note="Zinc finger protein ZOP1"
FT /id="PRO_0000436557"
FT ZN_FING 11..42
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 154..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 42..71
FT /evidence="ECO:0000255"
FT COMPBIAS 196..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 242 AA; 27052 MW; C28C0083981D3356 CRC64;
MTEYWVSQGN KWCEFCKIWI QNNPTSIRNH DLGKRHRECV DKKLTDMRER SAAKDKELKK
NEKLLQQIEA KATRSYQKDI ATAQQVAKAN GAPEDGTSDW MLDSASGYYY NQTNGLHYDS
QSGFYYSDSI GHWVTQDEAY AAVKTSSGTK VPLVKKPVSS SGAGPSVGKP PGRLVTASLN
PKRAVKGAAS SVDLGNNKRK RQDEKPKKVS AEEKAALKAR EAARKRVEDR EKPLLGLYNR
PF
