PIAL2_ARATH
ID PIAL2_ARATH Reviewed; 760 AA.
AC F4JYG0; Q0WP46; Q9FFS2;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=E4 SUMO-protein ligase PIAL2 {ECO:0000303|PubMed:25415977};
DE EC=2.3.2.- {ECO:0000269|PubMed:25415977};
DE AltName: Full=Protein INHIBITOR OF ACTIVATED STAT-LIKE 2 {ECO:0000303|PubMed:25415977};
GN Name=PIAL2 {ECO:0000303|PubMed:25415977};
GN OrderedLocusNames=At5g41580 {ECO:0000312|Araport:AT5G41580};
GN ORFNames=MBK23.10 {ECO:0000312|EMBL:BAB11464.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-329; CYS-355;
RP 425-VAL--LEU-428 AND 475-ILE--ILE-478, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=25415977; DOI=10.1105/tpc.114.131300;
RA Tomanov K., Zeschmann A., Hermkes R., Eifler K., Ziba I., Grieco M.,
RA Novatchkova M., Hofmann K., Hesse H., Bachmair A.;
RT "Arabidopsis PIAL1 and 2 promote SUMO chain formation as E4-type SUMO
RT ligases and are involved in stress responses and sulfur metabolism.";
RL Plant Cell 26:4547-4560(2014).
CC -!- FUNCTION: E4-type SUMO ligase that promotes SUMO chain formation in a
CC SCE1-dependent manner and thus contributes to a pathway for proteolytic
CC removal of sumoylation substrates. Involved in stress responses and
CC sulfur metabolism. {ECO:0000269|PubMed:25415977}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000269|PubMed:25415977}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flowers, and, at low
CC levels, in siliques and old leaves. {ECO:0000269|PubMed:25415977}.
CC -!- DISRUPTION PHENOTYPE: No obvious growth difference under standard
CC greenhouse conditions. Altered sulfur metabolism. Reduced growth in
CC high osmotic pressure (mannitol) and in response to abscisic acid
CC (ABA), but enhanced growth and fitness in high salt (NaCl) condition.
CC Abnormal steady state levels of SUMO conjugates in various conditions.
CC {ECO:0000269|PubMed:25415977}.
CC -!- SIMILARITY: Belongs to the PIAL protein ligase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB11464.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB005233; BAB11464.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94694.1; -; Genomic_DNA.
DR EMBL; AK229237; BAF01103.1; -; mRNA.
DR RefSeq; NP_198973.3; NM_123522.4.
DR AlphaFoldDB; F4JYG0; -.
DR SMR; F4JYG0; -.
DR IntAct; F4JYG0; 6.
DR STRING; 3702.AT5G41580.1; -.
DR PaxDb; F4JYG0; -.
DR PRIDE; F4JYG0; -.
DR ProteomicsDB; 236790; -.
DR EnsemblPlants; AT5G41580.1; AT5G41580.1; AT5G41580.
DR GeneID; 834160; -.
DR Gramene; AT5G41580.1; AT5G41580.1; AT5G41580.
DR KEGG; ath:AT5G41580; -.
DR Araport; AT5G41580; -.
DR TAIR; locus:2160417; AT5G41580.
DR eggNOG; KOG2169; Eukaryota.
DR HOGENOM; CLU_016114_0_0_1; -.
DR InParanoid; F4JYG0; -.
DR OMA; QFSQVHA; -.
DR OrthoDB; 241422at2759; -.
DR UniPathway; UPA00886; -.
DR PRO; PR:F4JYG0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JYG0; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0019789; F:SUMO transferase activity; TAS:TAIR.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051176; P:positive regulation of sulfur metabolic process; IGI:TAIR.
DR GO; GO:0016925; P:protein sumoylation; IDA:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IMP:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IMP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IMP:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02891; zf-MIZ; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW Ligase; Metal-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..760
FT /note="E4 SUMO-protein ligase PIAL2"
FT /id="PRO_0000434952"
FT ZN_FING 298..379
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT REGION 440..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 329
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 352
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT MUTAGEN 329
FT /note="C->A: Slight reduction of SUMO ligase activity; when
FT associated with A-355. Complete loss of activity; when
FT associated with A-355 and 425-A--A-428."
FT /evidence="ECO:0000269|PubMed:25415977"
FT MUTAGEN 355
FT /note="C->A: Slight reduction of SUMO ligase activity; when
FT associated with A-329. Complete loss of activity; when
FT associated with A-329 and 425-A--A-428."
FT /evidence="ECO:0000269|PubMed:25415977"
FT MUTAGEN 425..428
FT /note="VFDL->AAAA: Slight reduction of SUMO ligase
FT activity. Complete loss of activity; when associated with
FT A-329 and A-355."
FT /evidence="ECO:0000269|PubMed:25415977"
FT MUTAGEN 475..478
FT /note="IFDI->AAAA: Slight reduction of SUMO ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:25415977"
FT CONFLICT 441
FT /note="D -> G (in Ref. 3; BAF01103)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="S -> P (in Ref. 3; BAF01103)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 760 AA; 83109 MW; 75EA8A7CB3587E3E CRC64;
MSTAAAARPV AGTGLREKTA ASLVNSFRLA SVTQRLRYHI QDGAKVDPKE FQICCISFAK
GIDFAIANND IPKKVEEFPW LLKQLCRHGT DVYTKTALMV LMISVKHACH LGWFSDSESQ
ELIALADEIR TCFGSSGSTS PGIKSPGSTF SQIMERFYPF VKLGHVLVSF EVKAGYTMLA
HDFYISKNMP HSLQEKIRLF VAQTDNIDTS ACISNPPEVS FLLNGKGVEK RVNIAMDTGP
QLPTNVTAQL KYGTNLLQVM GNFKGNYIII IAFTGLVVPP EKPVLKDYLQ SGVIEASPDS
DIIEGPSRVS LSCPISRKRI KLPVKGQLCK HLQCFDFSNY VHINMRNPTW RCPHCNQPVC
YPDIRLDQNM AKILKDVEHN AADVIIDAGG TWKVTKNTGE TPEPVREIIH DLEDPMSLLN
SGPVVFDLTG DDDAELEVFG DNKVEDRKPC MSDAQGQSNN NNTNKHPSND DYSSIFDISD
VIALDPEILS ALGNTAPQPH QASNTGTGQQ YSNLSQIPMS IDPMPVPVPF SQTPSPRDRP
ATTSTVFTIP NPSPQYSQVH ASPVTPTGTY LGRTTSPRWN QTYQSQAPPM TTPYTSRKVS
VPVTSQSPAN VSSFVQSQHV PRVLSQPNNY GVRGLTSSHA STSRQHPSGP TVQSVSRLSD
LVDVDLTVPD TSNWRPRMRG SLVPGSHSTA LDHMIIRPSQ QSQTSTRLNS SQPVQTPSVQ
TSQAQSPFTT AAYRTETVLG NRNHPVPAPP GIVRPTGPTS
