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Fatty-acid-binding protein 3, chloroplastic (AtFAP3) (Chalcone-flavanone isomerase family protein 3)

 FAP3_ARATH              Reviewed;         287 AA.
Q9C8L2; Q8LFP0; Q9LPG8;
01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
28-FEB-2018, entry version 101.
RecName: Full=Fatty-acid-binding protein 3, chloroplastic;
Short=AtFAP3;
AltName: Full=Chalcone-flavanone isomerase family protein 3;
Flags: Precursor;
Name=FAP3; OrderedLocusNames=At1g53520; ORFNames=F22G10.11, T3F20.16;
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 [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).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF clone.";
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-73, CLEAVAGE OF TRANSIT
PEPTIDE [LARGE SCALE ANALYSIS] AFTER SER-72, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[6]
X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 71-287 IN COMPLEX WITH
PALMITIC ACID, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
DISRUPTION PHENOTYPE.
PubMed=22622584; DOI=10.1038/nature11009;
Ngaki M.N., Louie G.V., Philippe R.N., Manning G., Pojer F.,
Bowman M.E., Li L., Larsen E., Wurtele E.S., Noel J.P.;
"Evolution of the chalcone-isomerase fold from fatty-acid binding to
stereospecific catalysis.";
Nature 485:530-533(2012).
-!- FUNCTION: Fatty-acid-binding protein. Interacts with most fatty
acids tested and has maximal relative affinity for C16:0.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
{ECO:0000269|PubMed:22622584}.
-!- TISSUE SPECIFICITY: Expressed in developing cotyledons, young
seedlings, roots, seeds, embryos, macrospores, preanthesis and
tapetum. Restricted to developing and reproductive tissues.
{ECO:0000269|PubMed:22622584}.
-!- DISRUPTION PHENOTYPE: Embryo lethal.
{ECO:0000269|PubMed:22622584}.
-!- SIMILARITY: Belongs to the chalcone isomerase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF78437.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC018748; AAF78437.1; ALT_SEQ; Genomic_DNA.
EMBL; AC024260; AAG51975.1; -; Genomic_DNA.
EMBL; CP002684; AEE32951.1; -; Genomic_DNA.
EMBL; BT025725; ABF82628.1; -; mRNA.
EMBL; AY084729; AAM61303.1; -; mRNA.
PIR; D96575; D96575.
RefSeq; NP_175757.1; NM_104230.2.
UniGene; At.37393; -.
PDB; 4DOL; X-ray; 1.70 A; A=71-287.
PDBsum; 4DOL; -.
ProteinModelPortal; Q9C8L2; -.
SMR; Q9C8L2; -.
BioGrid; 27012; 2.
STRING; 3702.AT1G53520.1; -.
iPTMnet; Q9C8L2; -.
PaxDb; Q9C8L2; -.
EnsemblPlants; AT1G53520.1; AT1G53520.1; AT1G53520.
GeneID; 841787; -.
Gramene; AT1G53520.1; AT1G53520.1; AT1G53520.
KEGG; ath:AT1G53520; -.
Araport; AT1G53520; -.
TAIR; locus:2024877; AT1G53520.
eggNOG; ENOG410IU0B; Eukaryota.
eggNOG; ENOG4111QE0; LUCA.
HOGENOM; HOG000005777; -.
InParanoid; Q9C8L2; -.
OMA; ISPRIKA; -.
OrthoDB; EOG09360N27; -.
PhylomeDB; Q9C8L2; -.
PRO; PR:Q9C8L2; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9C8L2; baseline and differential.
Genevisible; Q9C8L2; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005504; F:fatty acid binding; IPI:TAIR.
GO; GO:0016872; F:intramolecular lyase activity; IEA:InterPro.
GO; GO:0006631; P:fatty acid metabolic process; IMP:TAIR.
Gene3D; 1.10.890.20; -; 2.
Gene3D; 3.50.70.10; -; 2.
InterPro; IPR016087; Chalcone_isomerase.
InterPro; IPR016088; Chalcone_isomerase_3-sand.
InterPro; IPR016089; Chalcone_isomerase_bundle_sf.
InterPro; IPR036298; Chalcone_isomerase_sf.
Pfam; PF02431; Chalcone; 1.
SUPFAM; SSF54626; SSF54626; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chloroplast; Complete proteome; Plastid;
Reference proteome; Transit peptide.
TRANSIT 1 72 Chloroplast.
{ECO:0000244|PubMed:22223895}.
CHAIN 73 287 Fatty-acid-binding protein 3,
chloroplastic.
/FTId=PRO_0000422079.
BINDING 114 114 Fatty acid.
BINDING 126 126 Fatty acid.
MOD_RES 73 73 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
CONFLICT 144 144 T -> K (in Ref. 4; AAM61303).
{ECO:0000305}.
CONFLICT 263 263 V -> L (in Ref. 4; AAM61303).
{ECO:0000305}.
STRAND 83 85 {ECO:0000244|PDB:4DOL}.
TURN 87 89 {ECO:0000244|PDB:4DOL}.
STRAND 92 97 {ECO:0000244|PDB:4DOL}.
STRAND 106 132 {ECO:0000244|PDB:4DOL}.
HELIX 134 136 {ECO:0000244|PDB:4DOL}.
HELIX 138 143 {ECO:0000244|PDB:4DOL}.
HELIX 148 152 {ECO:0000244|PDB:4DOL}.
HELIX 155 163 {ECO:0000244|PDB:4DOL}.
STRAND 164 166 {ECO:0000244|PDB:4DOL}.
STRAND 168 176 {ECO:0000244|PDB:4DOL}.
HELIX 180 191 {ECO:0000244|PDB:4DOL}.
TURN 192 194 {ECO:0000244|PDB:4DOL}.
HELIX 200 213 {ECO:0000244|PDB:4DOL}.
STRAND 223 230 {ECO:0000244|PDB:4DOL}.
STRAND 233 242 {ECO:0000244|PDB:4DOL}.
STRAND 249 252 {ECO:0000244|PDB:4DOL}.
HELIX 254 265 {ECO:0000244|PDB:4DOL}.
STRAND 266 268 {ECO:0000244|PDB:4DOL}.
HELIX 272 285 {ECO:0000244|PDB:4DOL}.
SEQUENCE 287 AA; 30729 MW; BDBEB4F4F4E7D9F1 CRC64;
MDGILAAVPS AVCVSLRISC RNLDNAESIY HFPGKSLNRV SVLQTGNYVS RKGNSLLKNR
HCGEISRVIV KSAASSVGNA EDYAEETATS VKFKRSVTLP GCSSPLSLLG TGFREKKFAI
IGVKVYAAGY YVNESILSGL SAWTGRSADE IQRDSSLFVS IFQAQAEKSL QIVLVRDVDG
KTFWDALDEA ISPRIKSPSS EDTTALSTFR GIFQNRPLNK GSVILLTWIN TSNMLVSVSS
GGLPTNVDAT IESGNVTSAL FDVFFGDSPV SPTLKSSVAN QLAMTLV


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