PIAL1_ARATH
ID PIAL1_ARATH Reviewed; 847 AA.
AC A0A0A7EPL0; F4HXS5; O04038;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 04-MAR-2015, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=E4 SUMO-protein ligase PIAL1 {ECO:0000303|PubMed:25415977};
DE EC=2.3.2.- {ECO:0000269|PubMed:25415977};
DE AltName: Full=Protein EMBRYO DEFECTIVE 3001;
DE AltName: Full=Protein INHIBITOR OF ACTIVATED STAT-LIKE 1 {ECO:0000303|PubMed:25415977};
GN Name=PIAL1 {ECO:0000303|PubMed:25415977};
GN Synonyms=EMB3001 {ECO:0000312|EMBL:AEE28366.1};
GN OrderedLocusNames=At1g08910 {ECO:0000312|Araport:AT1G08910};
GN ORFNames=F7G19.21 {ECO:0000312|EMBL:AAB70421.1};
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 [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP 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).
RN [2]
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 [3]
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: 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 (e.g.
CC osmotic, salt and abscisic acid ABA) and sulfur metabolism.
CC {ECO:0000269|PubMed:25415977}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC {ECO:0000269|PubMed:25415977}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0A0A7EPL0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A0A7EPL0-2; Sequence=VSP_057991;
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=AAB70421.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KP067953; AIY68679.1; -; mRNA.
DR EMBL; AC000106; AAB70421.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28366.1; -; Genomic_DNA.
DR PIR; H86220; H86220.
DR RefSeq; NP_172366.3; NM_100763.5. [A0A0A7EPL0-2]
DR AlphaFoldDB; A0A0A7EPL0; -.
DR SMR; A0A0A7EPL0; -.
DR STRING; 3702.AT1G08910.1; -.
DR PaxDb; A0A0A7EPL0; -.
DR PeptideAtlas; A0A0A7EPL0; -.
DR ProteomicsDB; 236752; -. [A0A0A7EPL0-1]
DR EnsemblPlants; AT1G08910.1; AT1G08910.1; AT1G08910. [A0A0A7EPL0-2]
DR GeneID; 837412; -.
DR Gramene; AT1G08910.1; AT1G08910.1; AT1G08910. [A0A0A7EPL0-2]
DR KEGG; ath:AT1G08910; -.
DR Araport; AT1G08910; -.
DR TAIR; locus:2035999; AT1G08910.
DR eggNOG; KOG2169; Eukaryota.
DR OMA; DQRPMPS; -.
DR OrthoDB; 1205949at2759; -.
DR UniPathway; UPA00886; -.
DR PRO; PR:A0A0A7EPL0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; A0A0A7EPL0; 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:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051176; P:positive regulation of sulfur metabolic process; IGI:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
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 2: Evidence at transcript level;
KW Alternative splicing; Ligase; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..847
FT /note="E4 SUMO-protein ligase PIAL1"
FT /id="PRO_0000434951"
FT REPEAT 569..591
FT /note="1"
FT /evidence="ECO:0000303|PubMed:25415977"
FT REPEAT 592..614
FT /note="2"
FT /evidence="ECO:0000303|PubMed:25415977"
FT REPEAT 615..637
FT /note="3"
FT /evidence="ECO:0000303|PubMed:25415977"
FT REPEAT 638..659
FT /note="4"
FT /evidence="ECO:0000303|PubMed:25415977"
FT REPEAT 660..682
FT /note="5"
FT /evidence="ECO:0000303|PubMed:25415977"
FT REPEAT 683..705
FT /note="6"
FT /evidence="ECO:0000303|PubMed:25415977"
FT REPEAT 706..728
FT /note="7"
FT /evidence="ECO:0000303|PubMed:25415977"
FT ZN_FING 268..349
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT REGION 569..728
FT /note="7 X 23 AA approximate tandem repeats"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT VAR_SEQ 318..342
FT /note="PSWRCPHCNQSVCYTDIRVDQKLRK -> HHGAARI (in isoform 2)"
FT /id="VSP_057991"
SQ SEQUENCE 847 AA; 93475 MW; FF232EDE3000CCB1 CRC64;
MVIPATSRFG FRAEFNTKEF QASCISLANE IDAAIGRNEV PGNIQELALI LNNVCRRKCD
DYQTRAVVMA LMISVKSACQ LGWFPERETQ ELLAIIDLMW NGFSCPENVT SCVNSPVTLI
SQVIERFYPC VKLGHILVSF EAKPESKMMM KDFHISKKMP HSPKQKVGLF VVRTEDISRS
NCIVHPQGVS FLLNGKGIDK RVNISMESGP QLPTNVTALL NLGANLLQAI GCFGGSYLIA
IAFMDVIPLP NKPLLKDYVH PEVVGSNSDC DIIEGPSRIS LSCPISRTRI KLPVKGHVCK
HLQCFDFWNY VNMNTRRPSW RCPHCNQSVC YTDIRVDQKL RKILEEVGRN AADVVISADG
TWMVETENDE DVELVPETTH DHGDPNSFIN LGPTVKNPAR DENEMETSTQ VEEHNPCLSE
IQGPSNDTHR PASDYTMLNQ SHTSTNTLPQ LPRTLNAFDG QQFVNLPQVI NTRDSPASQA
LPMTFSPTPS PQDILATNAA NFGTSMPAAQ SSQFQGSHVT SLGNCEGRTS DLMARWNHIY
GRVQTQFPPA PLSHHHYSMQ NQSPSPAQQR PVPSYIAHPQ TFHVNYGENA DQRWMPSSIA
HPQTLPVNYG GNTNQRPIPS SIAHPQTLPV NYRGNTDHRS TPYSITHLQT LLNYGGNADQ
RPMPSSITNL QTLPATYGGY AHQRPMSSSI THPRTSPVNY GGTPDQRPMP SSITHPQTLP
VSYGGTTDQI LNPGGAMGQF SSREFMNLTP ANTENWRPQS RMRGSVAPGT GYDHMIIHPT
RPVHPQAQTP PAPLSTSYDG ADEIQAFIGH PSYPVSNNET QAGTSSLPVA EGLGYSGSFW
SMPPETW
