KCS20_ORYSJ
ID KCS20_ORYSJ Reviewed; 523 AA.
AC Q7XEM4; Q0IXP5;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Probable 3-ketoacyl-CoA synthase 20 {ECO:0000305};
DE Short=OsKCS20 {ECO:0000303|Ref.5};
DE EC=2.3.1.199 {ECO:0000250|UniProtKB:Q38860};
DE AltName: Full=Protein SCREW FLAG LEAF 1 {ECO:0000303|Ref.5};
GN Name=KCS20 {ECO:0000303|Ref.5}; Synonyms=SFL1 {ECO:0000303|Ref.5};
GN OrderedLocusNames=Os10g0416200 {ECO:0000312|EMBL:BAT10854.1},
GN LOC_Os10g28060 {ECO:0000312|EMBL:AAP53764.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ALA-406.
RX DOI=10.1007/s11105-017-1039-x;
RA Alamin M., Zeng D.D., Qin R., Sultana M.H., Jin X.L., Shi C.H.;
RT "Characterization and fine mapping of SFL1, a gene controlling screw flag
RT leaf in rice.";
RL Plant Mol. Biol. Rep. 35:491-503(2017).
CC -!- FUNCTION: Contributes to fatty acids elongation (By similarity). Plays
CC a role in controlling leaf anatomy and plant architecture (Ref.5).
CC {ECO:0000250|UniProtKB:Q38860, ECO:0000269|Ref.5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very-long-chain acyl-CoA + H(+) + malonyl-CoA = a very-long-
CC chain 3-oxoacyl-CoA + CO2 + CoA; Xref=Rhea:RHEA:32727,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:90725, ChEBI:CHEBI:90736;
CC EC=2.3.1.199; Evidence={ECO:0000250|UniProtKB:Q38860};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32728;
CC Evidence={ECO:0000250|UniProtKB:Q38860};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaf sheaths (Ref.5). Expressed
CC in leaves, flag leaves and panicles (Ref.5). {ECO:0000269|Ref.5}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC synthases family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF26520.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DP000086; AAP53764.1; -; Genomic_DNA.
DR EMBL; AP008216; BAF26520.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014966; BAT10854.1; -; Genomic_DNA.
DR RefSeq; XP_015614625.1; XM_015759139.1.
DR AlphaFoldDB; Q7XEM4; -.
DR SMR; Q7XEM4; -.
DR STRING; 4530.OS10T0416200-01; -.
DR PaxDb; Q7XEM4; -.
DR PRIDE; Q7XEM4; -.
DR EnsemblPlants; Os10t0416200-01; Os10t0416200-01; Os10g0416200.
DR GeneID; 4348632; -.
DR Gramene; Os10t0416200-01; Os10t0416200-01; Os10g0416200.
DR KEGG; osa:4348632; -.
DR eggNOG; ENOG502QPKZ; Eukaryota.
DR HOGENOM; CLU_013238_5_1_1; -.
DR OrthoDB; 801187at2759; -.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0102756; F:very-long-chain 3-ketoacyl-CoA synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.47.10; -; 1.
DR InterPro; IPR012392; 3-ktacl-CoA_syn.
DR InterPro; IPR013747; ACP_syn_III_C.
DR InterPro; IPR013601; FAE1_typ3_polyketide_synth.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR31561; PTHR31561; 1.
DR Pfam; PF08541; ACP_syn_III_C; 1.
DR Pfam; PF08392; FAE1_CUT1_RppA; 1.
DR PIRSF; PIRSF036417; 3-ktacl-CoA_syn; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
PE 1: Evidence at protein level;
KW Acyltransferase; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..523
FT /note="Probable 3-ketoacyl-CoA synthase 20"
FT /id="PRO_0000448358"
FT TRANSMEM 31..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 93..382
FT /note="FAE"
FT /evidence="ECO:0000255"
FT ACT_SITE 237
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 317
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 401
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 405
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT ACT_SITE 438
FT /evidence="ECO:0000250|UniProtKB:Q38860"
FT MUTAGEN 406
FT /note="A->V: In sfl1; screw flag leaf phenotype due to
FT increased bulliform cell number and size, reduced plant
FT height, flag leaf length and width, panicle length, and
FT grain width."
FT /evidence="ECO:0000269|Ref.5"
SQ SEQUENCE 523 AA; 56868 MW; 013BF2C209DC96E7 CRC64;
MDRELVRTVK LATKNHAGVL FRRAVRHLPH IVAVTALVAA APRLSTLLAA AAAGGSTMRW
ARALWSDLAG ELGPSAPALA VACWAAALAA YTYAASRPRP VYLIDLAGYK APREHEASRA
KTIAHFGRCG RFSGESMAFQ KRMLERSGLG EATHFPTSLI SLPVDMCLRT AREESHAVIF
GVVDEVLRKS GVAAADVGVL IFNSSLLSPT PSFTSLIVNR YGMRPGVVSH NLSGMGCSAG
IIAIDLAKRL LQVHENTYAL VVSTENITLN AYMGNNRPML VTNTLFRVGG AAILLSNRAA
DRRGRAKYQL IHTVRTHRGA HDQSFGCVTQ EEDDAGEVGV SLSKELMVVA GEALKTNITT
LGPLVLPISE QLRFLATVVL KRVFRADVKA YLPDFKLALD HFCIHAGGRG VLDELEKSLK
LSPWDMEPSR MTLYRFGNTS SSSLWYELAY CEAKGRIKRG DRVWQIAFGS GFKCNSAVWR
ALRTVDAAGL DAGDNPWMKE VDMLPVDVPK VAPIDETSYQ IPN
