(data stored in ACNUC14452 zone)

HOGENOM: MOUSE13_PE1143

ID   MOUSE13_PE1143                       STANDARD;      PRT;   534 AA.
AC   MOUSE13_PE1143; Q3TFD2; Q3TAX4; Q6NXZ6; Q8BG23; Q8BUX7; Q99JU6;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Lysophosphatidylcholine acyltransferase 1; Short=LPC
DE   acyltransferase 1; Short=LPCAT-1; Short=LysoPC acyltransferase 1;
DE   Short=mLPCAT1; EC=2.3.1.-;AltName: Full=1-acylglycerophosphocholine
DE   O-acyltransferase; EC=2.3.1.23;AltName: Full=1-alkylglycerophosphocholine
DE   O-acetyltransferase; EC=2.3.1 67;AltName:
DE   Full=Acetyl-CoA:lyso-platelet-activating factor acetyltransferase;
DE   Short=Acetyl-CoA:lyso-PAF acetyltransferase; Short=Lyso-PAF
DE   acetyltransferase; Short=LysoPAFAT;AltName: Full=Acyltransferase-like 2;
DE   (MOUSE13.PE1143).
GN   Name=Lpcat1; Synonyms=Aytl2;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE13.PE1143.
CC       Mus musculus chromosome 13 NCBIM37  sequence 1..120284312 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:PCAT1_MOUSE
CC   -!- FUNCTION: Possesses both acyltransferase and acetyltransferase
CC       activities. Activity is calcium-independent. Mediates the
CC       conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into
CC       phosphatidylcholine (PC). Displays a clear preference for
CC       saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as
CC       acyl donors and acceptors, respectively. May synthesize
CC       phosphatidylcholine in pulmonary surfactant, thereby playing a
CC       pivotal role in respiratory physiology.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CC       = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + 1-alkyl-sn-glycero-3-
CC       phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-
CC       phosphocholine.
CC   -!- ENZYME REGULATION: Not activated by inflammatory stimulation.
CC       Inhibited by Cu(2+) and Fe(2+). Activity is not affected by
CC       Co(2+), Mg(2+) or Mn(2+).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.3 uM for 1-palmitoyl-LPC;
CC         KM=3 uM for palmitoyl-CoA;
CC       pH dependence:
CC         Optimum pH is 7.5;
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type II membrane protein. Golgi apparatus membrane; Single-pass
CC       type II membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3TFD2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TFD2-2; Sequence=VSP_019914;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3TFD2-3; Sequence=VSP_019913;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in lung where it is
CC       enriched in alveolar type II cells. Expressed at lower levels in
CC       spleen and brain. Also detected in erythroleukemic cells and
CC       reticulocytes. Weakly or not expressed in other tissues.
CC   -!- DEVELOPMENTAL STAGE: Expression increases steadily throughout
CC       embryogenesis and decreases slightly in the adult.
CC   -!- INDUCTION: Constitutively expressed. Not induced by inflammatory
CC       stimulation.
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-phosphocholine (By similarity).
CC   -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
CC       localization for type I membrane proteins (By similarity).
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH05662.1; Type=Erroneous initiation;
CC       Sequence=BAC32594.1; Type=Erroneous initiation;
CC       Sequence=BAC32760.1; Type=Erroneous initiation;
CC   -!- GENE_FAMILY: HOG000234374 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000021608;ENSMUST00000022099;ENSMUSP00000022099.
DR   EMBL; AB244717; - ;
DR   EMBL; AK046079; - ;
DR   EMBL; AK046507; - ;
DR   EMBL; AK079946; - ;
DR   EMBL; AK081865; - ;
DR   EMBL; AK155286; - ;
DR   EMBL; AK169190; - ;
DR   EMBL; AK170723; - ;
DR   EMBL; AK171582; - ;
DR   EMBL; BC005662; - ;
DR   EMBL; BC066809; - ;
DR   UniProtKB/Swiss-Prot; Q3TFD2; Q3TAX4; Q6NXZ6; Q8BG23; Q8BUX7; Q99JU6; -.
DR   EMBL; AB244717; BAE94687.2; -; mRNA.
DR   EMBL; AK046079; BAC32594.1; ALT_INIT; mRNA.
DR   EMBL; AK046507; BAC32760.1; ALT_INIT; mRNA.
DR   EMBL; AK081865; BAC38353.1; -; mRNA.
DR   EMBL; AK155286; BAE33166.1; -; mRNA.
DR   EMBL; AK169190; BAE40966.1; -; mRNA.
DR   EMBL; AK170723; BAE41980.1; -; mRNA.
DR   EMBL; AK171582; BAE42540.1; -; mRNA.
DR   EMBL; BC005662; AAH05662.1; ALT_INIT; mRNA.
DR   EMBL; BC066809; AAH66809.1; -; mRNA.
DR   IPI; IPI00225732; -.
DR   IPI; IPI00775928; -.
DR   IPI; IPI00776243; -.
DR   RefSeq; NP_663351.3; NM_145376.5.
DR   UniGene; Mm.284649; -.
DR   ProteinModelPortal; Q3TFD2; -.
DR   SMR; Q3TFD2; 342-488.
DR   STRING; Q3TFD2; -.
DR   PhosphoSite; Q3TFD2; -.
DR   PRIDE; Q3TFD2; -.
DR   Ensembl; ENSMUST00000022099; ENSMUSP00000022099; ENSMUSG00000021608.
DR   GeneID; 210992; -.
DR   KEGG; mmu:210992; -.
DR   UCSC; uc007rdk.1; mouse.
DR   UCSC; uc007rdl.1; mouse.
DR   UCSC; uc007rdm.1; mouse.
DR   CTD; 79888; -.
DR   MGI; MGI:2384812; Lpcat1.
DR   eggNOG; roNOG14370; -.
DR   InParanoid; Q3TFD2; -.
DR   OMA; RAQSNGK; -.
DR   OrthoDB; EOG49GKGF; -.
DR   PhylomeDB; Q3TFD2; -.
DR   BRENDA; 2.3.1.23; 3474.
DR   NextBio; 373109; -.
DR   ArrayExpress; Q3TFD2; -.
DR   Bgee; Q3TFD2; -.
DR   CleanEx; MM_LPCAT1; -.
DR   Genevestigator; Q3TFD2; -.
DR   GermOnline; ENSMUSG00000021608; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0047192; F:1-alkylglycerophosphocholine O-acetyltransferase activity; IEA:EC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR   InterPro; IPR002123; Acyltransferase.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00054; EFh; 3.
DR   SMART; SM00563; PlsC; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   HOGENOMDNA; MOUSE13.PE1143; -.
KW   ENSMUSG000000216085old_1320000031; ENSMUSP000000220991old_1320000031;
KW   Q8BJT4_MOUSE; AB244717; AK046079; AK046507; AK079946; AK081865; AK155286;
KW   AK170723; AK171582; BC005662; BC066809;
KW   Acyltransferase; Alternative splicing; Calcium; Complete proteome;
KW   Endoplasmic reticulum; Golgi apparatus; Membrane;
KW   Phospholipid biosynthesis; Reference proteome; Repeat; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   534 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MRLRGRGPRA APSSSSGAGD ARRLAPPGRN PFVHELRLSA LQKAQVAFMT LTLFPIRLLF
     AAFMMLLAWP FALLASLGPP DKEPEQPLAL WRKVVDFLLK AIMRTMWFAG GFHRVAVKGR
     QALPTEAAIL TLAPHSSYFD AIPVTMTMSS IVMKAESRDI PIWGTLIRYI RPVFVSRSDQ
     DSRRKTVEEI KRRAQSNGKW PQIMIFPEGT CTNRTCLITF KPGAFIPGVP VQPVVLRYPN
     KLDTITWTWQ GPGALKILWL TLCQFQNQVE IEFLPVYCPS EEEKRNPALY ASNVRRVMAK
     ALGVSVTDYT FEDCQLALAE GQLRLPADTC LLEFARLVRG LGLKPENLEK DLDKYSESAR
     MKRGEKIRLP EFAAYLEVPV SDALEDMFSL FDESGGGEID LREYVVALSV VCRPSQTLAT
     IQLAFKMYGS PEDGSIDEAN LSCILKTALG VSELTVTDLF QAIDQEDKGR ITFDDFCGFA
     EMYPDYAEDY LYPDQTHFDS CAQTPPAPTP NGFCIDFSPE NSDFGRKNSC KKAD
//

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