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LCAT4_ARATH
ID   LCAT4_ARATH             Reviewed;         535 AA.
AC   Q71N54; O81867;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Lecithin-cholesterol acyltransferase-like 4;
DE            EC=2.3.1.-;
GN   Name=LCAT4; OrderedLocusNames=At4g19860; ORFNames=T16H5.220;
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 [MRNA].
RX   PubMed=15355352; DOI=10.1111/j.1432-1033.2004.04317.x;
RA   Noiriel A., Benveniste P., Banas A., Stymne S., Bouvier-Nave P.;
RT   "Expression in yeast of a novel phospholipase A1 cDNA from Arabidopsis
RT   thaliana.";
RL   Eur. J. Biochem. 271:3752-3764(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Cheuk R., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA19703.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB78988.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF421149; AAQ04052.1; -; mRNA.
DR   EMBL; AL024486; CAA19703.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161551; CAB78988.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE84235.1; -; Genomic_DNA.
DR   EMBL; BT022028; AAY25440.1; -; mRNA.
DR   PIR; T04767; T04767.
DR   RefSeq; NP_193721.2; NM_118106.4.
DR   AlphaFoldDB; Q71N54; -.
DR   SMR; Q71N54; -.
DR   STRING; 3702.AT4G19860.1; -.
DR   ESTHER; arath-LCAT4; PC-sterol_acyltransferase.
DR   iPTMnet; Q71N54; -.
DR   PaxDb; Q71N54; -.
DR   PRIDE; Q71N54; -.
DR   ProteomicsDB; 237058; -.
DR   EnsemblPlants; AT4G19860.1; AT4G19860.1; AT4G19860.
DR   GeneID; 827730; -.
DR   Gramene; AT4G19860.1; AT4G19860.1; AT4G19860.
DR   KEGG; ath:AT4G19860; -.
DR   Araport; AT4G19860; -.
DR   TAIR; locus:2133975; AT4G19860.
DR   eggNOG; KOG2369; Eukaryota.
DR   HOGENOM; CLU_035096_0_0_1; -.
DR   InParanoid; Q71N54; -.
DR   OMA; HVELNAM; -.
DR   OrthoDB; 828056at2759; -.
DR   PhylomeDB; Q71N54; -.
DR   BioCyc; ARA:AT4G19860-MON; -.
DR   PRO; PR:Q71N54; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q71N54; baseline and differential.
DR   Genevisible; Q71N54; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR   GO; GO:0004620; F:phospholipase activity; IDA:TAIR.
DR   GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR   GO; GO:0009395; P:phospholipid catabolic process; IDA:TAIR.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003386; LACT/PDAT_acylTrfase.
DR   Pfam; PF02450; LCAT; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..535
FT                   /note="Lecithin-cholesterol acyltransferase-like 4"
FT                   /id="PRO_0000398822"
FT   REGION          488..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        182
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        391
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        416
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
SQ   SEQUENCE   535 AA;  60431 MW;  A60A460DB07BD305 CRC64;
     MSLLLEEIIR SVEALLKLRN RNQEPYVDPN LNPVLLVPGI AGSILNAVDH ENGNEERVWV
     RIFGADHEFR TKMWSRFDPS TGKTISLDPK TSIVVPQDRA GLHAIDVLDP DMIVGRESVY
     YFHEMIVEMI GWGFEEGKTL FGFGYDFRQS NRLQETLDQF AKKLETVYKA SGEKKINVIS
     HSMGGLLVKC FMGLHSDIFE KYVQNWIAIA APFRGAPGYI TSTLLNGMSF VNGWEQNFFV
     SKWSMHQLLI ECPSIYELMC CPYFKWELPP VLELWREKES NDGVGTSYVV LESYCSLESL
     EVFTKSLSNN TADYCGESID LPFNWKIMEW AHKTKQVLAS AKLPPKVKFY NIYGTNLETP
     HSVCYGNEKM PVKDLTNLRY FQPTYICVDG DGTVPMESAM ADGLEAVARV GVPGEHRGIL
     NDHRVFRMLK KWLNVGEPDP FYNPVNDYVI LPTTYEFEKF HENGLEVASV KESWDIISDD
     NNIGTTGSTV NSISVSQPGD DQNPQAEARA TLTVQPQSDG RQHVELNAVS VSVDA
 
 
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