SP1_ARATH
ID SP1_ARATH Reviewed; 343 AA.
AC Q8L7N4; Q9CAK2; Q9CAK3;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 158.
DE RecName: Full=E3 ubiquitin-protein ligase SP1 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=DIAP1-like protein 1 {ECO:0000303|PubMed:20972793};
DE AltName: Full=Protein SUPPRESSOR OF PPI1 LOCUS 1 {ECO:0000303|PubMed:23118188};
DE AltName: Full=RING-type E3 ubiquitin transferase SP1 {ECO:0000305};
GN Name=SP1 {ECO:0000303|PubMed:23118188};
GN Synonyms=DIAL1 {ECO:0000303|PubMed:20972793};
GN OrderedLocusNames=At1g63900/At1g63890 {ECO:0000312|Araport:AT1G63900};
GN ORFNames=T12P18.8/T12P18.9 {ECO:0000312|EMBL:AAG52446.1,
GN ECO:0000312|EMBL:AAG52461.1};
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 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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 229-343.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=15644464; DOI=10.1104/pp.104.052423;
RA Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT "Functional analysis of the RING-type ubiquitin ligase family of
RT Arabidopsis.";
RL Plant Physiol. 137:13-30(2005).
RN [6]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20972793; DOI=10.1007/s00299-010-0941-6;
RA Basnayake B.M., Li D., Zhang H., Li G., Virk N., Song F.;
RT "Arabidopsis DAL1 and DAL2, two RING finger proteins homologous to
RT Drosophila DIAP1, are involved in regulation of programmed cell death.";
RL Plant Cell Rep. 30:37-48(2011).
RN [7]
RP FUNCTION, INTERACTION WITH TOC33; TOC75-3 AND TOC159, SUBCELLULAR LOCATION,
RP DOMAIN, TOPOLOGY, AUTOUBIQUITINATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS
RP OF CYS-330.
RX PubMed=23118188; DOI=10.1126/science.1225053;
RA Ling Q., Huang W., Baldwin A., Jarvis P.;
RT "Chloroplast biogenesis is regulated by direct action of the ubiquitin-
RT proteasome system.";
RL Science 338:655-659(2012).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26387714; DOI=10.1016/j.cub.2015.08.015;
RA Ling Q., Jarvis P.;
RT "Regulation of chloroplast protein import by the ubiquitin E3 ligase SP1 is
RT important for stress tolerance in plants.";
RL Curr. Biol. 25:2527-2534(2015).
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in the regulation of
CC protein import in the chloroplast. Associates with TOC complexes and
CC mediates ubiquitination of TOC components, promoting their degradation
CC via the ubiquitin-proteasome system (UPS). Plays a role in the
CC reorganization of the TOC machinery. Involved in a mechanism that
CC regulates plastid biogenesis via UPS (PubMed:23118188). Promotes stress
CC tolerance by depleting the chloroplast protein import apparatus, which
CC limits photosystem assembly and the potential for reactive oxygen
CC species (ROS) formation (PubMed:26387714). May act as negative
CC regulator of programmed cell death (PCD) during biotic stress
CC (PubMed:20972793). {ECO:0000269|PubMed:20972793,
CC ECO:0000269|PubMed:23118188, ECO:0000269|PubMed:26387714}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Interacts with TOC33, TOC75-3 and TOC159.
CC {ECO:0000269|PubMed:23118188}.
CC -!- INTERACTION:
CC Q8L7N4; O81283: TOC159; NbExp=2; IntAct=EBI-6559199, EBI-639063;
CC Q8L7N4; O23680: TOC33; NbExp=2; IntAct=EBI-6559199, EBI-639377;
CC Q8L7N4; Q9STE8: TOC75-3; NbExp=2; IntAct=EBI-6559199, EBI-639078;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC {ECO:0000269|PubMed:23118188}; Multi-pass membrane protein
CC {ECO:0000255}.
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=Q8L7N4-1; Sequence=Displayed;
CC -!- INDUCTION: By infection with the bacterial pathogen Pseudomonas
CC syringae pv. tomato, and treatment with fumonisin B1, a mycotoxin
CC inducing apoptosis-like programmed cell death (PCD).
CC {ECO:0000269|PubMed:20972793}.
CC -!- DOMAIN: The zinc finger domain is required for E3 ligase activity.
CC {ECO:0000269|PubMed:23118188}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:23118188}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants show increased disease symptoms and cell
CC death after inoculation with an avirulent strain of Pseudomonas
CC syringae pv. tomato DC3000 (PubMed:20972793). Pale-green phenotype with
CC low survival rates during de-etiolation (PubMed:23118188).
CC Hypersensitivity to salt, osmotic, and oxidative stresses
CC (PubMed:26387714). {ECO:0000269|PubMed:20972793,
CC ECO:0000269|PubMed:23118188, ECO:0000269|PubMed:26387714}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52446.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At1g63890 and At1g63900.; Evidence={ECO:0000305};
CC Sequence=AAG52461.1; Type=Erroneous gene model prediction; Note=Was originally thought to correspond to two different genes At1g63890 and At1g63900.; Evidence={ECO:0000305};
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DR EMBL; AC010852; AAG52446.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC010852; AAG52461.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34164.1; -; Genomic_DNA.
DR EMBL; AY128352; AAM91555.1; -; mRNA.
DR EMBL; BT000008; AAN15327.1; -; mRNA.
DR EMBL; AK176213; BAD43976.1; -; mRNA.
DR EMBL; AK176755; BAD44518.1; -; mRNA.
DR EMBL; DQ059103; AAY57589.1; -; mRNA.
DR PIR; A96664; A96664.
DR PIR; B96664; B96664.
DR RefSeq; NP_176574.2; NM_105064.4. [Q8L7N4-1]
DR AlphaFoldDB; Q8L7N4; -.
DR SMR; Q8L7N4; -.
DR IntAct; Q8L7N4; 6.
DR STRING; 3702.AT1G63900.2; -.
DR ProteomicsDB; 245332; -. [Q8L7N4-1]
DR EnsemblPlants; AT1G63900.1; AT1G63900.1; AT1G63900. [Q8L7N4-1]
DR GeneID; 842693; -.
DR Gramene; AT1G63900.1; AT1G63900.1; AT1G63900. [Q8L7N4-1]
DR KEGG; ath:AT1G63900; -.
DR Araport; AT1G63900; -.
DR eggNOG; KOG1571; Eukaryota.
DR OMA; LKAAPQY; -.
DR OrthoDB; 926101at2759; -.
DR PhylomeDB; Q8L7N4; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q8L7N4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L7N4; baseline and differential.
DR GO; GO:0009707; C:chloroplast outer membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006996; P:organelle organization; IEA:InterPro.
DR GO; GO:1904215; P:regulation of protein import into chloroplast stroma; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR022170; MUL1-like.
DR InterPro; IPR044231; SP1/SPL1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47568; PTHR47568; 1.
DR Pfam; PF12483; GIDE; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Membrane; Metal-binding; Plastid;
KW Plastid outer membrane; Reference proteome; Stress response; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..343
FT /note="E3 ubiquitin-protein ligase SP1"
FT /id="PRO_0000436708"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..222
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305|PubMed:23118188"
FT TRANSMEM 223..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23118188"
FT ZN_FING 296..331
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MUTAGEN 330
FT /note="C->A: Loss of E3 ubiquitin-protein ligase activity;
FT loss of auto-ubiquitination."
FT /evidence="ECO:0000269|PubMed:23118188"
SQ SEQUENCE 343 AA; 37908 MW; 427B50E9BB3AC18B CRC64;
MIPWGGVTCC LSAAALYLLG RSSGRDAEVL ETVTRVNQLK ELAQLLELDS KILPFIVAVS
GRVGSETPIK CEHSGIRGVI VEETAEQHFL KHNETGSWVQ DSALMLSMSK EVPWFLDDGT
SRVHVMGARG ATGFALTVGS EVFEESGRSL VRGTLDYLQG LKMLGVKRIE RVLPTGIPLT
IVGEAVKDDI GEFRIQKPDR GPFYVSSKSL DQLISNLGKW SRLYKYASMG FTVLGVFLIT
KHVIDSVLER RRRRQLQKRV LDAAAKRAEL ESEGSNGTRE SISDSTKKED AVPDLCVICL
EQEYNAVFVP CGHMCCCTAC SSHLTSCPLC RRRIDLAVKT YRH
