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Database: UniProt
Entry: Q84P26
LinkDB: Q84P26
Original site: Q84P26 
ID   4CLL8_ARATH             Reviewed;         550 AA.
AC   Q84P26; Q8GXU2; Q9FF44;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   29-OCT-2014, entry version 77.
DE   RecName: Full=4-coumarate--CoA ligase-like 8;
DE            EC=6.2.1.-;
DE   AltName: Full=4-coumarate--CoA ligase isoform 11;
DE            Short=At4CL11;
GN   Name=4CLL8; OrderedLocusNames=At5g38120; ORFNames=MXA21.23, MXA21_10;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND GENE FAMILY ORGANIZATION.
RC   STRAIN=cv. Wassilewskija;
RX   PubMed=12805634; DOI=10.1104/pp.103.020552;
RA   Shockey J.M., Fulda M.S., Browse J.;
RT   "Arabidopsis contains a large superfamily of acyl-activating enzymes.
RT   Phylogenetic and biochemical analysis reveals a new class of acyl-
RT   coenzyme a synthetases.";
RL   Plant Physiol. 132:1065-1076(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Lawrence P.K.;
RT   "Functional classification of Arabidopsis thaliana 4-coumarate CoA
RT   ligase genes.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA   Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA   Miyajima N., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT   features of the 1.6 Mb regions covered by twenty physically assigned
RT   P1 clones.";
RL   DNA Res. 4:215-230(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA   Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T.,
RA   Shibata K., Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [6]
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [7]
RP   GENE FAMILY ORGANIZATION.
RX   PubMed=12819348; DOI=10.1073/pnas.1430550100;
RA   Schneider K., Hoevel K., Witzel K., Hamberger B., Schomburg D.,
RA   Kombrink E., Stuible H.-P.;
RT   "The substrate specificity-determining amino acid code of 4-
RT   coumarate:CoA ligase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8601-8606(2003).
RN   [8]
RP   INDUCTION.
RX   PubMed=16963437; DOI=10.1074/jbc.M607854200;
RA   Koo A.J.K., Chung H.S., Kobayashi Y., Howe G.A.;
RT   "Identification of a peroxisomal acyl-activating enzyme involved in
RT   the biosynthesis of jasmonic acid in Arabidopsis.";
RL   J. Biol. Chem. 281:33511-33520(2006).
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC   -!- INDUCTION: By wounding or by jasmonic acid (JA) treatment.
CC       {ECO:0000269|PubMed:16963437}.
CC   -!- DOMAIN: Both substrate-binding domains (SBD1 and SBD2) are
CC       involved in the substrate recognition, and are sufficient to
CC       confer the substrate specificity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB11279.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY250832; AAP03015.1; -; mRNA.
DR   EMBL; AY376735; AAQ86594.1; -; mRNA.
DR   EMBL; AB005247; BAB11279.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED94270.1; -; Genomic_DNA.
DR   EMBL; AK118041; BAC42672.1; -; mRNA.
DR   EMBL; BT005689; AAO64109.1; -; mRNA.
DR   RefSeq; NP_198628.2; NM_123172.3.
DR   UniGene; At.30435; -.
DR   UniGene; At.68167; -.
DR   ProteinModelPortal; Q84P26; -.
DR   SMR; Q84P26; 24-542.
DR   PRIDE; Q84P26; -.
DR   EnsemblPlants; AT5G38120.1; AT5G38120.1; AT5G38120.
DR   GeneID; 833792; -.
DR   KEGG; ath:AT5G38120; -.
DR   TAIR; AT5G38120; -.
DR   eggNOG; COG0318; -.
DR   HOGENOM; HOG000230009; -.
DR   InParanoid; Q84P26; -.
DR   OMA; ISIPIVC; -.
DR   PhylomeDB; Q84P26; -.
DR   BioCyc; ARA:AT5G38120-MONOMER; -.
DR   Genevestigator; Q84P26; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Ligase; Nucleotide-binding;
KW   Peroxisome; Reference proteome.
FT   CHAIN         1    550       4-coumarate--CoA ligase-like 8.
FT                                /FTId=PRO_0000299181.
FT   NP_BIND     207    215       ATP. {ECO:0000250}.
FT   NP_BIND     348    353       ATP. {ECO:0000250}.
FT   REGION      276    347       SBD1. {ECO:0000250}.
FT   REGION      348    412       SBD2. {ECO:0000250}.
FT   MOTIF       548    550       Microbody targeting signal.
FT                                {ECO:0000255}.
FT   BINDING     430    430       ATP. {ECO:0000250}.
FT   BINDING     445    445       ATP. {ECO:0000250}.
FT   BINDING     536    536       ATP. {ECO:0000250}.
FT   CONFLICT     72     72       M -> R (in Ref. 1; AAP03015).
FT                                {ECO:0000305}.
SQ   SEQUENCE   550 AA;  60393 MW;  F1E2D4A82864C623 CRC64;
     MANSQRSSSL IDPRNGFCTS NSTFYSKRKP LALPSKESLD ITTFISSQTY RGKTAFIDAA
     TDHRISFSDL WMAVDRVADC LLHDVGIRRG DVVLVLSPNT ISIPIVCLSV MSLGAVLTTA
     NPLNTASEIL RQIADSNPKL AFTTPELAPK IASSGISIVL ERVEDTLRVP RGLKVVGNLT
     EMMKKEPSGQ AVRNQVHKDD TAMLLYSSGT TGRSKGVNSS HGNLIAHVAR YIAEPFEQPQ
     QTFICTVPLF HTFGLLNFVL ATLALGTTVV ILPRFDLGEM MAAVEKYRAT TLILVPPVLV
     TMINKADQIM KKYDVSFLRT VRCGGAPLSK EVTQGFMKKY PTVDVYQGYA LTESNGAGAS
     IESVEESRRY GAVGLLSCGV EARIVDPNTG QVMGLNQTGE LWLKGPSIAK GYFRNEEEII
     TSEGWLKTGD LCYIDNDGFL FIVDRLKELI KYKGYQVPPA ELEALLLNHP DILDAAVIPF
     PDKEAGQFPM AYVARKPESN LCEKKVIDFI SKQVAPYKKI RKVAFIDSIP KTPSGKTLRK
     DLIKFAISKI
//
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