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Lysophospholipid acyltransferase 5 (LPLAT 5) (EC 2.3.1.-) (1-acylglycerophosphocholine O-acyltransferase) (EC 2.3.1.23) (1-acylglycerophosphoserine O-acyltransferase) (EC 2.3.1.n6) (Lysophosphatidylcholine acyltransferase) (LPCAT) (Lyso-PC acyltransferase) (Lysophosphatidylcholine acyltransferase 3) (Lyso-PC acyltransferase 3) (Lysophosphatidylserine acyltransferase) (LPSAT) (Lyso-PS acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 5) (O-acyltransferase domain-containing protein 5)

 MBOA5_HUMAN             Reviewed;         487 AA.
Q6P1A2; B2RDH0; B7Z3N3; Q7KZS1; Q92980; Q9BW40;
02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
05-DEC-2018, entry version 128.
RecName: Full=Lysophospholipid acyltransferase 5;
Short=LPLAT 5;
EC=2.3.1.-;
AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
EC=2.3.1.23;
AltName: Full=1-acylglycerophosphoserine O-acyltransferase;
EC=2.3.1.n6;
AltName: Full=Lysophosphatidylcholine acyltransferase;
Short=LPCAT;
Short=Lyso-PC acyltransferase;
AltName: Full=Lysophosphatidylcholine acyltransferase 3;
Short=Lyso-PC acyltransferase 3;
AltName: Full=Lysophosphatidylserine acyltransferase;
Short=LPSAT;
Short=Lyso-PS acyltransferase;
AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 5;
Short=O-acyltransferase domain-containing protein 5;
Name=LPCAT3; Synonyms=MBOAT5, OACT5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Endometrium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4] {ECO:0000312|EMBL:AAH65194.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon {ECO:0000312|EMBL:AAH00664.2}, and
Pancreas {ECO:0000312|EMBL:AAH65194.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5] {ECO:0000305, ECO:0000312|EMBL:AAC51640.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 50-487 (ISOFORM 1).
PubMed=9074930; DOI=10.1101/gr.7.3.268;
Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.;
"Large-scale sequencing in human chromosome 12p13: experimental and
computational gene structure determination.";
Genome Res. 7:268-280(1997).
[6] {ECO:0000305, ECO:0000312|EMBL:AAP35646.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-487 (ISOFORM 1/2).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND TISSUE SPECIFICITY.
PubMed=18195019; DOI=10.1074/jbc.M710422200;
Zhao Y., Chen Y.Q., Bonacci T.M., Bredt D.S., Li S., Bensch W.R.,
Moller D.E., Kowala M., Konrad R.J., Cao G.;
"Identification and characterization of a major liver
lysophosphatidylcholine acyltransferase.";
J. Biol. Chem. 283:8258-8265(2008).
[8]
FUNCTION, TISSUE SPECIFICITY, AND SUBSTRATE SPECIFICITY.
PubMed=18772128; DOI=10.1074/jbc.M806194200;
Gijon M.A., Riekhof W.R., Zarini S., Murphy R.C., Voelker D.R.;
"Lysophospholipid acyltransferases and arachidonate recycling in human
neutrophils.";
J. Biol. Chem. 283:30235-30245(2008).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Acyltransferase which mediates the conversion of
lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or
LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-
phosphocholine or PC) (LPCAT activity). Catalyzes also the
conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-
3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-
glycero-3-phospho-L-serine or PS) (LPSAT activity). Has also weak
lysophosphatidylethanolamine acyltransferase activity (LPEAT
activity). Favors polyunsaturated fatty acyl-CoAs as acyl donors
compared to saturated fatty acyl-CoAs. Seems to be the major
enzyme contributing to LPCAT activity in the liver.
Lysophospholipid acyltransferases (LPLATs) catalyze the
reacylation step of the phospholipid remodeling pathway also known
as the Lands cycle. {ECO:0000269|PubMed:18195019,
ECO:0000269|PubMed:18772128}.
-!- CATALYTIC ACTIVITY:
Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a
1,2-diacyl-sn-glycero-3-phosphocholine + CoA;
Xref=Rhea:RHEA:12937, ChEBI:CHEBI:57287, ChEBI:CHEBI:57643,
ChEBI:CHEBI:58168, ChEBI:CHEBI:58342; EC=2.3.1.23;
-!- CATALYTIC ACTIVITY:
Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA =
1,2-diacyl-sn-glycero-3-phospho-L-serine + CoA;
Xref=Rhea:RHEA:33191, ChEBI:CHEBI:57262, ChEBI:CHEBI:57287,
ChEBI:CHEBI:58342, ChEBI:CHEBI:64379; EC=2.3.1.n6;
-!- ACTIVITY REGULATION: Activity is inhibited by thimerosal.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=41.29 uM for palmitoyl-CoA {ECO:0000269|PubMed:18195019};
KM=36.65 uM for stearoyl-CoA {ECO:0000269|PubMed:18195019};
KM=72.68 uM for oleoyl-CoA {ECO:0000269|PubMed:18195019};
KM=201.4 uM for linoleoyl-CoA {ECO:0000269|PubMed:18195019};
KM=71.56 uM for arachidonoyl-CoA {ECO:0000269|PubMed:18195019};
KM=72.19 uM for 1-palmitoyl-lysophosphatidylcholine
{ECO:0000269|PubMed:18195019};
Vmax=1782 nmol/min/mg enzyme with palmitoyl-CoA and 1-palmitoyl-
lysophosphatidylcholine as substrates
{ECO:0000269|PubMed:18195019};
Vmax=996 nmol/min/mg enzyme with stearoyl-CoA and 1-palmitoyl-
lysophosphatidylcholine as substrates
{ECO:0000269|PubMed:18195019};
Vmax=4698 nmol/min/mg enzyme with oleoyl-CoA and 1-palmitoyl-
lysophosphatidylcholine as substrates
{ECO:0000269|PubMed:18195019};
Vmax=18148 nmol/min/mg enzyme with linoleoyl-CoA and 1-
palmitoyl-lysophosphatidylcholine as substrates
{ECO:0000269|PubMed:18195019};
Vmax=6247 nmol/min/mg enzyme with arachidonoyl-CoA and 1-
palmitoyl-lysophosphatidylcholine as substrates
{ECO:0000269|PubMed:18195019};
-!- PATHWAY: Lipid metabolism; phospholipid metabolism.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:18195019}; Multi-pass membrane protein
{ECO:0000269|PubMed:18195019}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q6P1A2-1; Sequence=Displayed;
Name=2;
IsoId=Q6P1A2-2; Sequence=VSP_053680;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in liver, pancreas and
adipose tissue. Very low expression in skeletal muscle and heart.
Detected in neutrophils. {ECO:0000269|PubMed:18195019,
ECO:0000269|PubMed:18772128}.
-!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
localization.
-!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
{ECO:0000255}.
-!- SEQUENCE CAUTION:
Sequence=AAB51326.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAC51640.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG37917.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; BX648009; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK296145; BAH12269.1; -; mRNA.
EMBL; AK315538; BAG37917.1; ALT_INIT; mRNA.
EMBL; AC006512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000664; AAH00664.2; -; mRNA.
EMBL; BC065194; AAH65194.1; -; mRNA.
EMBL; U47924; AAB51326.1; ALT_INIT; Genomic_DNA.
EMBL; U72515; AAC51640.1; ALT_INIT; mRNA.
EMBL; BT007000; AAP35646.1; -; mRNA.
CCDS; CCDS8572.1; -. [Q6P1A2-1]
RefSeq; NP_005759.4; NM_005768.5. [Q6P1A2-1]
UniGene; Hs.655248; -.
ProteinModelPortal; Q6P1A2; -.
BioGrid; 115464; 26.
IntAct; Q6P1A2; 4.
MINT; Q6P1A2; -.
STRING; 9606.ENSP00000261407; -.
SwissLipids; SLP:000000127; -.
iPTMnet; Q6P1A2; -.
PhosphoSitePlus; Q6P1A2; -.
BioMuta; LPCAT3; -.
DMDM; 74737127; -.
EPD; Q6P1A2; -.
MaxQB; Q6P1A2; -.
PaxDb; Q6P1A2; -.
PeptideAtlas; Q6P1A2; -.
PRIDE; Q6P1A2; -.
ProteomicsDB; 66828; -.
DNASU; 10162; -.
Ensembl; ENST00000261407; ENSP00000261407; ENSG00000111684. [Q6P1A2-1]
GeneID; 10162; -.
KEGG; hsa:10162; -.
UCSC; uc001qsi.4; human. [Q6P1A2-1]
CTD; 10162; -.
DisGeNET; 10162; -.
EuPathDB; HostDB:ENSG00000111684.10; -.
GeneCards; LPCAT3; -.
H-InvDB; HIX0129675; -.
HGNC; HGNC:30244; LPCAT3.
MIM; 611950; gene.
neXtProt; NX_Q6P1A2; -.
OpenTargets; ENSG00000111684; -.
PharmGKB; PA162394266; -.
eggNOG; KOG2705; Eukaryota.
eggNOG; COG5202; LUCA.
GeneTree; ENSGT00940000153938; -.
HOGENOM; HOG000019529; -.
HOVERGEN; HBG054659; -.
InParanoid; Q6P1A2; -.
KO; K13515; -.
OMA; TMPHCIL; -.
OrthoDB; EOG091G062X; -.
PhylomeDB; Q6P1A2; -.
TreeFam; TF106143; -.
BRENDA; 2.3.1.23; 2681.
Reactome; R-HSA-1482788; Acyl chain remodelling of PC.
Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
SABIO-RK; Q6P1A2; -.
UniPathway; UPA00085; -.
ChiTaRS; LPCAT3; human.
GeneWiki; MBOAT5; -.
GenomeRNAi; 10162; -.
PRO; PR:Q6P1A2; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111684; Expressed in 199 organ(s), highest expression level in right adrenal gland.
CleanEx; HS_LPCAT3; -.
ExpressionAtlas; Q6P1A2; baseline and differential.
Genevisible; Q6P1A2; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; TAS:Reactome.
GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IMP:MGI.
GO; GO:0047144; F:2-acylglycerol-3-phosphate O-acyltransferase activity; TAS:Reactome.
GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; TAS:Reactome.
GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; TAS:Reactome.
GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; TAS:Reactome.
GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0097006; P:regulation of plasma lipoprotein particle levels; IEA:Ensembl.
InterPro; IPR004299; MBOAT_fam.
Pfam; PF03062; MBOAT; 1.
1: Evidence at protein level;
Acetylation; Acyltransferase; Alternative splicing; Complete proteome;
Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
Phospholipid biosynthesis; Phospholipid metabolism; Polymorphism;
Reference proteome; Transferase; Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:25944712}.
CHAIN 2 487 Lysophospholipid acyltransferase 5.
/FTId=PRO_0000233382.
TRANSMEM 44 64 Helical. {ECO:0000255}.
TRANSMEM 84 104 Helical. {ECO:0000255}.
TRANSMEM 111 131 Helical. {ECO:0000255}.
TRANSMEM 180 200 Helical. {ECO:0000255}.
TRANSMEM 227 247 Helical. {ECO:0000255}.
TRANSMEM 285 305 Helical. {ECO:0000255}.
TRANSMEM 364 384 Helical. {ECO:0000255}.
TRANSMEM 422 442 Helical. {ECO:0000255}.
TRANSMEM 453 473 Helical. {ECO:0000255}.
MOTIF 484 487 Di-lysine motif.
ACT_SITE 338 338 {ECO:0000250}.
ACT_SITE 374 374 {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:25944712}.
VAR_SEQ 21 100 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053680.
VARIANT 63 63 F -> L (in dbSNP:rs34196984).
/FTId=VAR_050027.
VARIANT 217 217 I -> T (in dbSNP:rs1984564).
/FTId=VAR_050028.
CONFLICT 387 387 E -> K (in Ref. 4; AAH00664 and 6;
AAP35646). {ECO:0000305}.
SEQUENCE 487 AA; 56035 MW; 429258B54585B4A7 CRC64;
MASSAEGDEG TVVALAGVLQ SGFQELSLNK LATSLGASEQ ALRLIISIFL GYPFALFYRH
YLFYKETYLI HLFHTFTGLS IAYFNFGNQL YHSLLCIVLQ FLILRLMGRT ITAVLTTFCF
QMAYLLAGYY YTATGNYDIK WTMPHCVLTL KLIGLAVDYF DGGKDQNSLS SEQQKYAIRG
VPSLLEVAGF SYFYGAFLVG PQFSMNHYMK LVQGELIDIP GKIPNSIIPA LKRLSLGLFY
LVGYTLLSPH ITEDYLLTED YDNHPFWFRC MYMLIWGKFV LYKYVTCWLV TEGVCILTGL
GFNGFEEKGK AKWDACANMK VWLFETNPRF TGTIASFNIN TNAWVARYIF KRLKFLGNKE
LSQGLSLLFL ALWHGLHSGY LVCFQMEFLI VIVERQAARL IQESPTLSKL AAITVLQPFY
YLVQQTIHWL FMGYSMTAFC LFTWDKWLKV YKSIYFLGHI FFLSLLFILP YIHKAMVPRK
EKLKKME


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EIAAB25114 2-acylglycerol O-acyltransferase 2,Acyl-CoA monoacylglycerol acyltransferase 2,Dgat2l5,Diacylglycerol acyltransferase 2-like protein 5,Mgat1l,MGAT2,Mogat2,Monoacylglycerol O-acyltransferase 1-like,Mon
EIAAB31420 1-acylglycerol-3-phosphate O-acyltransferase 2,1-acyl-sn-glycerol-3-phosphate acyltransferase beta,1-AGP acyltransferase 2,1-AGPAT 2,Agpat2,LPAAT-beta,Lysophosphatidic acid acyltransferase beta,Mouse,
EIAAB31437 1-acylglycerol-3-phosphate O-acyltransferase 4,1-acyl-sn-glycerol-3-phosphate acyltransferase delta,1-AGP acyltransferase 4,1-AGPAT 4,Agpat4,LPAAT-delta,Lysophosphatidic acid acyltransferase delta,Mou
EIAAB31439 1-acylglycerol-3-phosphate O-acyltransferase 4,1-acyl-sn-glycerol-3-phosphate acyltransferase delta,1-AGP acyltransferase 4,1-AGPAT 4,Agpat4,LPAAT-delta,Lysophosphatidic acid acyltransferase delta,Rat
EIAAB31416 1-acylglycerol-3-phosphate O-acyltransferase 1,1-acyl-sn-glycerol-3-phosphate acyltransferase alpha,1-AGP acyltransferase 1,1-AGPAT 1,Agpat1,LPAAT-alpha,Lysophosphatidic acid acyltransferase alpha,Mou
EIAAB31435 1-acylglycerol-3-phosphate O-acyltransferase 3,1-acyl-sn-glycerol-3-phosphate acyltransferase gamma,1-AGP acyltransferase 3,1-AGPAT 3,Agpat3,LPAAT-gamma,Lysophosphatidic acid acyltransferase gamma,Mou
EIAAB30216 Acyltransferase-like 1-B,Aytl1b,Lpcat2b,Lysophosphatidylcholine acyltransferase 2B,Rat,Rattus norvegicus
EIAAB30215 Acyltransferase-like 1-B,Aytl1b,Lpcat2b,Lysophosphatidylcholine acyltransferase 2B,Mouse,Mus musculus
U2114Rb CLIA LCAT,Lecithin-cholesterol acyltransferase,Oryctolagus cuniculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rabbit 96T
U2114h CLIA Homo sapiens,Human,LCAT,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase 96T
U2114Rb CLIA kit LCAT,Lecithin-cholesterol acyltransferase,Oryctolagus cuniculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rabbit 96T
E2114h ELISA Homo sapiens,Human,LCAT,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase 96T
E2114Rb ELISA kit LCAT,Lecithin-cholesterol acyltransferase,Oryctolagus cuniculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rabbit 96T
U2114h CLIA kit Homo sapiens,Human,LCAT,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase 96T
EIAAB39180 Acact-2,Acat2,ACAT-2,Acyl-coenzyme A cholesterol acyltransferase 2,Cholesterol acyltransferase 2,Mouse,Mus musculus,Soat2,Sterol O-acyltransferase 2
E2114Rb ELISA LCAT,Lecithin-cholesterol acyltransferase,Oryctolagus cuniculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rabbit 96T
E2114h ELISA kit Homo sapiens,Human,LCAT,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase 96T
EIAAB39181 ACACT2,ACAT2,ACAT-2,Acyl-coenzyme A cholesterol acyltransferase 2,Cholesterol acyltransferase 2,Homo sapiens,Human,SOAT2,Sterol O-acyltransferase 2
U2114r CLIA Lcat,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rat,Rattus norvegicus 96T
E2114r ELISA Lcat,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rat,Rattus norvegicus 96T
E2114r ELISA kit Lcat,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rat,Rattus norvegicus 96T


 

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