SCO2_ARATH
ID SCO2_ARATH Reviewed; 187 AA.
AC Q93YN0;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Protein disulfide-isomerase SCO2;
DE EC=5.3.4.1;
DE AltName: Full=Protein SNOWY COTYLEDON 2;
DE Flags: Precursor;
GN Name=SCO2; Synonyms=CYO1; OrderedLocusNames=At3g19220; ORFNames=MVI11.22;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Wassilewskija;
RX PubMed=17921316; DOI=10.1105/tpc.107.051714;
RA Shimada H., Mochizuki M., Ogura K., Froehlich J.E., Osteryoung K.W.,
RA Shirano Y., Shibata D., Masuda S., Mori K., Takamiya K.;
RT "Arabidopsis cotyledon-specific chloroplast biogenesis factor CYO1 is a
RT protein disulfide isomerase.";
RL Plant Cell 19:3157-3169(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=18209955; DOI=10.1007/s11103-008-9291-y;
RA Albrecht V., Ingenfeld A., Apel K.;
RT "Snowy cotyledon 2: the identification of a zinc finger domain protein
RT essential for chloroplast development in cotyledons but not in true
RT leaves.";
RL Plant Mol. Biol. 66:599-608(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
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 [5]
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 [6]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH LHCB1 PROTEINS.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=22040291; DOI=10.1111/j.1365-313x.2011.04833.x;
RA Tanz S., Kilian J., Johnsson C., Apel K., Small I., Harter K., Wanke D.,
RA Pogson B., Albrecht V.;
RT "The SCO2 protein disulphide isomerase is required for thylakoid biogenesis
RT and interacts with LCHB1 chlorophyl a/b binding proteins which affects
RT chlorophyll biosynthesis in Arabidopsis seedlings.";
RL Plant J. 69:743-754(2012).
CC -!- FUNCTION: Protein disulfide-isomerase involved in chloroplast
CC development in cotyledons. Involved in the process of vesicle-derived
CC thylakoid formation, probably at the level of the integration and
CC folding of LHCB proteins at the initial location of integration. Acts
CC only in germinating seeds after dormancy, during the transition from
CC heterotrophic to autotrophic growth. {ECO:0000269|PubMed:17921316,
CC ECO:0000269|PubMed:18209955, ECO:0000269|PubMed:22040291}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000269|PubMed:17921316};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:17921316};
CC -!- SUBUNIT: Homomer. Interacts with LHCB1 proteins, but is not part of the
CC signal recognition particle protein targeting pathway.
CC {ECO:0000269|PubMed:22040291}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:17921316, ECO:0000269|PubMed:18209955}; Peripheral
CC membrane protein {ECO:0000269|PubMed:17921316,
CC ECO:0000269|PubMed:18209955}. Note=Associates with multiple thylakoid
CC complexes.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette and cauline leaves,
CC stems, inflorescences and young siliques of light-grown plants, but not
CC in etiolated seedlings or in senescing tissues.
CC {ECO:0000269|PubMed:18209955}.
CC -!- DEVELOPMENTAL STAGE: Very low expression in etiolated seedlings, but
CC gradual increase upon illumination with a maximum after 6 hours.
CC Expressed mainly in young plants grown under light conditions.
CC {ECO:0000269|PubMed:17921316}.
CC -!- DISRUPTION PHENOTYPE: Albino cotyledons but normal green true leaves.
CC {ECO:0000269|PubMed:17921316, ECO:0000269|PubMed:18209955}.
CC -!- MISCELLANEOUS: Its sequence is related to the DnaJ family but lacks the
CC J domain. The CR-type-like region is similar to CR-type zinc-fingers.
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DR EMBL; EU402409; ABY91282.1; -; mRNA.
DR EMBL; AP000419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002686; AEE76210.1; -; Genomic_DNA.
DR EMBL; AY059925; AAL24407.1; -; mRNA.
DR EMBL; AY081606; AAM10168.1; -; mRNA.
DR RefSeq; NP_566627.1; NM_112809.4.
DR AlphaFoldDB; Q93YN0; -.
DR BioGRID; 6789; 6.
DR IntAct; Q93YN0; 1.
DR STRING; 3702.AT3G19220.1; -.
DR PaxDb; Q93YN0; -.
DR PRIDE; Q93YN0; -.
DR ProteomicsDB; 232816; -.
DR EnsemblPlants; AT3G19220.1; AT3G19220.1; AT3G19220.
DR GeneID; 821456; -.
DR Gramene; AT3G19220.1; AT3G19220.1; AT3G19220.
DR KEGG; ath:AT3G19220; -.
DR Araport; AT3G19220; -.
DR TAIR; locus:2094093; AT3G19220.
DR eggNOG; ENOG502RZYJ; Eukaryota.
DR HOGENOM; CLU_089799_1_0_1; -.
DR InParanoid; Q93YN0; -.
DR OMA; AGKWRKR; -.
DR OrthoDB; 1414371at2759; -.
DR PhylomeDB; Q93YN0; -.
DR BRENDA; 5.3.4.1; 399.
DR PRO; PR:Q93YN0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q93YN0; baseline and differential.
DR Genevisible; Q93YN0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:TAIR.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR InterPro; IPR037477; SCO2.
DR PANTHER; PTHR36035; PTHR36035; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Isomerase; Membrane; Metal-binding; Plastid;
KW Reference proteome; Repeat; Thylakoid; Transit peptide; Zinc.
FT TRANSIT 1..30
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 31..187
FT /note="Protein disulfide-isomerase SCO2"
FT /id="PRO_0000415339"
FT REPEAT 135..142
FT /note="CXXCXGXG motif"
FT REPEAT 158..165
FT /note="CXXCXGXG motif"
FT REGION 41..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..175
FT /note="CR-type-like"
SQ SEQUENCE 187 AA; 20843 MW; FE2475458110A313 CRC64;
MFRLYPNCSL PSHRPLVFLP RLPSRSLRCR AAADIPLGDG IRLPREADST SDTARSRDVS
VAAGGNGEGA KWRKRRLLWS KSGESYLVDD GDALPLPMTY PDTSPVSPDV IDRRLQCDPV
VEDCREVVYE WTGKCRSCQG SGTVSYYKKR GKEVICKCIP CQGIGYVQKI TSRTDIEVME
DLDNEPS
