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KCS10_ARATH
ID   KCS10_ARATH             Reviewed;         550 AA.
AC   Q570B4; O64846; Q9LDX6; Q9LLE3; Q9LLE4; Q9LLE5; Q9LLE6; Q9LLE7; Q9LLE8;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=3-ketoacyl-CoA synthase 10 {ECO:0000303|PubMed:18465198};
DE            Short=KCS-10 {ECO:0000303|PubMed:18465198};
DE            EC=2.3.1.199 {ECO:0000305};
DE   AltName: Full=Protein FIDDLEHEAD {ECO:0000303|PubMed:10559443};
DE   AltName: Full=Very long-chain fatty acid condensing enzyme 10 {ECO:0000303|PubMed:18465198};
DE            Short=VLCFA condensing enzyme 10 {ECO:0000303|PubMed:18465198};
GN   Name=FDH {ECO:0000303|PubMed:10559443};
GN   Synonyms=EL4, KCS10 {ECO:0000303|PubMed:18465198};
GN   OrderedLocusNames=At2g26250 {ECO:0000312|Araport:AT2G26250};
GN   ORFNames=T1D16.11 {ECO:0000312|EMBL:AAC14526.1};
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 [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE, TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=cv. Columbia;
RX   PubMed=10559443; DOI=10.2307/3871018;
RA   Yephremov A., Wisman E., Huijser P., Huijser C., Wellesen K., Saedler H.;
RT   "Characterization of the FIDDLEHEAD gene of Arabidopsis reveals a link
RT   between adhesion response and cell differentiation in the epidermis.";
RL   Plant Cell 11:2187-2201(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLY-256; GLU-497; GLY-514;
RP   346-SER--LEU-550; 353-GLU--LEU-550; 390-GLN--LEU-550 AND 509-TRP--LEU-550.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=10655527; DOI=10.1073/pnas.97.3.1311;
RA   Pruitt R.E., Vielle-Calzada J.-P., Ploense S.E., Grossniklaus U.,
RA   Lolle S.J.;
RT   "FIDDLEHEAD, a gene required to suppress epidermal cell interactions in
RT   Arabidopsis, encodes a putative lipid biosynthetic enzyme.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:1311-1316(2000).
RN   [3]
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   [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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 455-550.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION, AND MUTAGENESIS OF 346-SER--LEU-550.
RX   PubMed=1644226; DOI=10.1016/0012-1606(92)90145-7;
RA   Lolle S.J., Cheung A.Y., Sussex I.M.;
RT   "Fiddlehead: an Arabidopsis mutant constitutively expressing an organ
RT   fusion program that involves interactions between epidermal cells.";
RL   Dev. Biol. 152:383-392(1992).
RN   [8]
RP   FUNCTION, AND MUTAGENESIS OF 346-SER--LEU-550.
RX   PubMed=8416837; DOI=10.1006/dbio.1993.1022;
RA   Lolle S.J., Cheung A.Y.;
RT   "Promiscuous germination and growth of wildtype pollen from Arabidopsis and
RT   related species on the shoot of the Arabidopsis mutant, fiddlehead.";
RL   Dev. Biol. 155:250-258(1993).
RN   [9]
RP   FUNCTION.
RX   PubMed=9299123; DOI=10.1006/dbio.1997.8671;
RA   Lolle S.J., Berlyn G.P., Engstrom E.M., Krolikowski K.A., Reiter W.-D.,
RA   Pruitt R.E.;
RT   "Developmental regulation of cell interactions in the Arabidopsis
RT   fiddlehead-1 mutant: a role for the epidermal cell wall and cuticle.";
RL   Dev. Biol. 189:311-321(1997).
RN   [10]
RP   FUNCTION, AND MUTAGENESIS OF GLY-256; GLU-497; GLY-514; 346-SER--LEU-550;
RP   390-GLN--LEU-550 AND 509-TRP--LEU-550.
RX   PubMed=9611177; DOI=10.1093/genetics/149.2.607;
RA   Lolle S.J., Hsu W., Pruitt R.E.;
RT   "Genetic analysis of organ fusion in Arabidopsis thaliana.";
RL   Genetics 149:607-619(1998).
RN   [11]
RP   INDUCTION, AND GENE FAMILY.
RX   PubMed=12916765; DOI=10.1002/ps.714;
RA   Lechelt-Kunze C., Meissner R.C., Drewes M., Tietjen K.;
RT   "Flufenacet herbicide treatment phenocopies the fiddlehead mutant in
RT   Arabidopsis thaliana.";
RL   Pest Manag. Sci. 59:847-856(2003).
RN   [12]
RP   GENE FAMILY, NOMENCLATURE, 3D-STRUCTURE MODELING, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=18465198; DOI=10.1007/s11103-008-9339-z;
RA   Joubes J., Raffaele S., Bourdenx B., Garcia C., Laroche-Traineau J.,
RA   Moreau P., Domergue F., Lessire R.;
RT   "The VLCFA elongase gene family in Arabidopsis thaliana: phylogenetic
RT   analysis, 3D modelling and expression profiling.";
RL   Plant Mol. Biol. 67:547-566(2008).
CC   -!- FUNCTION: Contributes to cuticular wax and suberin biosynthesis.
CC       Prevents the postgenital fusion of epiderm cells in organs in contact,
CC       as well as ectopic pollen hydration and germination. Required during
CC       ovules formation. May regulate an epidermis-specific developmental
CC       program during gynoecial ontogeny. {ECO:0000269|PubMed:10559443,
CC       ECO:0000269|PubMed:10655527, ECO:0000269|PubMed:1644226,
CC       ECO:0000269|PubMed:8416837, ECO:0000269|PubMed:9299123,
CC       ECO:0000269|PubMed:9611177}.
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:0000305};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:18465198}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in epidermal cells of floral and
CC       vegetative meristems and, to a lower extent, of leaves and coleoptiles,
CC       especially in young tissues. Also present in trichomes and phloem
CC       (PubMed:10559443, PubMed:10655527). Expressed in siliques, seedlings,
CC       flowers and leaves (PubMed:18465198). {ECO:0000269|PubMed:10559443,
CC       ECO:0000269|PubMed:10655527, ECO:0000269|PubMed:18465198}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in prefusion carpel abaxial and adaxial
CC       epidermis. Accumulates in ovule primordia, but restricted to chalaza in
CC       mature ovules. Also present in cells of stigmatic papillae, at the
CC       margins of ovules, and around the embryo sac.
CC       {ECO:0000269|PubMed:10559443, ECO:0000269|PubMed:10655527}.
CC   -!- INDUCTION: Repressed by herbicides such as flufenacet and benfuresate
CC       (PubMed:12916765). Down-regulated by darkness and low temperature, and
CC       up-regulated by salt and osmotic stress (PubMed:18465198).
CC       {ECO:0000269|PubMed:12916765, ECO:0000269|PubMed:18465198}.
CC   -!- DISRUPTION PHENOTYPE: In additions to several malformations due to
CC       organ fusion, plants lacking FDH demonstrate an enhanced cell wall
CC       permeability, reduced trichome formation, and are female sterile.
CC       {ECO:0000269|PubMed:10559443}.
CC   -!- MISCELLANEOUS: Called 'FIDDLEHEAD' because of the shape of mutants, in
CC       which adhering floral buds cause curling of inflorescence, resulting in
CC       structures reminiscent of fern fiddlehead.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF73974.1; Type=Erroneous gene model prediction;
CC       Sequence=AAF73975.1; Type=Erroneous gene model prediction;
CC       Sequence=AAF73977.1; Type=Erroneous gene model prediction;
CC       Sequence=AAF73978.1; Type=Erroneous gene model prediction;
CC       Sequence=AAF73981.1; Type=Erroneous gene model prediction;
CC       Sequence=BAD94049.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ010713; CAA09311.1; -; Genomic_DNA.
DR   EMBL; AH009409; AAF73973.1; -; Genomic_DNA.
DR   EMBL; AH009410; AAF73974.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AH009411; AAF73975.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AH009412; AAF73976.1; -; Genomic_DNA.
DR   EMBL; AH009413; AAF73977.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AH009414; AAF73978.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AH009415; AAF73979.1; -; Genomic_DNA.
DR   EMBL; AH009416; AAF73980.1; -; Genomic_DNA.
DR   EMBL; AH009417; AAF73981.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC004484; AAC14526.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07813.1; -; Genomic_DNA.
DR   EMBL; AY039563; AAK62618.1; -; mRNA.
DR   EMBL; AY149961; AAN31115.1; -; mRNA.
DR   EMBL; AF337910; AAG60062.1; -; mRNA.
DR   EMBL; BT002360; AAN86193.1; -; mRNA.
DR   EMBL; AK220796; BAD94049.1; ALT_INIT; mRNA.
DR   PIR; B84658; B84658.
DR   RefSeq; NP_180193.1; NM_128182.4.
DR   AlphaFoldDB; Q570B4; -.
DR   SMR; Q570B4; -.
DR   BioGRID; 2517; 3.
DR   STRING; 3702.AT2G26250.1; -.
DR   iPTMnet; Q570B4; -.
DR   PaxDb; Q570B4; -.
DR   PRIDE; Q570B4; -.
DR   ProteomicsDB; 247146; -.
DR   EnsemblPlants; AT2G26250.1; AT2G26250.1; AT2G26250.
DR   GeneID; 817165; -.
DR   Gramene; AT2G26250.1; AT2G26250.1; AT2G26250.
DR   KEGG; ath:AT2G26250; -.
DR   Araport; AT2G26250; -.
DR   TAIR; locus:2057706; AT2G26250.
DR   eggNOG; ENOG502QU93; Eukaryota.
DR   HOGENOM; CLU_013238_2_0_1; -.
DR   InParanoid; Q570B4; -.
DR   OMA; YELSHIV; -.
DR   OrthoDB; 801187at2759; -.
DR   PhylomeDB; Q570B4; -.
DR   BioCyc; ARA:AT2G26250-MON; -.
DR   UniPathway; UPA00094; -.
DR   PRO; PR:Q570B4; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q570B4; baseline and differential.
DR   Genevisible; Q570B4; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005777; C:peroxisome; HDA:TAIR.
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:UniProtKB-UniPathway.
DR   GO; GO:0009409; P:response to cold; IEP:TAIR.
DR   GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
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; Endoplasmic reticulum; Membrane; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..550
FT                   /note="3-ketoacyl-CoA synthase 10"
FT                   /id="PRO_0000249102"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          113..402
FT                   /note="FAE"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        257
FT                   /evidence="ECO:0000250|UniProtKB:Q38860"
FT   ACT_SITE        336
FT                   /evidence="ECO:0000250|UniProtKB:Q38860"
FT   ACT_SITE        446
FT                   /evidence="ECO:0000250|UniProtKB:Q38860"
FT   ACT_SITE        450
FT                   /evidence="ECO:0000250|UniProtKB:Q38860"
FT   ACT_SITE        479
FT                   /evidence="ECO:0000250|UniProtKB:Q38860"
FT   ACT_SITE        483
FT                   /evidence="ECO:0000250|UniProtKB:Q38860"
FT   MUTAGEN         256
FT                   /note="G->R: In fdh-6; constitutive postgenital fusion
FT                   between floral organs and some leaves, which result in
FT                   malformations including abnormal ovules development."
FT                   /evidence="ECO:0000269|PubMed:10655527,
FT                   ECO:0000269|PubMed:9611177"
FT   MUTAGEN         346..351
FT                   /note="SVYQEE->FHSFWY: In fdh-1 and fdh-2; constitutive
FT                   postgenital fusion between floral organs and some leaves,
FT                   which result in malformations. Ectopic germination of
FT                   pollen aerial organs."
FT   MUTAGEN         352..550
FT                   /note="Missing: In fdh-1 and fdh-2; constitutive
FT                   postgenital fusion between floral organs and some leaves,
FT                   which result in malformations. Ectopic germination of
FT                   pollen aerial organs."
FT   MUTAGEN         353..550
FT                   /note="Missing: In fdh-9; constitutive postgenital fusion
FT                   between floral organs and some leaves, which result in
FT                   malformations."
FT                   /evidence="ECO:0000269|PubMed:10655527"
FT   MUTAGEN         390..550
FT                   /note="Missing: In fdh-4; constitutive postgenital fusion
FT                   between floral organs and some leaves, which result in
FT                   malformations."
FT                   /evidence="ECO:0000269|PubMed:10655527,
FT                   ECO:0000269|PubMed:9611177"
FT   MUTAGEN         497
FT                   /note="E->K: In fdh-7; constitutive postgenital fusion
FT                   between floral organs and some leaves, which result in
FT                   malformations."
FT                   /evidence="ECO:0000269|PubMed:10655527,
FT                   ECO:0000269|PubMed:9611177"
FT   MUTAGEN         509..550
FT                   /note="Missing: In fdh-5; constitutive postgenital fusion
FT                   between floral organs and some leaves, which result in
FT                   malformations including abnormal ovules development."
FT                   /evidence="ECO:0000269|PubMed:10655527,
FT                   ECO:0000269|PubMed:9611177"
FT   MUTAGEN         514
FT                   /note="G->D: In fdh-3; constitutive postgenital fusion
FT                   between floral organs and some leaves, which result in
FT                   malformations."
FT                   /evidence="ECO:0000269|PubMed:10655527,
FT                   ECO:0000269|PubMed:9611177"
FT   CONFLICT        256
FT                   /note="G -> R (in Ref. 2; AAF73979)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        455
FT                   /note="V -> L (in Ref. 6; BAD94049)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        497
FT                   /note="E -> K (in Ref. 2; AAF73980)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        514
FT                   /note="G -> D (in Ref. 2; AAF73976)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   550 AA;  61961 MW;  5DB3368601EDF174 CRC64;
     MGRSNEQDLL STEIVNRGIE PSGPNAGSPT FSVRVRRRLP DFLQSVNLKY VKLGYHYLIN
     HAVYLATIPV LVLVFSAEVG SLSREEIWKK LWDYDLATVI GFFGVFVLTA CVYFMSRPRS
     VYLIDFACYK PSDEHKVTKE EFIELARKSG KFDEETLGFK KRILQASGIG DETYVPRSIS
     SSENITTMKE GREEASTVIF GALDELFEKT RVKPKDVGVL VVNCSIFNPT PSLSAMVINH
     YKMRGNILSY NLGGMGCSAG IIAIDLARDM LQSNPNSYAV VVSTEMVGYN WYVGSDKSMV
     IPNCFFRMGC SAVMLSNRRR DFRHAKYRLE HIVRTHKAAD DRSFRSVYQE EDEQGFKGLK
     ISRDLMEVGG EALKTNITTL GPLVLPFSEQ LLFFAALLRR TFSPAAKTST TTSFSTSATA
     KTNGIKSSSS DLSKPYIPDY KLAFEHFCFH AASKVVLEEL QKNLGLSEEN MEASRMTLHR
     FGNTSSSGIW YELAYMEAKE SVRRGDRVWQ IAFGSGFKCN SVVWKAMRKV KKPTRNNPWV
     DCINRYPVPL
 
 
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