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ALT3_ARATH
ID   ALT3_ARATH              Reviewed;         190 AA.
AC   Q8W583; Q9C9G1;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Acyl-acyl carrier protein thioesterase ATL3, chloroplastic {ECO:0000305};
DE            EC=3.1.2.- {ECO:0000305};
DE   AltName: Full=Acyl-ACP thioesterase ATL3 {ECO:0000305};
DE   AltName: Full=Acyl-lipid thioesterase 3 {ECO:0000303|PubMed:24214063};
DE   Flags: Precursor;
GN   Name=ALT3 {ECO:0000303|PubMed:24214063};
GN   OrderedLocusNames=At1g68260 {ECO:0000312|Araport:AT1G68260};
GN   ORFNames=T22E19.11 {ECO:0000312|EMBL:AAG52599.1};
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, 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 fatty acids of long chain
CC       (14:1 and 16:1) and beta-keto fatty acids of medium to long chain (8:0,
CC       10:0, 12:0, 12:1, 14:0 and 16:0) when expressed in a heterologous
CC       organism (E.coli). Possesses thioesterase activity for lauroyl-ACP
CC       (12:0-ACP) in vitro. May play a role in the generation of long fatty
CC       acids in the chloroplast. {ECO:0000269|PubMed:24214063}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:24214063}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in stems and flowers and at lower
CC       levels in rosette leaves, cauline leaves and siliques.
CC       {ECO:0000269|PubMed:24214063}.
CC   -!- SIMILARITY: Belongs to the 4-hydroxybenzoyl-CoA thioesterase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG52599.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AC016447; AAG52599.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002684; AEE34774.1; -; Genomic_DNA.
DR   EMBL; AF419571; AAL31903.1; -; mRNA.
DR   EMBL; AY143819; AAN28758.1; -; mRNA.
DR   EMBL; AY085771; AAM62988.1; -; mRNA.
DR   PIR; B96706; B96706.
DR   RefSeq; NP_564926.1; NM_105497.5.
DR   AlphaFoldDB; Q8W583; -.
DR   SMR; Q8W583; -.
DR   STRING; 3702.AT1G68260.1; -.
DR   PaxDb; Q8W583; -.
DR   PRIDE; Q8W583; -.
DR   ProteomicsDB; 244459; -.
DR   EnsemblPlants; AT1G68260.1; AT1G68260.1; AT1G68260.
DR   GeneID; 843155; -.
DR   Gramene; AT1G68260.1; AT1G68260.1; AT1G68260.
DR   KEGG; ath:AT1G68260; -.
DR   Araport; AT1G68260; -.
DR   TAIR; locus:2199277; AT1G68260.
DR   eggNOG; ENOG502RYRP; Eukaryota.
DR   HOGENOM; CLU_101141_1_2_1; -.
DR   InParanoid; Q8W583; -.
DR   OMA; YFDHFIF; -.
DR   OrthoDB; 1286085at2759; -.
DR   PhylomeDB; Q8W583; -.
DR   BioCyc; ARA:AT1G68260-MON; -.
DR   BRENDA; 3.1.2.14; 399.
DR   PRO; PR:Q8W583; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8W583; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; 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   2: Evidence at transcript level;
KW   Chloroplast; Hydrolase; Lipid metabolism; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..49
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..190
FT                   /note="Acyl-acyl carrier protein thioesterase ATL3,
FT                   chloroplastic"
FT                   /id="PRO_0000435263"
FT   ACT_SITE        66
FT                   /evidence="ECO:0000250|UniProtKB:P56653,
FT                   ECO:0000250|UniProtKB:Q9C7I5"
SQ   SEQUENCE   190 AA;  21540 MW;  9F816427955DC857 CRC64;
     MFLQVTGTAT PAMPAVVFLN SWRRPLSIPL RSVKTFKPLA FFDLKGGKGM SEFHEVELKV
     RDYELDQFGV VNNAVYANYC QHGRHEFLES IGINCDEVAR SGEALAISEL TMKFLSPLRS
     GDKFVVKARI SGTSAARIYF DHFIFKLPNQ EPILEAKGIA VWLDNKYRPV RIPSSIRSKF
     VHFLRQDDAV
 
 
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