ALT1_ARATH
ID ALT1_ARATH Reviewed; 189 AA.
AC Q9C7I5; Q8LDP5;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Acyl-acyl carrier protein thioesterase ATL1, chloroplastic {ECO:0000305};
DE EC=3.1.2.- {ECO:0000305};
DE AltName: Full=Acyl-ACP thioesterase ATL1 {ECO:0000305};
DE AltName: Full=Acyl-lipid thioesterase 1 {ECO:0000303|PubMed:24214063};
DE Flags: Precursor;
GN Name=ALT1 {ECO:0000303|PubMed:24214063};
GN OrderedLocusNames=At1g35290 {ECO:0000312|Araport:AT1G35290};
GN ORFNames=T9I1.6 {ECO:0000312|EMBL:AAG51465.1};
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;
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]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP ASP-64.
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 fatty acids of medium to
CC long chain (12:0, 14:1, 14:0, 16:1 and 16:0) when expressed in a
CC heterologous organism (E.coli). Possesses thioesterase activity toward
CC lauroyl-ACP (12:0-ACP) in vitro. May play a role in cuticular wax
CC synthesis. {ECO:0000269|PubMed:24214063}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:24214063}.
CC -!- TISSUE SPECIFICITY: Expressed in epidermal cells of stems, in the top
CC portion of the gynoecium, petals and trichomes.
CC {ECO:0000269|PubMed:24214063}.
CC -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
CC {ECO:0000305}.
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DR EMBL; AC069160; AAG51465.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31776.1; -; Genomic_DNA.
DR EMBL; AF428452; AAL16221.1; -; mRNA.
DR EMBL; AY125550; AAM78060.1; -; mRNA.
DR EMBL; AY085874; AAM63087.1; -; mRNA.
DR PIR; H86473; H86473.
DR RefSeq; NP_564457.1; NM_103226.3.
DR AlphaFoldDB; Q9C7I5; -.
DR SMR; Q9C7I5; -.
DR STRING; 3702.AT1G35290.1; -.
DR PaxDb; Q9C7I5; -.
DR PRIDE; Q9C7I5; -.
DR ProteomicsDB; 245052; -.
DR EnsemblPlants; AT1G35290.1; AT1G35290.1; AT1G35290.
DR GeneID; 840418; -.
DR Gramene; AT1G35290.1; AT1G35290.1; AT1G35290.
DR KEGG; ath:AT1G35290; -.
DR Araport; AT1G35290; -.
DR TAIR; locus:2206752; AT1G35290.
DR eggNOG; ENOG502RYRP; Eukaryota.
DR HOGENOM; CLU_101141_1_2_1; -.
DR InParanoid; Q9C7I5; -.
DR OMA; FDQFIHQ; -.
DR OrthoDB; 1286085at2759; -.
DR PhylomeDB; Q9C7I5; -.
DR PRO; PR:Q9C7I5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C7I5; 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; IBA:GO_Central.
DR GO; GO:0047381; F:dodecanoyl-[acyl-carrier-protein] hydrolase activity; IDA:UniProtKB.
DR GO; GO:0016295; F:myristoyl-[acyl-carrier-protein] hydrolase activity; IDA:UniProtKB.
DR GO; GO:0016296; F:palmitoyl-[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 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Lipid metabolism; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..48
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 49..189
FT /note="Acyl-acyl carrier protein thioesterase ATL1,
FT chloroplastic"
FT /id="PRO_0000435261"
FT ACT_SITE 64
FT /evidence="ECO:0000250|UniProtKB:P56653,
FT ECO:0000305|PubMed:24214063"
FT MUTAGEN 64
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24214063"
FT CONFLICT 8
FT /note="V -> A (in Ref. 4; AAM63087)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 21500 MW; 47E7DDD146DDC496 CRC64;
MLKATGTVAP AMHVVFPCFS SRPLILPLRS TKTFKPLSCF KQQGGKGMNG VHEIELKVRD
YELDQFGVVN NAVYANYCQH GQHEFMETIG INCDEVSRSG EALAVSELTI KFLAPLRSGC
KFVVKTRISG TSMTRIYFEQ FIFKLPNQEP ILEAKGMAVW LDKRYRPVCI PSYIRSNFGH
FQRQHVVEY
