UBA1C_ARATH
ID UBA1C_ARATH Reviewed; 613 AA.
AC O64571;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=UBP1-associated proteins 1C;
GN Name=UBA1C; OrderedLocusNames=At2g19380; ORFNames=F27F23.27;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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).
CC -!- FUNCTION: May regulate the turnover of mRNAs in the nucleus.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AC003058; AAC16468.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC06874.1; -; Genomic_DNA.
DR PIR; T01286; T01286.
DR RefSeq; NP_565450.1; NM_127495.2.
DR AlphaFoldDB; O64571; -.
DR SMR; O64571; -.
DR STRING; 3702.AT2G19380.1; -.
DR PaxDb; O64571; -.
DR PRIDE; O64571; -.
DR ProteomicsDB; 242616; -.
DR EnsemblPlants; AT2G19380.1; AT2G19380.1; AT2G19380.
DR GeneID; 816456; -.
DR Gramene; AT2G19380.1; AT2G19380.1; AT2G19380.
DR KEGG; ath:AT2G19380; -.
DR Araport; AT2G19380; -.
DR TAIR; locus:2047685; AT2G19380.
DR eggNOG; KOG2186; Eukaryota.
DR HOGENOM; CLU_445767_0_0_1; -.
DR InParanoid; O64571; -.
DR OMA; CIDCGNM; -.
DR OrthoDB; 1567501at2759; -.
DR PhylomeDB; O64571; -.
DR PRO; PR:O64571; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64571; baseline and differential.
DR Genevisible; O64571; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR014898; Znf_C2H2_LYAR.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF08790; zf-LYAR; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SMART; SM00451; ZnF_U1; 3.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS51804; ZF_C2HC_LYAR; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW Metal-binding; Nucleus; Reference proteome; Repeat; RNA-binding; Zinc;
KW Zinc-finger.
FT CHAIN 1..613
FT /note="UBP1-associated proteins 1C"
FT /id="PRO_0000425439"
FT DOMAIN 408..485
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 1..26
FT /note="C2HC LYAR-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT ZN_FING 27..51
FT /note="C2HC LYAR-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT ZN_FING 85..115
FT /note="Matrin-type 1"
FT ZN_FING 154..184
FT /note="Matrin-type 2"
FT ZN_FING 224..254
FT /note="Matrin-type 3"
FT REGION 322..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 6
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01145"
SQ SEQUENCE 613 AA; 69597 MW; F569EDFD506DFCBB CRC64;
MVWFQCDDCG ENLKKPRLPR HMSMCTATKF SCIDCGNMFG QVSVHYHNQC ITEAEKYGPM
VRSNGESSKQ KHDFDINAEL FNSQWFCSLC NATMTCEQDY FAHVYGKKHQ EKANEVADMD
YSKQQSEHPA VDKNNLTQQP DLDIYVGLSN DYPWFCSLCD INATSEQTLL AHANGKKHRV
KVERFDAEQQ KRQSTQHSTV DKKDYSKQQI EVDINVGLSN CYPWFCSLCN VKATCQQNLL
SHANGRKHRE NVELFDATQQ QQLEKTTVDK KDTTVNASDG NSEQKKVDLL VSSGVANGYS
QAHKKRKLET CDETWKREVV QAEEAKGGGE QKSESKKAKK QDKEKKRKKD KKQTKSDSDF
EHDKEDIKQL LVAYSKEELV NLIYKTAEKG SRLISAILES ADRDIAQRNI FVRGFGWDTT
QENLKTAFES YGEIEECSVV MDKDTGRGKG YGFVMFKTRK GAREALKRPE KRMYNRIVVC
NLASEKPGKA GKEQDMAEPV NIDLTKMANQ SEAVLPGIEL GRGHVLEKMH HQQQQTMDMF
GQNMPFYGYS HQFPGFDPMY GALSGNQMLA GLPNYGMFGS GMMTNQGSML PPPNHLGMAG
QYFGDGEQAW HQR
