FAP3_ARATH
ID FAP3_ARATH Reviewed; 287 AA.
AC Q9C8L2; Q8LFP0; Q9LPG8;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Fatty-acid-binding protein 3, chloroplastic;
DE Short=AtFAP3;
DE AltName: Full=Chalcone-flavanone isomerase family protein 3;
DE Flags: Precursor;
GN Name=FAP3; OrderedLocusNames=At1g53520; ORFNames=F22G10.11, T3F20.16;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clone.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-73, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER SER-72, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [6] {ECO:0007744|PDB:4DOL}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 71-287 IN COMPLEX WITH PALMITIC
RP ACID, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=22622584; DOI=10.1038/nature11009;
RA Ngaki M.N., Louie G.V., Philippe R.N., Manning G., Pojer F., Bowman M.E.,
RA Li L., Larsen E., Wurtele E.S., Noel J.P.;
RT "Evolution of the chalcone-isomerase fold from fatty-acid binding to
RT stereospecific catalysis.";
RL Nature 485:530-533(2012).
CC -!- FUNCTION: Fatty-acid-binding protein. Interacts with most fatty acids
CC tested and has maximal relative affinity for C16:0.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:22622584}.
CC -!- TISSUE SPECIFICITY: Expressed in developing cotyledons, young
CC seedlings, roots, seeds, embryos, macrospores, preanthesis and tapetum.
CC Restricted to developing and reproductive tissues.
CC {ECO:0000269|PubMed:22622584}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethal. {ECO:0000269|PubMed:22622584}.
CC -!- SIMILARITY: Belongs to the chalcone isomerase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF78437.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC018748; AAF78437.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC024260; AAG51975.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32951.1; -; Genomic_DNA.
DR EMBL; BT025725; ABF82628.1; -; mRNA.
DR EMBL; AY084729; AAM61303.1; -; mRNA.
DR PIR; D96575; D96575.
DR RefSeq; NP_175757.1; NM_104230.2.
DR PDB; 4DOL; X-ray; 1.70 A; A=71-287.
DR PDBsum; 4DOL; -.
DR AlphaFoldDB; Q9C8L2; -.
DR SMR; Q9C8L2; -.
DR BioGRID; 27012; 2.
DR STRING; 3702.AT1G53520.1; -.
DR iPTMnet; Q9C8L2; -.
DR PaxDb; Q9C8L2; -.
DR PRIDE; Q9C8L2; -.
DR ProteomicsDB; 230875; -.
DR EnsemblPlants; AT1G53520.1; AT1G53520.1; AT1G53520.
DR GeneID; 841787; -.
DR Gramene; AT1G53520.1; AT1G53520.1; AT1G53520.
DR KEGG; ath:AT1G53520; -.
DR Araport; AT1G53520; -.
DR TAIR; locus:2024877; AT1G53520.
DR eggNOG; ENOG502QQUK; Eukaryota.
DR HOGENOM; CLU_070923_0_0_1; -.
DR InParanoid; Q9C8L2; -.
DR OMA; IFLTWID; -.
DR OrthoDB; 1185120at2759; -.
DR PhylomeDB; Q9C8L2; -.
DR PRO; PR:Q9C8L2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C8L2; baseline and differential.
DR Genevisible; Q9C8L2; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005504; F:fatty acid binding; IPI:TAIR.
DR GO; GO:0016872; F:intramolecular lyase activity; IEA:InterPro.
DR GO; GO:0006631; P:fatty acid metabolic process; IMP:TAIR.
DR Gene3D; 1.10.890.20; -; 1.
DR Gene3D; 3.50.70.10; -; 1.
DR InterPro; IPR016087; Chalcone_isomerase.
DR InterPro; IPR016088; Chalcone_isomerase_3-sand.
DR InterPro; IPR016089; Chalcone_isomerase_bundle_sf.
DR InterPro; IPR036298; Chalcone_isomerase_sf.
DR Pfam; PF02431; Chalcone; 1.
DR SUPFAM; SSF54626; SSF54626; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chloroplast; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 73..287
FT /note="Fatty-acid-binding protein 3, chloroplastic"
FT /id="PRO_0000422079"
FT BINDING 114
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:22622584,
FT ECO:0007744|PDB:4DOL"
FT BINDING 126
FT /ligand="hexadecanoate"
FT /ligand_id="ChEBI:CHEBI:7896"
FT /evidence="ECO:0000269|PubMed:22622584,
FT ECO:0007744|PDB:4DOL"
FT MOD_RES 73
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 144
FT /note="T -> K (in Ref. 4; AAM61303)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="V -> L (in Ref. 4; AAM61303)"
FT /evidence="ECO:0000305"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:4DOL"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:4DOL"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:4DOL"
FT STRAND 106..132
FT /evidence="ECO:0007829|PDB:4DOL"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:4DOL"
FT HELIX 138..143
FT /evidence="ECO:0007829|PDB:4DOL"
FT HELIX 148..152
FT /evidence="ECO:0007829|PDB:4DOL"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:4DOL"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:4DOL"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:4DOL"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:4DOL"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:4DOL"
FT HELIX 200..213
FT /evidence="ECO:0007829|PDB:4DOL"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:4DOL"
FT STRAND 233..242
FT /evidence="ECO:0007829|PDB:4DOL"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:4DOL"
FT HELIX 254..265
FT /evidence="ECO:0007829|PDB:4DOL"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:4DOL"
FT HELIX 272..285
FT /evidence="ECO:0007829|PDB:4DOL"
SQ 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
