GC1_ARATH
ID GC1_ARATH Reviewed; 347 AA.
AC Q9SJU9; Q9FEG0;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Epimerase family protein SDR39U1 homolog, chloroplastic {ECO:0000305};
DE EC=1.1.1.-;
DE AltName: Full=Protein GIANT CHLOROPLAST 1 {ECO:0000303|PubMed:15120068};
DE AltName: Full=Protein SulA homolog {ECO:0000303|PubMed:15208387};
DE Short=AtSulA {ECO:0000303|PubMed:15208387};
DE Flags: Precursor;
GN Name=GC1 {ECO:0000303|PubMed:15120068};
GN Synonyms=SULA {ECO:0000303|PubMed:15208387};
GN OrderedLocusNames=At2g21280 {ECO:0000312|Araport:AT2G21280};
GN ORFNames=F3K23;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Wassilewskija {ECO:0000305};
RX PubMed=15208387; DOI=10.1105/tpc.022335;
RA Raynaud C., Cassier-Chauvat C., Perennes C., Bergounioux C.;
RT "An Arabidopsis homolog of the bacterial cell division inhibitor SulA is
RT involved in plastid division.";
RL Plant Cell 16:1801-1811(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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).
RN [4]
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 [5]
RP FUNCTION, HOMODIMERIZATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15120068; DOI=10.1016/j.cub.2004.04.031;
RA Maple J., Fujiwara M.T., Kitahata N., Lawson T., Baker N.R., Yoshida S.,
RA Moller S.G.;
RT "GIANT CHLOROPLAST 1 is essential for correct plastid division in
RT Arabidopsis.";
RL Curr. Biol. 14:776-781(2004).
CC -!- FUNCTION: Putative NADP-dependent oxidoreductase that acts as positive
CC regulator of chloroplast division. May play a role at an early stage of
CC the division process. {ECO:0000269|PubMed:15120068}.
CC -!- SUBUNIT: Can form homodimers. {ECO:0000269|PubMed:15120068}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane; Peripheral
CC membrane protein; Stromal side {ECO:0000269|PubMed:15120068}. Plastid,
CC chloroplast {ECO:0000269|PubMed:15208387}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems and flower buds.
CC {ECO:0000269|PubMed:15120068, ECO:0000269|PubMed:15208387}.
CC -!- MISCELLANEOUS: Plants silencing GC1 show greatly enlarged chloroplasts
CC containing densely packed thylakoid membranes in mesophyll cells and
CC leaves with decreased rates of CO(2) assimilation.
CC {ECO:0000269|PubMed:15120068}.
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DR EMBL; AJ516948; CAD56855.1; -; mRNA.
DR EMBL; AC006841; AAD23676.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07155.1; -; Genomic_DNA.
DR EMBL; AF324701; AAG40052.1; -; mRNA.
DR EMBL; AF326895; AAG41477.1; -; mRNA.
DR EMBL; AF339713; AAK00395.1; -; mRNA.
DR EMBL; BT000757; AAN31897.1; -; mRNA.
DR PIR; D84599; D84599.
DR RefSeq; NP_565505.1; NM_127700.4.
DR AlphaFoldDB; Q9SJU9; -.
DR SMR; Q9SJU9; -.
DR BioGRID; 2020; 2.
DR IntAct; Q9SJU9; 1.
DR STRING; 3702.AT2G21280.1; -.
DR iPTMnet; Q9SJU9; -.
DR PaxDb; Q9SJU9; -.
DR PRIDE; Q9SJU9; -.
DR ProteomicsDB; 222228; -.
DR EnsemblPlants; AT2G21280.1; AT2G21280.1; AT2G21280.
DR GeneID; 816667; -.
DR Gramene; AT2G21280.1; AT2G21280.1; AT2G21280.
DR KEGG; ath:AT2G21280; -.
DR Araport; AT2G21280; -.
DR TAIR; locus:2050090; AT2G21280.
DR eggNOG; KOG3019; Eukaryota.
DR HOGENOM; CLU_047373_0_3_1; -.
DR InParanoid; Q9SJU9; -.
DR OMA; YMPWIHI; -.
DR PhylomeDB; Q9SJU9; -.
DR PRO; PR:Q9SJU9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJU9; baseline and differential.
DR Genevisible; Q9SJU9; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009536; C:plastid; IDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0010020; P:chloroplast fission; IMP:TAIR.
DR InterPro; IPR013549; DUF1731.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR010099; SDR39U1.
DR Pfam; PF08338; DUF1731; 1.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01777; yfcH; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Membrane; NADP; Oxidoreductase; Plastid;
KW Plastid inner membrane; Reference proteome; Transit peptide.
FT TRANSIT 1..37
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 38..347
FT /note="Epimerase family protein SDR39U1 homolog,
FT chloroplastic"
FT /id="PRO_5001126579"
FT BINDING 54..57
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9NRG7"
FT BINDING 76..77
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9NRG7"
FT BINDING 115..119
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9NRG7"
FT BINDING 136
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9NRG7"
SQ SEQUENCE 347 AA; 37746 MW; 0F069BFEE6D947C8 CRC64;
MELLCSPTSL SSSFALSSAL LVPRSFSMPG TRRFMVLCSS QKESQMTVSV TGATGFIGRR
LVQRLRADNH AIRVLTRSKS KAEQIFPAKD FPGIVIAEES EWKNCVQGST AVVNLAGLPI
STRWSPEIKK EIKGSRIRVT SKVVDLINNS PAEARPTVLV SATAVGYYGT SETGVFDENS
PSGKDYLAEV CREWEGTALK ANKDVRVALI RIGVVLGKDG GALAMMIPFF QMFAGGPLGS
GQQWFSWIHV DDLVNLIYEA LTNPSYKGVI NGTAPNPVRL GEMCQQLGSV LSRPSWLPVP
DFALKALLGE GATVVLEGQK VLPVRAKELG FEFKYKYVKD ALRAIMQ
