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STAD6_ORYSJ
ID   STAD6_ORYSJ             Reviewed;         419 AA.
AC   Q0J7E4; A0A0P0XD46; Q6Z1J5;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Acyl-[acyl-carrier-protein] desaturase 6, chloroplastic;
DE            EC=1.14.19.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os08g0199400, LOC_Os08g09950; ORFNames=OSJNBb0094P23.29;
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=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   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [5]
RP   GENE FAMILY.
RX   PubMed=19522564; DOI=10.1094/mpmi-22-7-0820;
RA   Jiang C.J., Shimono M., Maeda S., Inoue H., Mori M., Hasegawa M.,
RA   Sugano S., Takatsuji H.;
RT   "Suppression of the rice fatty-acid desaturase gene OsSSI2 enhances
RT   resistance to blast and leaf blight diseases in rice.";
RL   Mol. Plant Microbe Interact. 22:820-829(2009).
CC   -!- FUNCTION: Introduces a cis double bond in the acyl chain of an acyl-
CC       [acyl-carrier protein]. {ECO:0000305}.
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:P22337};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:P22337};
CC   -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P22337}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the fatty acid desaturase type 2 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD03577.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AP005416; BAD03577.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AP008214; BAF23121.1; -; Genomic_DNA.
DR   EMBL; AP014964; BAT04247.1; -; Genomic_DNA.
DR   EMBL; AK105852; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015650772.1; XM_015795286.1.
DR   AlphaFoldDB; Q0J7E4; -.
DR   SMR; Q0J7E4; -.
DR   STRING; 4530.OS08T0199400-01; -.
DR   PaxDb; Q0J7E4; -.
DR   PRIDE; Q0J7E4; -.
DR   EnsemblPlants; Os08t0199400-01; Os08t0199400-01; Os08g0199400.
DR   GeneID; 4344895; -.
DR   Gramene; Os08t0199400-01; Os08t0199400-01; Os08g0199400.
DR   KEGG; osa:4344895; -.
DR   eggNOG; ENOG502QRJK; Eukaryota.
DR   HOGENOM; CLU_034505_1_0_1; -.
DR   InParanoid; Q0J7E4; -.
DR   OMA; FDMREVE; -.
DR   OrthoDB; 608188at2759; -.
DR   UniPathway; UPA00199; -.
DR   Proteomes; UP000000763; Chromosome 8.
DR   Proteomes; UP000059680; Chromosome 8.
DR   Genevisible; Q0J7E4; OS.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0045300; F:acyl-[acyl-carrier-protein] desaturase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR   CDD; cd01050; Acyl_ACP_Desat; 1.
DR   Gene3D; 1.10.620.20; -; 1.
DR   InterPro; IPR005067; Fatty_acid_desaturase-2.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR012348; RNR-like.
DR   PANTHER; PTHR31155; PTHR31155; 1.
DR   Pfam; PF03405; FA_desaturase_2; 1.
DR   PIRSF; PIRSF000346; Dlt9_acylACP_des; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism; Iron;
KW   Lipid biosynthesis; Lipid metabolism; Metal-binding; Oxidoreductase;
KW   Plastid; Reference proteome; Transit peptide.
FT   TRANSIT         1..54
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           55..419
FT                   /note="Acyl-[acyl-carrier-protein] desaturase 6,
FT                   chloroplastic"
FT                   /id="PRO_0000401434"
FT   BINDING         151
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         189
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         189
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         192
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         242
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         277
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         277
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   BINDING         280
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P22337"
FT   CONFLICT        64
FT                   /note="R -> W (in Ref. 4; AK105852)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   419 AA;  46101 MW;  238A68652D1A18D9 CRC64;
     MAATATMAMP LANRLRCKPN TNSSSPSRTL FGRRVTMISS SRWGSAVSGS AIMSAAADVA
     AAVRREEDEE MRSYLSPEKL EVLTQMEPWV EEHVLPLLKP VEAAWQPSDL LPDPAVLGGE
     GFHAACAELR ERAAGVPDLL LVCLVANMVT EEALPTYQSS LNRVRAVGDL TGADATAWAR
     WIRGWSAEEN RHGDVLNRYM YLSGRFDMAE VERAVHRLIR SGMAVDPPCS PYHAFVYTAF
     QERATAVAHG NTARLVGARG HGDAALARVC GTVAADEKRH EAAYTRIVSR LLEADPDAGV
     RAVARMLRRG VAMPTSPISD GRRDDLYACV VSLAEQAGTY TVSDYCSIVE HLVREWRVEE
     LAAGLSGEGR RARDYVCELP QKIRRMKEKA HERAVKAQKK PISIPINWIF DRHVSVMLP
 
 
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