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LPAT4_ARATH
ID   LPAT4_ARATH             Reviewed;         378 AA.
AC   Q8L4Y2; Q9C9P8; Q9SSH0;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 4;
DE            EC=2.3.1.51;
DE   AltName: Full=Lysophosphatidyl acyltransferase 4;
GN   Name=LPAT4; Synonyms=LPAAT4; OrderedLocusNames=At1g75020; ORFNames=F25A4.2;
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   TISSUE SPECIFICITY.
RX   PubMed=15772283; DOI=10.1105/tpc.104.030403;
RA   Kim H.U., Li Y., Huang A.H.C.;
RT   "Ubiquitous and endoplasmic reticulum-located lysophosphatidyl
RT   acyltransferase, LPAT2, is essential for female but not male gametophyte
RT   development in Arabidopsis.";
RL   Plant Cell 17:1073-1089(2005).
CC   -!- FUNCTION: May convert lysophosphatidic acid (LPA) into phosphatidic
CC       acid by incorporating acyl moiety at the 2 position (By similarity).
CC       Has no activity when expressed in bacteria or yeast. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC         ChEBI:CHEBI:58608; EC=2.3.1.51;
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Widely expressed at low level.
CC       {ECO:0000269|PubMed:15772283}.
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC       may constitute the binding site for the phosphate moiety of the
CC       glycerol-3-phosphate. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD55275.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG51931.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC008263; AAD55275.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC013258; AAG51931.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE35662.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE35663.1; -; Genomic_DNA.
DR   EMBL; AY099547; AAM20399.1; -; mRNA.
DR   EMBL; BT001236; AAN65123.1; -; mRNA.
DR   EMBL; AY084709; AAM61283.1; -; mRNA.
DR   PIR; B96780; B96780.
DR   RefSeq; NP_565098.1; NM_106159.3.
DR   RefSeq; NP_974144.1; NM_202415.2.
DR   AlphaFoldDB; Q8L4Y2; -.
DR   SMR; Q8L4Y2; -.
DR   BioGRID; 29059; 9.
DR   IntAct; Q8L4Y2; 9.
DR   STRING; 3702.AT1G75020.2; -.
DR   PaxDb; Q8L4Y2; -.
DR   PRIDE; Q8L4Y2; -.
DR   ProteomicsDB; 238718; -.
DR   EnsemblPlants; AT1G75020.1; AT1G75020.1; AT1G75020.
DR   EnsemblPlants; AT1G75020.2; AT1G75020.2; AT1G75020.
DR   GeneID; 843840; -.
DR   Gramene; AT1G75020.1; AT1G75020.1; AT1G75020.
DR   Gramene; AT1G75020.2; AT1G75020.2; AT1G75020.
DR   KEGG; ath:AT1G75020; -.
DR   Araport; AT1G75020; -.
DR   TAIR; locus:2027196; AT1G75020.
DR   eggNOG; KOG1505; Eukaryota.
DR   HOGENOM; CLU_041844_0_0_1; -.
DR   InParanoid; Q8L4Y2; -.
DR   OMA; ESSAWLM; -.
DR   OrthoDB; 959325at2759; -.
DR   PhylomeDB; Q8L4Y2; -.
DR   BioCyc; ARA:AT1G75020-MON; -.
DR   BRENDA; 2.3.1.51; 399.
DR   UniPathway; UPA00557; UER00613.
DR   PRO; PR:Q8L4Y2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8L4Y2; baseline and differential.
DR   Genevisible; Q8L4Y2; AT.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR032098; Acyltransf_C.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF16076; Acyltransf_C; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..378
FT                   /note="Probable 1-acyl-sn-glycerol-3-phosphate
FT                   acyltransferase 4"
FT                   /id="PRO_0000208183"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        62..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           105..110
FT                   /note="HXXXXD motif"
SQ   SEQUENCE   378 AA;  43064 MW;  36DB41D29E3B7ABC CRC64;
     MEVCGDLKSD NLKNRPLTPL RILRGLMILL VFLSTAFMFL LYFAPIAALG LRLLSVQQSR
     KVVSLIFGLW LALWPYLFET VNGTTVVFSG DIIPVEKRVL LIANHRTEVD WMYLWNIALR
     KGCLGYIKYV LKSSLMKLPI FGWGFHVLEF IPVERKREVD EPVLLQMLSS FKDPQEPLWL
     ALFPEGTDFT EEKCKRSQKF AAEVGLPALS NVLLPKTRGF GVCLEVLHNS LDAVYDLTIA
     YKPRCPSFMD NVFGTDPSEV HIHVRRVLLK EIPANEAESS AWLMDSFKLK DKLLSDFNAQ
     GKFPNQRPEE ELSVLKCIAT FAGVISLTVV FIYLTLYSHS CFKVYACLSG TYLTFATYYK
     FQPSPGCFRE DSCKVKNH
 
 
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