ID SPL2P_ARATH Reviewed; 383 AA.
AC Q9SYH3;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 162.
DE RecName: Full=E3 ubiquitin-protein ligase SPL2 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=RING-type E3 ubiquitin transferase SPL2 {ECO:0000305};
DE AltName: Full=SP1-like protein 2 {ECO:0000303|PubMed:23118188};
GN Name=SPL2 {ECO:0000303|PubMed:23118188};
GN OrderedLocusNames=At1g54150 {ECO:0000312|Araport:AT1G54150};
GN ORFNames=F15I1.25 {ECO:0000312|EMBL:AAD25789.1};
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 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}.
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DR EMBL; AC006577; AAD25789.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33055.1; -; Genomic_DNA.
DR EMBL; AY058075; AAL24183.1; -; mRNA.
DR EMBL; AY143876; AAN28815.1; -; mRNA.
DR PIR; F96582; F96582.
DR RefSeq; NP_564653.1; NM_104293.4.
DR AlphaFoldDB; Q9SYH3; -.
DR SMR; Q9SYH3; -.
DR STRING; 3702.Q9SYH3; -.
DR PaxDb; 3702-AT1G54150-1; -.
DR ProteomicsDB; 228396; -.
DR EnsemblPlants; AT1G54150.1; AT1G54150.1; AT1G54150.
DR GeneID; 841855; -.
DR Gramene; AT1G54150.1; AT1G54150.1; AT1G54150.
DR KEGG; ath:AT1G54150; -.
DR Araport; AT1G54150; -.
DR TAIR; AT1G54150; SPL2.
DR eggNOG; KOG1571; Eukaryota.
DR HOGENOM; CLU_050604_0_0_1; -.
DR InParanoid; Q9SYH3; -.
DR OMA; WNRWKEW; -.
DR OrthoDB; 5406876at2759; -.
DR PhylomeDB; Q9SYH3; -.
DR BRENDA; 2.3.2.27; 399.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9SYH3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SYH3; 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: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:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd23145; RING-HC_SPL2-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR022170; MUL1-like.
DR InterPro; IPR044247; SPL2-like.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR47355; E3 UBIQUITIN-PROTEIN LIGASE SPL2; 1.
DR PANTHER; PTHR47355:SF1; E3 UBIQUITIN-PROTEIN LIGASE SPL2; 1.
DR Pfam; PF12483; GIDE; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 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..383
FT /note="E3 ubiquitin-protein ligase SPL2"
FT /id="PRO_0000436710"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..269
FT /note="Chloroplast intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..383
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT ZN_FING 331..370
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 383 AA; 42697 MW; 68B8DD775D0B615F CRC64;
MSSPERALLN LLTDIALSFD GAILGLTLAV SAVGSALKYA STNAALKKIK DAPEVSISDL
RSLLPASEDK SETNDNRKSN DQRIVVVRGV VKPKISGDEG YKNNNVLISP ETGDKALIIQ
RTQTYVYSGW KRLFQSTGHR FMLERSLRKH GADFTRTVPF VIVGKDQQSN SSFVAVNMDG
SRQPLPLTTV YNRLQPINSS FLQAFLYPDY PVGLLDIEKI LPPGKDITAV GIYSFNNGVP
EIKSCQDLPY FLSEMTKDKM IEDLMEQTNF IFLGSVILGI VSVGILSYAA VRTWNKWKQW
NHQRELPQRP NDSVVDDEPE DADEIPDGEL CVICVSRRRV PAFIPCGHVV CCRRCASTVE
RELNPKCPVC LQSIRGSMRV YYS
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