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FAP2_ARATH
ID   FAP2_ARATH              Reviewed;         398 AA.
AC   Q84RK2; F4IUI5; O64841; Q58G09; Q84RK3; Q8GXU6;
DT   01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2013, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Fatty-acid-binding protein 2;
DE            Short=AtFAP2;
DE   AltName: Full=Chalcone-flavanone isomerase family protein 2;
GN   Name=FAP2; OrderedLocusNames=At2g26310; ORFNames=T1D16.5;
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=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   [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] (ISOFORMS 1 AND 3).
RX   PubMed=12481096; DOI=10.1104/pp.010207;
RA   Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.;
RT   "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2
RT   of Arabidopsis.";
RL   Plant Physiol. 130:2118-2128(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RA   Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA   Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   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. Associates with saturated fatty
CC       acid.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000269|PubMed:22622584}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q84RK2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q84RK2-2; Sequence=VSP_046341;
CC       Name=3;
CC         IsoId=Q84RK2-3; Sequence=VSP_046339;
CC       Name=4;
CC         IsoId=Q84RK2-4; Sequence=VSP_046338, VSP_046340;
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       {ECO:0000269|PubMed:22622584}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Derived from proteomicsdata. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the chalcone isomerase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC14521.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC004484; AAC14521.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC07821.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07822.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM62745.1; -; Genomic_DNA.
DR   EMBL; AY231415; AAO86843.1; -; mRNA.
DR   EMBL; AY231416; AAO86844.1; -; mRNA.
DR   EMBL; AK118033; BAC42664.1; -; mRNA.
DR   EMBL; BT005236; AAO63300.1; -; mRNA.
DR   EMBL; AY954800; AAX55126.1; -; mRNA.
DR   PIR; H84658; H84658.
DR   RefSeq; NP_001189606.1; NM_001202677.1. [Q84RK2-2]
DR   RefSeq; NP_001324880.1; NM_001336058.1. [Q84RK2-1]
DR   RefSeq; NP_180199.3; NM_128188.5. [Q84RK2-1]
DR   AlphaFoldDB; Q84RK2; -.
DR   SMR; Q84RK2; -.
DR   STRING; 3702.AT2G26310.1; -.
DR   PaxDb; Q84RK2; -.
DR   PRIDE; Q84RK2; -.
DR   ProteomicsDB; 230853; -. [Q84RK2-1]
DR   EnsemblPlants; AT2G26310.1; AT2G26310.1; AT2G26310. [Q84RK2-1]
DR   EnsemblPlants; AT2G26310.2; AT2G26310.2; AT2G26310. [Q84RK2-2]
DR   EnsemblPlants; AT2G26310.5; AT2G26310.5; AT2G26310. [Q84RK2-1]
DR   GeneID; 817171; -.
DR   Gramene; AT2G26310.1; AT2G26310.1; AT2G26310. [Q84RK2-1]
DR   Gramene; AT2G26310.2; AT2G26310.2; AT2G26310. [Q84RK2-2]
DR   Gramene; AT2G26310.5; AT2G26310.5; AT2G26310. [Q84RK2-1]
DR   KEGG; ath:AT2G26310; -.
DR   Araport; AT2G26310; -.
DR   TAIR; locus:2057751; AT2G26310.
DR   eggNOG; ENOG502QWEB; Eukaryota.
DR   HOGENOM; CLU_031098_1_0_1; -.
DR   InParanoid; Q84RK2; -.
DR   OMA; YLQPNTI; -.
DR   PhylomeDB; Q84RK2; -.
DR   PRO; PR:Q84RK2; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q84RK2; baseline and differential.
DR   GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR   GO; GO:0005504; F:fatty acid binding; IDA:TAIR.
DR   GO; GO:0016872; F:intramolecular lyase activity; IEA:InterPro.
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; PF16035; Chalcone_2; 1.
DR   SUPFAM; SSF54626; SSF54626; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chloroplast; Plastid; Reference proteome.
FT   CHAIN           1..398
FT                   /note="Fatty-acid-binding protein 2"
FT                   /id="PRO_0000422078"
FT   BINDING         222
FT                   /ligand="dodecanoate"
FT                   /ligand_id="ChEBI:CHEBI:18262"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M1X2"
FT   BINDING         235
FT                   /ligand="dodecanoate"
FT                   /ligand_id="ChEBI:CHEBI:18262"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M1X2"
FT   BINDING         302
FT                   /ligand="dodecanoate"
FT                   /ligand_id="ChEBI:CHEBI:18262"
FT                   /evidence="ECO:0000250|UniProtKB:Q9M1X2"
FT   VAR_SEQ         1..181
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11910074,
FT                   ECO:0000303|PubMed:14593172"
FT                   /id="VSP_046338"
FT   VAR_SEQ         1..128
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12481096"
FT                   /id="VSP_046339"
FT   VAR_SEQ         182..186
FT                   /note="FQKLD -> MTREP (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11910074,
FT                   ECO:0000303|PubMed:14593172"
FT                   /id="VSP_046340"
FT   VAR_SEQ         310..334
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.6"
FT                   /id="VSP_046341"
FT   CONFLICT        331
FT                   /note="P -> A (in Ref. 3; AAO86844)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   398 AA;  44809 MW;  4B3741C1BE7E9D43 CRC64;
     MSNMDPNSVL PKRSFLQHEL FSQLHIPGSL AFEAFSCISK FTGALLCWFS HGNLQKEVSK
     HQWGLTCKSR DSLKHVFEHR NVSVFPFHYV SKDISPGFFG NISKSTIQHF VNEAERLHSC
     SLLSLAAAMI PSLNVMSANG LALPLGSNDV KLRENIEHRT CPENTEHRTC QVGCEEYSGL
     SFQKLDWTRQ SVEPRTGIEF PMLLKENASR SNSEVLVATG SRTMKIIRIK SLKVYAFGFY
     VHPSSVCQKL GRKYASVPAS KLDKCDDLYK DLLREDIVMS VRLVVNYNGL KINTVRDVFE
     KSLRARLVKA NPKTDFNCLN DFGSFFRQDI PIPAGTIIDF RRTEDGQLIT EIGGNLIGAV
     RSKDLCRAFF GMYIGDVPVS EQTKEEIGRK VVGIIKRC
 
 
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