ALT2_ARATH
ID ALT2_ARATH Reviewed; 188 AA.
AC Q9C7I8;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Acyl-acyl carrier protein thioesterase ATL2, chloroplastic {ECO:0000305};
DE EC=3.1.2.- {ECO:0000305};
DE AltName: Full=Acyl-ACP thioesterase ATL2 {ECO:0000305};
DE AltName: Full=Acyl-lipid thioesterase 2 {ECO:0000303|PubMed:24214063};
DE Flags: Precursor;
GN Name=ALT2 {ECO:0000303|PubMed:24214063};
GN OrderedLocusNames=At1g35250 {ECO:0000312|Araport:AT1G35250};
GN ORFNames=T9I1.4 {ECO:0000312|EMBL:AAG51460.1};
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 [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].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24214063; DOI=10.1007/s11103-013-0151-z;
RA Pulsifer I.P., Lowe C., Narayaran S.A., Busuttil A.S., Vishwanath S.J.,
RA Domergue F., Rowland O.;
RT "Acyl-lipid thioesterase1-4 from Arabidopsis thaliana form a novel family
RT of fatty acyl-acyl carrier protein thioesterases with divergent expression
RT patterns and substrate specificities.";
RL Plant Mol. Biol. 84:549-563(2014).
CC -!- FUNCTION: Acyl-ACP thioesterase involved in the production of fatty
CC acids and beta-keto fatty acids. Can produce beta-keto fatty acids of
CC medium chain (8:0 and 10:0) and small amounts of 8:0 fatty acid when
CC expressed in a heterologous organism (E.coli). May play a role in
CC suberin biosynthesis. {ECO:0000269|PubMed:24214063}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:24214063}.
CC -!- TISSUE SPECIFICITY: Expressed in endodermal and peridermal cells in
CC young and mature roots, in boundaries of stem lateral organs and
CC developing seeds. {ECO:0000269|PubMed:24214063}.
CC -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
CC {ECO:0000305}.
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DR EMBL; AC069160; AAG51460.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31773.1; -; Genomic_DNA.
DR EMBL; BT024833; ABD60716.1; -; mRNA.
DR PIR; E86473; E86473.
DR RefSeq; NP_174759.1; NM_103223.4.
DR AlphaFoldDB; Q9C7I8; -.
DR SMR; Q9C7I8; -.
DR STRING; 3702.AT1G35250.1; -.
DR PaxDb; Q9C7I8; -.
DR PRIDE; Q9C7I8; -.
DR ProteomicsDB; 244420; -.
DR EnsemblPlants; AT1G35250.1; AT1G35250.1; AT1G35250.
DR GeneID; 840414; -.
DR Gramene; AT1G35250.1; AT1G35250.1; AT1G35250.
DR KEGG; ath:AT1G35250; -.
DR Araport; AT1G35250; -.
DR TAIR; locus:2206727; AT1G35250.
DR eggNOG; ENOG502RYRP; Eukaryota.
DR HOGENOM; CLU_101141_1_2_1; -.
DR InParanoid; Q9C7I8; -.
DR OMA; RDYECDI; -.
DR OrthoDB; 1286085at2759; -.
DR PhylomeDB; Q9C7I8; -.
DR PRO; PR:Q9C7I8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7I8; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0016297; F:acyl-[acyl-carrier-protein] hydrolase activity; IDA:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR006683; Thioestr_dom.
DR Pfam; PF03061; 4HBT; 1.
DR SUPFAM; SSF54637; SSF54637; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Hydrolase; Lipid metabolism; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..188
FT /note="Acyl-acyl carrier protein thioesterase ATL2,
FT chloroplastic"
FT /id="PRO_0000435262"
FT ACT_SITE 64
FT /evidence="ECO:0000250|UniProtKB:P56653,
FT ECO:0000250|UniProtKB:Q9C7I5"
SQ SEQUENCE 188 AA; 21325 MW; 8F2A7B745E5C0916 CRC64;
MFQATSTGAQ IMHAAFPRSW RRGHVLPLRS AKIFKPLACL ELRGSTGIGG FHEIELKVRD
YELDQFGVVN NAVYANYCQH GRHEFMDSIG INCNEVSRSG GALAIPELTI KFLAPLRSGC
RFVVKTRISG ISLVRIYFEQ FIFKLPNQEP ILEAKGTAVW LDNKYRPTRV PSHVRSYFGH
FQCQHLVD
