FAP1_ARATH
ID FAP1_ARATH Reviewed; 279 AA.
AC Q9M1X2;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Fatty-acid-binding protein 1;
DE Short=AtFAP1;
DE AltName: Full=Chalcone-flavanone isomerase family protein 1;
GN Name=FAP1; OrderedLocusNames=At3g63170; ORFNames=F16M2.20;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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 [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] {ECO:0007744|PDB:4DOO}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 74-278 IN COMPLEX WITH
RP DODECANOATE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP 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 preferentially with
CC saturated fatty acid. May be involved in alpha-linolenic (C18:3)
CC metabolism.
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: No visible phenotype during vegetative growth,
CC but shorter siliques containing a reduced number of viable seeds.
CC Elevated total fatty-acid levels in leaves and seeds of plants grown at
CC 15 and 22 degrees Celsius. {ECO:0000269|PubMed:22622584}.
CC -!- SIMILARITY: Belongs to the chalcone isomerase family. {ECO:0000305}.
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DR EMBL; AL138648; CAB86418.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80443.1; -; Genomic_DNA.
DR EMBL; AY065149; AAL38325.1; -; mRNA.
DR EMBL; AY081626; AAM10188.1; -; mRNA.
DR EMBL; AY088229; AAM65770.1; -; mRNA.
DR PIR; T48106; T48106.
DR RefSeq; NP_567140.1; NM_116182.5.
DR PDB; 4DOO; X-ray; 1.90 A; A/B=74-278.
DR PDBsum; 4DOO; -.
DR AlphaFoldDB; Q9M1X2; -.
DR SMR; Q9M1X2; -.
DR STRING; 3702.AT3G63170.1; -.
DR iPTMnet; Q9M1X2; -.
DR PaxDb; Q9M1X2; -.
DR PRIDE; Q9M1X2; -.
DR ProteomicsDB; 230852; -.
DR EnsemblPlants; AT3G63170.1; AT3G63170.1; AT3G63170.
DR GeneID; 825492; -.
DR Gramene; AT3G63170.1; AT3G63170.1; AT3G63170.
DR KEGG; ath:AT3G63170; -.
DR Araport; AT3G63170; -.
DR TAIR; locus:2077229; AT3G63170.
DR eggNOG; ENOG502QQ8D; Eukaryota.
DR HOGENOM; CLU_070923_1_0_1; -.
DR InParanoid; Q9M1X2; -.
DR OMA; PWGSITL; -.
DR OrthoDB; 1185120at2759; -.
DR PhylomeDB; Q9M1X2; -.
DR PRO; PR:Q9M1X2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M1X2; baseline and differential.
DR Genevisible; Q9M1X2; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA: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 InterPro; IPR044228; FAP1.
DR PANTHER; PTHR47589; PTHR47589; 1.
DR Pfam; PF16035; Chalcone_2; 1.
DR SUPFAM; SSF54626; SSF54626; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloroplast; Plastid; Reference proteome.
FT CHAIN 1..279
FT /note="Fatty-acid-binding protein 1"
FT /id="PRO_0000422077"
FT BINDING 103
FT /ligand="dodecanoate"
FT /ligand_id="ChEBI:CHEBI:18262"
FT /evidence="ECO:0000269|PubMed:22622584,
FT ECO:0007744|PDB:4DOO"
FT BINDING 116
FT /ligand="dodecanoate"
FT /ligand_id="ChEBI:CHEBI:18262"
FT /evidence="ECO:0000269|PubMed:22622584,
FT ECO:0007744|PDB:4DOO"
FT BINDING 183
FT /ligand="dodecanoate"
FT /ligand_id="ChEBI:CHEBI:18262"
FT /evidence="ECO:0000269|PubMed:22622584,
FT ECO:0007744|PDB:4DOO"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:4DOO"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4DOO"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:4DOO"
FT STRAND 95..106
FT /evidence="ECO:0007829|PDB:4DOO"
FT STRAND 112..123
FT /evidence="ECO:0007829|PDB:4DOO"
FT HELIX 124..134
FT /evidence="ECO:0007829|PDB:4DOO"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:4DOO"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:4DOO"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:4DOO"
FT HELIX 173..191
FT /evidence="ECO:0007829|PDB:4DOO"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:4DOO"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:4DOO"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:4DOO"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:4DOO"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:4DOO"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:4DOO"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:4DOO"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:4DOO"
FT HELIX 262..275
FT /evidence="ECO:0007829|PDB:4DOO"
SQ SEQUENCE 279 AA; 30394 MW; F7AECC580FD805D1 CRC64;
MVSFRFPFSF SQPPRATTSF SGFSISAVAV SVTVGAAAAG AAIAASRNPS HPILEWAFSS
HRSSLSPWGS ITLADESVVE PKTGFSFPAS IGDSRRLLGV GLRKKSLLGL KNIDVYAFGV
YADCDDVKKL VGDKYANLPA SEIRGNKSFM DDLMEADIKM TIRLQIVYGK LNIRSVRNAF
QESVGNRLKK FGGSDNDELL QSFTSLFKDE YKIPRNSTID LTKDPGHVLS VAIEGNHVGS
VKSHLLCRSI LDLYIGEEPF DKNAREDFLD NAASLAFDN
