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SPL1P_ARATH
ID   SPL1P_ARATH             Reviewed;         338 AA.
AC   Q94HV7; Q9LQ59; Q9SLU0;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=E3 ubiquitin-protein ligase SPL1 {ECO:0000305};
DE            EC=2.3.2.27 {ECO:0000305};
DE   AltName: Full=DIAP1-like protein 2 {ECO:0000303|PubMed:20972793};
DE   AltName: Full=RING-type E3 ubiquitin transferase SPL1 {ECO:0000305};
DE   AltName: Full=SP1-like protein 1 {ECO:0000303|PubMed:23118188};
GN   Name=SPL1 {ECO:0000303|PubMed:23118188};
GN   Synonyms=DIAL2 {ECO:0000303|PubMed:20972793},
GN   ZCF61 {ECO:0000303|PubMed:10548732};
GN   OrderedLocusNames=At1g59560 {ECO:0000312|Araport:AT1G59560};
GN   ORFNames=T30E16.12 {ECO:0000312|EMBL:AAF79749.1},
GN   T4M14.12 {ECO:0000312|EMBL:AAK62796.1};
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 96-338.
RC   STRAIN=cv. Columbia;
RX   PubMed=10548732; DOI=10.1016/s0378-1119(99)00403-5;
RA   Kato A., Suzuki M., Kuwahara A., Ooe H., Higano-Inaba K., Komeda Y.;
RT   "Isolation and analysis of cDNA within a 300 kb Arabidopsis thaliana
RT   genomic region located around the 100 map unit of chromosome 1.";
RL   Gene 239:309-316(1999).
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   SUBCELLULAR LOCATION.
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).
CC   -!- FUNCTION: Possesses E3 ubiquitin-protein ligase activity.
CC       {ECO:0000250|UniProtKB:Q8L7N4}.
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.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC       {ECO:0000269|PubMed:23118188}; Multi-pass membrane protein
CC       {ECO:0000255}.
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   -!- 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. {ECO:0000269|PubMed:20972793}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF79749.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAA87953.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC009317; AAF79749.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC027036; AAK62796.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE33589.1; -; Genomic_DNA.
DR   EMBL; BT006461; AAP21269.1; -; mRNA.
DR   EMBL; AK228076; BAF00035.1; -; mRNA.
DR   EMBL; AB028228; BAA87953.1; ALT_INIT; mRNA.
DR   PIR; T52432; T52432.
DR   RefSeq; NP_564745.1; NM_104650.4.
DR   AlphaFoldDB; Q94HV7; -.
DR   SMR; Q94HV7; -.
DR   IntAct; Q94HV7; 21.
DR   STRING; 3702.AT1G59560.1; -.
DR   PaxDb; Q94HV7; -.
DR   PRIDE; Q94HV7; -.
DR   ProteomicsDB; 228367; -.
DR   EnsemblPlants; AT1G59560.1; AT1G59560.1; AT1G59560.
DR   GeneID; 842247; -.
DR   Gramene; AT1G59560.1; AT1G59560.1; AT1G59560.
DR   KEGG; ath:AT1G59560; -.
DR   Araport; AT1G59560; -.
DR   TAIR; locus:2202882; AT1G59560.
DR   eggNOG; KOG1571; Eukaryota.
DR   HOGENOM; CLU_050604_2_0_1; -.
DR   InParanoid; Q94HV7; -.
DR   OMA; APHYSID; -.
DR   OrthoDB; 926101at2759; -.
DR   PhylomeDB; Q94HV7; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q94HV7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q94HV7; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
DR   GO; GO:0009707; C:chloroplast outer membrane; IEA:UniProtKB-SubCell.
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   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   2: Evidence at transcript level;
KW   Chloroplast; Membrane; Metal-binding; Plastid; Plastid outer membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..338
FT                   /note="E3 ubiquitin-protein ligase SPL1"
FT                   /id="PRO_0000436709"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        22..223
FT                   /note="Chloroplast intermembrane"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        224..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        247..338
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   ZN_FING         291..326
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ   SEQUENCE   338 AA;  37729 MW;  BA5598FB4C0D296C CRC64;
     MIHLAGFTCC LGGVALYLLT RSTGRDIKSI TRVYQLKDLE QLVEVESKVV PLIIAVSGDV
     GSETPIKCEH SYVLGVFLKR TAEQQVLRRN WRFSWVRNST LMQPMTKEVP WYLDDGTGRV
     NVDVSQGELG LALTVGSDVF EKAEPVSLVQ GALGYLKGFK ILGVRHVERV VPIGTPLTVV
     GEAVRDGMGN VRIQKPEQGP FYVTYIPLDQ LISKLGDLSR RFKYASMGLT VLGVILISKP
     VIEYILKRIE DTLERRRRQF ALKRVVDAAA RRAKPVTGGG TSRDGDTPDL CVVCLDQKYN
     TAFVECGHMC CCTPCSLQLR TCPLCRERIQ QVLKIYRH
 
 
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