GENTAUR Molecular Products.

 KASC2_ARATH             Reviewed;         541 AA.
 Q9C9P4; Q8RXF5; Q945N5; Q9SSG8;
 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
 01-JUN-2001, sequence version 1.
 25-APR-2018, entry version 116.
 RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase II, chloroplastic;
          EC=2.3.1.41;
 AltName: Full=Beta-ketoacyl-acyl-carrier-protein synthase II;
          Short=AtKAS2;
          Short=Beta-ketoacyl-ACP synthetase 2;
 AltName: Full=Protein FATTY ACID BIOSYNTHESIS 1;
 Flags: Precursor;
 Name=KAS2; Synonyms=FAB1; OrderedLocusNames=At1g74960;
 ORFNames=F25A4.7, F9E10.19;
 Arabidopsis thaliana (Mouse-ear cress).
 Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
 Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
 Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
 Arabidopsis.
 NCBI_TaxID=3702;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF LEU-337.
 STRAIN=cv. Wassilewskija;
 PubMed=12148534; DOI=10.1046/j.1365-313X.2002.01253.x;
 Carlsson A.S., LaBrie S.T., Kinney A.J., von Wettstein-Knowles P.,
 Browse J.;
 "A KAS2 cDNA complements the phenotypes of the Arabidopsis fab1 mutant
 that differs in a single residue bordering the substrate binding
 pocket.";
 Plant J. 29:761-770(2002).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 STRAIN=cv. Columbia;
 PubMed=11130712; DOI=10.1038/35048500;
 Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
 White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
 Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
 Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
 Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
 Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
 Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
 Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
 Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
 Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
 Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
 Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
 Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
 Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
 Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
 Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
 "Sequence and analysis of chromosome 1 of the plant Arabidopsis
 thaliana.";
 Nature 408:816-820(2000).
 [3]
 GENOME REANNOTATION.
 STRAIN=cv. Columbia;
 PubMed=27862469; DOI=10.1111/tpj.13415;
 Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
 Town C.D.;
 "Araport11: a complete reannotation of the Arabidopsis thaliana
 reference genome.";
 Plant J. 89:789-804(2017).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 STRAIN=cv. Columbia;
 PubMed=14593172; DOI=10.1126/science.1088305;
 Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
 Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
 Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
 Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
 Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
 Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
 Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
 Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
 Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
 Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
 Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
 Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
 "Empirical analysis of transcriptional activity in the Arabidopsis
 genome.";
 Science 302:842-846(2003).
 [5]
 FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LEU-337.
 STRAIN=cv. Columbia;
 PubMed=12232312; DOI=10.1104/pp.106.1.143;
 Wu J., James D.W. Jr., Dooner H.K., Browse J.;
 "A Mutant of Arabidopsis Deficient in the Elongation of Palmitic
 Acid.";
 Plant Physiol. 106:143-150(1994).
 [6]
 FUNCTION, AND MUTAGENESIS OF LEU-337.
 STRAIN=cv. Columbia;
 PubMed=12242349; DOI=10.1105/tpc.7.1.17;
 Wu J., Browse J.;
 "Elevated levels of high-melting-point phosphatidylglycerols do not
 induce chilling sensitivity in an Arabidopsis mutant.";
 Plant Cell 7:17-27(1995).
 [7]
 FUNCTION, AND MUTAGENESIS OF LEU-337.
 STRAIN=cv. Columbia;
 PubMed=9046588; DOI=10.1104/pp.113.2.347;
 Wu J., Lightner J., Warwick N., Browse J.;
 "Low-temperature damage and subsequent recovery of fab1 mutant
 Arabidopsis exposed to 2 degrees C.";
 Plant Physiol. 113:347-356(1997).
 [8]
 FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF LEU-337.
 PubMed=17360594; DOI=10.1073/pnas.0611141104;
 Pidkowich M.S., Nguyen H.T., Heilmann I., Ischebeck T., Shanklin J.;
 "Modulating seed beta-ketoacyl-acyl carrier protein synthase II level
 converts the composition of a temperate seed oil to that of a palm-
 like tropical oil.";
 Proc. Natl. Acad. Sci. U.S.A. 104:4742-4747(2007).
 [9]
 FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
 STAGE.
 STRAIN=cv. Columbia;
 PubMed=18506098; DOI=10.1266/ggs.83.143;
 Hakozaki H., Park J.-I., Endo M., Takada Y., Kazama T., Takeda Y.,
 Suzuki G., Kawagishi-Kobayashi M., Watanabe M.;
 "Expression and developmental function of the 3-ketoacyl-ACP synthase2
 gene in Arabidopsis thaliana.";
 Genes Genet. Syst. 83:143-152(2008).
 [10]
 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE
 SCALE ANALYSIS].
 PubMed=18431481; DOI=10.1371/journal.pone.0001994;
 Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O.,
 Sun Q., van Wijk K.J.;
 "Sorting signals, N-terminal modifications and abundance of the
 chloroplast proteome.";
 PLoS ONE 3:E1994-E1994(2008).
 -!- FUNCTION: Essential protein that catalyzes the condensation
     reaction of fatty acid synthesis by the addition to an acyl
     acceptor of two carbons from malonyl-ACP. Specific for elongation
     from C-16 and C-16 to unsaturated C-18 fatty acids. Confers
     resistance to low temperatures by maintaining chloroplast
     membranes integrity. Involved in the regulation of fatty acids
     ratios during seed metabolism. Required for embryo development,
     especially at the transition from the globular to the heart stage.
     {ECO:0000269|PubMed:12148534, ECO:0000269|PubMed:12232312,
     ECO:0000269|PubMed:12242349, ECO:0000269|PubMed:17360594,
     ECO:0000269|PubMed:18506098, ECO:0000269|PubMed:9046588}.
 -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl-
     carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) +
     [acyl-carrier-protein]. {ECO:0000269|PubMed:12232312}.
 -!- SUBUNIT: Homodimer. {ECO:0000250}.
 -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
     {ECO:0000269|PubMed:18431481}.
 -!- TISSUE SPECIFICITY: Mostly expressed in siliques, and, to a lower
     extent, in leaves, stems, flower buds, and flowers.
     {ECO:0000269|PubMed:18506098}.
 -!- DEVELOPMENTAL STAGE: First observed during the transition from the
     late globular to the early heart embryo stages. Later observed
     during heart, tropedo, and cotyledonary embryo stages. In
     seedlings, observed in the shoot apex and stomatal guard cells. In
     adult plants, expressed in inflorescences. In flowers, strongly
     present in styles and pollen grains.
     {ECO:0000269|PubMed:18506098}.
 -!- DISRUPTION PHENOTYPE: Lethal when homozygous due to embryo
     abortion before the torpedo stage. Converts temperate oilseed
     composition (rich in unsaturated 18-carbon fatty acids) to that of
     a palm-like tropical oil (enriched in saturated 16-carbon fatty
     acids). {ECO:0000269|PubMed:17360594,
     ECO:0000269|PubMed:18506098}.
 -!- SIMILARITY: Belongs to the beta-ketoacyl-ACP synthases family.
     {ECO:0000305}.
 -!- SEQUENCE CAUTION:
     Sequence=AAD55280.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
     Sequence=AAL06498.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
     Sequence=AAL06498.1; Type=Frameshift; Positions=38, 328; Evidence={ECO:0000305};
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 EMBL; AF318307; AAK69603.1; -; mRNA.
 EMBL; AC008263; AAD55280.1; ALT_SEQ; Genomic_DNA.
 EMBL; AC013258; AAG51920.1; -; Genomic_DNA.
 EMBL; CP002684; AEE35655.1; -; Genomic_DNA.
 EMBL; CP002684; AEE35656.1; -; Genomic_DNA.
 EMBL; CP002684; AEE35657.1; -; Genomic_DNA.
 EMBL; AF412045; AAL06498.1; ALT_FRAME; mRNA.
 EMBL; AF419598; AAL31930.1; -; mRNA.
 EMBL; AY054196; AAL06857.1; -; mRNA.
 EMBL; AY081285; AAL91174.1; -; mRNA.
 EMBL; AY097344; AAM19860.1; -; mRNA.
 PIR; D96779; D96779.
 RefSeq; NP_001185400.1; NM_001198471.1.
 RefSeq; NP_565097.1; NM_106154.4.
 RefSeq; NP_849888.1; NM_179557.4.
 UniGene; At.26097; -.
 ProteinModelPortal; Q9C9P4; -.
 SMR; Q9C9P4; -.
 BioGrid; 29054; 1.
 STRING; 3702.AT1G74960.1; -.
 PaxDb; Q9C9P4; -.
 PRIDE; Q9C9P4; -.
 EnsemblPlants; AT1G74960.1; AT1G74960.1; AT1G74960.
 EnsemblPlants; AT1G74960.2; AT1G74960.2; AT1G74960.
 EnsemblPlants; AT1G74960.3; AT1G74960.3; AT1G74960.
 GeneID; 843835; -.
 Gramene; AT1G74960.1; AT1G74960.1; AT1G74960.
 Gramene; AT1G74960.2; AT1G74960.2; AT1G74960.
 Gramene; AT1G74960.3; AT1G74960.3; AT1G74960.
 KEGG; ath:AT1G74960; -.
 Araport; AT1G74960; -.
 TAIR; locus:2027252; AT1G74960.
 eggNOG; KOG1394; Eukaryota.
 eggNOG; COG0304; LUCA.
 HOGENOM; HOG000060166; -.
 InParanoid; Q9C9P4; -.
 KO; K09458; -.
 OMA; EACMNIV; -.
 OrthoDB; EOG093609PY; -.
 PhylomeDB; Q9C9P4; -.
 BioCyc; ARA:AT1G74960-MONOMER; -.
 BioCyc; ARA:GQT-1583-MONOMER; -.
 BioCyc; ARA:MONOMER-14118; -.
 BioCyc; MetaCyc:MONOMER-14118; -.
 BRENDA; 2.3.1.179; 399.
 PRO; PR:Q9C9P4; -.
 Proteomes; UP000006548; Chromosome 1.
 ExpressionAtlas; Q9C9P4; baseline and differential.
 Genevisible; Q9C9P4; AT.
 GO; GO:0009507; C:chloroplast; IDA:TAIR.
 GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
 GO; GO:0009536; C:plastid; ISS:TAIR.
 GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IDA:TAIR.
 GO; GO:0009631; P:cold acclimation; IMP:UniProtKB.
 GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:UniProtKB.
 GO; GO:0006633; P:fatty acid biosynthetic process; IDA:TAIR.
 GO; GO:0006636; P:unsaturated fatty acid biosynthetic process; TAS:TAIR.
 Gene3D; 3.40.47.10; -; 2.
 InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
 InterPro; IPR018201; Ketoacyl_synth_AS.
 InterPro; IPR014031; Ketoacyl_synth_C.
 InterPro; IPR014030; Ketoacyl_synth_N.
 InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
 InterPro; IPR016039; Thiolase-like.
 Pfam; PF00109; ketoacyl-synt; 1.
 Pfam; PF02801; Ketoacyl-synt_C; 1.
 SMART; SM00825; PKS_KS; 1.
 SUPFAM; SSF53901; SSF53901; 2.
 TIGRFAMs; TIGR03150; fabF; 1.
 PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
 1: Evidence at protein level;
 Acyltransferase; Chloroplast; Complete proteome;
 Developmental protein; Fatty acid biosynthesis; Fatty acid metabolism;
 Lipid biosynthesis; Lipid metabolism; Plastid; Reference proteome;
 Transferase; Transit peptide.
 TRANSIT       1    103       Chloroplast. {ECO:0000255}.
 CHAIN       104    541       3-oxoacyl-[acyl-carrier-protein] synthase
                              II, chloroplastic.
                              /FTId=PRO_0000406094.
 ACT_SITE    292    292       {ECO:0000255|PROSITE-ProRule:PRU10022}.
 MUTAGEN     337    337       L->F: In fab1; partial activity
                              deficience due to structural instability
                              and reduced substrate binding affinity,
                              resulting in increased levels of
                              saturated 16:0 but reduced levels of 18:0
                              fatty acids, particularly in
                              chloroplasts, and associated with damage
                              and death at continuous low temperature
                              (accompanied by chloroplast
                              degenerescence), but not after transient
                              chilling or freezing.
                              {ECO:0000269|PubMed:12148534,
                              ECO:0000269|PubMed:12232312,
                              ECO:0000269|PubMed:12242349,
                              ECO:0000269|PubMed:17360594,
                              ECO:0000269|PubMed:9046588}.
 CONFLICT    472    472       A -> V (in Ref. 4; AAL91174).
                              {ECO:0000305}.
 SEQUENCE   541 AA;  57600 MW;  CB4F87E7B0C82189 CRC64;
 MVGASSSYAS PLCTWFVAAC MSVSHGGGDS RQAVALQSGG RSRRRRQLSK CSVASGSASI
 QALVTSCLDF GPCTHYNNNN ALSSLFGSNS VSLNRNQRRL NRAASSGGAM AVMEMEKEAA
 VNKKPPTEQR RVVVTGMGVE TSLGHDPHTF YENLLQGNSG ISQIENFDCS EFPTRIAGEI
 KSFSTEGWVA PKLSKRMDKF MLYLLTAGKK ALADGGVTDE VMAEFDKTKC GVLIGSAMGG
 MKVFYDAIEA LRISYKKMNP FCVPFATTNM GSAMLAMDLG WMGPNYSIST ACATSNFCIL
 NSANHIIKGE ADVMLCGGSD AVIIPIGLGG FVACRALSQR NNDPTKASRP WDTNRDGFVM
 GEGAGVLLLE ELEHAKKRGA TIYAEFLGGS FTCDAYHMTE PHPDGAGVIL CIERALASAG
 ISKEQINYIN AHATSTHAGD IKEYQALAHC FGQNPELKVN STKSMIGHLL GAAGAVEAVA
 TVQAIRTGWV HPNINLENPD SGVDTKLLVG PKKERLDIKA ALSNSFGFGG HNSSIIFAPY
 K

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