ID   LPAT2_ARATH             Reviewed;         389 AA.
AC   Q8LG50; Q9SVX9;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 38.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase 2;
DE            EC=2.3.1.51;
DE   AltName: Full=Lysophosphatidyl acyltransferase 2;
GN   Name=LPAT2; Synonyms=LPAAT2; OrderedLocusNames=At3g57650;
GN   ORFNames=F15B8.160;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
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   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=14976237; DOI=10.1104/pp.103.035832;
RA   Kim H.U., Huang A.H.C.;
RT   "Plastid lysophosphatidyl acyltransferase is essential for embryo
RT   development in Arabidopsis.";
RL   Plant Physiol. 134:1206-1216(2004).
RN   [4]
RP   FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP   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
RT   gametophyte development in Arabidopsis.";
RL   Plant Cell 17:1073-1089(2005).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic
CC       acid by incorporating acyl moiety at the 2 position. Has
CC       preference for C-18-CoA substrates compared to C-16-CoA
CC       substrates. Required for female but not male gametophyte
CC       development.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate =
CC       CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- TISSUE SPECIFICITY: Present in roots, leaves, stems, floral buds
CC       and siliques (at protein level). Widely expressed. In contrast to
CC       LPAT1, it is not expressed at higher level in leaves.
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
CC       and may constitute the binding site for the phosphate moiety of
CC       the glycerol-3-phosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB41190.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL049660; CAB41190.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY084461; AAM61033.1; -; mRNA.
DR   IPI; IPI00528234; -.
DR   PIR; T06755; T06755.
DR   PRIDE; Q8LG50; -.
DR   GenomeReviews; BA000014_GR; AT3G57650.
DR   TAIR; At3g57650; -.
DR   BRENDA; 2.3.1.51; 302.
DR   GermOnline; AT3G57650; Arabidopsis thaliana.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferas...; IDA:TAIR.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002123; Acyltransferase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Complete proteome; Developmental protein;
KW   Endoplasmic reticulum; Membrane; Phospholipid biosynthesis;
KW   Transferase; Transmembrane.
FT   CHAIN         1    389       1-acyl-sn-glycerol-3-phosphate
FT                                acyltransferase 2.
FT                                /FTId=PRO_0000208179.
FT   TRANSMEM      2     22       Potential.
FT   TRANSMEM    305    325       Potential.
FT   TRANSMEM    333    353       Potential.
FT   MOTIF        91     96       HXXXXD motif.
SQ   SEQUENCE   389 AA;  43706 MW;  F34F73B2E2AC6837 CRC64;
     MVIAAAVIVP LGLLFFISGL AVNLFQAVCY VLIRPLSKNT YRKINRVVAE TLWLELVWIV
     DWWAGVKIQV FADNETFNRM GKEHALVVCN HRSDIDWLVG WILAQRSGCL GSALAVMKKS
     SKFLPVIGWS MWFSEYLFLE RNWAKDESTL KSGLQRLSDF PRPFWLALFV EGTRFTEAKL
     KAAQEYAASS ELPIPRNVLI PRTKSFVSAV SNMRSFVPAI YDMTVTIPKT SPPPTMLRLF
     KGQPSVVHVH IKCHSMKDLP ESDDAIAQWC RDQFVAKDAL LDKHIAADTF PGQQEQNIGR
     PIKSLAVVLS WACVLTLGAI KFLHWAQLFS SWKGITISAL GLGIITLCMQ ILIRSSQSER
     STPAKVVPAK PKDNHHPESS SQTETEKEK
//