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Lysophospholipid acyltransferase 7 (LPLAT 7) (EC 2.3.1.-) (1-acylglycerophosphatidylinositol O-acyltransferase) (EC 2.3.1.n4) (Bladder and breast carcinoma-overexpressed gene 1 protein) (Leukocyte receptor cluster member 4) (Lysophosphatidylinositol acyltransferase) (LPIAT) (Lyso-PI acyltransferase) (Membrane-bound O-acyltransferase domain-containing protein 7) (O-acyltransferase domain-containing protein 7) (h-mboa-7)

 MBOA7_HUMAN             Reviewed;         472 AA.
Q96N66; A9C4B6; B0V3I5; B4DQ87; Q05DF0; Q7L5N2; Q99908; Q9BPV2;
Q9BRE9;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 2.
22-NOV-2017, entry version 118.
RecName: Full=Lysophospholipid acyltransferase 7 {ECO:0000320};
Short=LPLAT 7 {ECO:0000320};
EC=2.3.1.- {ECO:0000269|PubMed:18094042};
AltName: Full=1-acylglycerophosphatidylinositol O-acyltransferase {ECO:0000320};
EC=2.3.1.n4 {ECO:0000269|PubMed:18094042};
AltName: Full=Bladder and breast carcinoma-overexpressed gene 1 protein;
AltName: Full=Leukocyte receptor cluster member 4;
AltName: Full=Lysophosphatidylinositol acyltransferase {ECO:0000319|PubMed:18094042};
Short=LPIAT {ECO:0000319|PubMed:18094042};
Short=Lyso-PI acyltransferase {ECO:0000319|PubMed:18094042};
AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 7 {ECO:0000319|PubMed:18094042};
Short=O-acyltransferase domain-containing protein 7 {ECO:0000319|PubMed:18094042};
Short=h-mboa-7 {ECO:0000319|PubMed:18094042};
Name=MBOAT7 {ECO:0000304|HGNC:HGNC:15505}; Synonyms=BB1, LENG4, OACT7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
AND PATHWAY.
PubMed=18094042; DOI=10.1091/mbc.E07-09-0893;
Lee H.C., Inoue T., Imae R., Kono N., Shirae S., Matsuda S.,
Gengyo-Ando K., Mitani S., Arai H.;
"Caenorhabditis elegans mboa-7, a member of the MBOAT family, is
required for selective incorporation of polyunsaturated fatty acids
into phosphatidylinositol.";
Mol. Biol. Cell 19:1174-1184(2008).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 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=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 2-472 (ISOFORM 1), AND VARIANT LEU-261.
TISSUE=Colon, Kidney, Lung, and Muscle;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 49-472 (ISOFORM 1).
PubMed=8702217;
Fukunaga-Johnson N., Lee S.W., Liebert M., Grossman H.B.;
"Molecular analysis of a gene, BB1, overexpressed in bladder and
breast carcinoma.";
Anticancer Res. 16:1085-1090(1996).
[7]
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).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
INVOLVEMENT IN MRT57, AND VARIANT MRT57 253-GLU--ALA-259 DEL.
PubMed=27616480; DOI=10.1016/j.ajhg.2016.07.019;
Johansen A., Rosti R.O., Musaev D., Sticca E., Harripaul R., Zaki M.,
Caglayan A.O., Azam M., Sultan T., Froukh T., Reis A., Popp B.,
Ahmed I., John P., Ayub M., Ben-Omran T., Vincent J.B., Gleeson J.G.,
Abou Jamra R.;
"Mutations in MBOAT7, Encoding Lysophosphatidylinositol
Acyltransferase I, Lead to Intellectual Disability Accompanied by
Epilepsy and Autistic Features.";
Am. J. Hum. Genet. 99:912-916(2016).
-!- FUNCTION: Acyltransferase which contributes to the regulation of
free arachidonic acid (AA) in the cell through the remodeling of
phospholipids. Mediates the conversion of lysophosphatidylinositol
(1-acylglycerophosphatidylinositol or LPI) into
phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or
PI) (LPIAT activity). Prefers arachidonoyl-CoA as the acyl donor.
Lysophospholipid acyltransferases (LPLATs) catalyze the
reacylation step of the phospholipid remodeling pathway also known
as the Lands cycle. Required for cortical lamination during brain
development (By similarity). {ECO:0000269|PubMed:18094042,
ECO:0000269|PubMed:18772128, ECO:0007001|UniProtKB:Q8CHK3}.
-!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-
phosphatidylinositol = CoA + 1,2-diacyl-sn-glycero-3-
phosphatidylinositol. {ECO:0000269|PubMed:18094042}.
-!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + 1-acyl-sn-
glycerol 3-phosphate = [acyl-carrier-protein] + 1,2-diacyl-sn-
glycerol 3-phosphate. {ECO:0000269|PubMed:18094042}.
-!- ENZYME REGULATION: Activity is inhibited by thimerosal.
-!- PATHWAY: Lipid metabolism; phospholipid metabolism.
{ECO:0000269|PubMed:18094042}.
-!- INTERACTION:
Q86WV6:TMEM173; NbExp=2; IntAct=EBI-6116499, EBI-2800345;
Q8VCW4:Unc93b1 (xeno); NbExp=2; IntAct=EBI-6116499, EBI-6116986;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000320}; Multi-pass membrane
protein {ECO:0000320}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q96N66-1; Sequence=Displayed;
Name=2;
IsoId=Q96N66-2; Sequence=VSP_030967;
Name=3;
IsoId=Q96N66-3; Sequence=VSP_030968;
-!- TISSUE SPECIFICITY: Overexpressed in metastatic breast and bladder
carcinomas relative to normal breast epithelium and urothelium.
{ECO:0000269|PubMed:18772128}.
-!- DISEASE: Mental retardation, autosomal recessive 57 (MRT57)
[MIM:617188]: A form of mental retardation, a disorder
characterized by significantly below average general intellectual
functioning associated with impairments in adaptive behavior and
manifested during the developmental period. MRT57 patients have
moderate to severe intellectual disability, and delayed
psychomotor development with poor or absent speech. Some patients
manifest seizures and autistic features.
{ECO:0000269|PubMed:27616480}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
{ECO:0000320}.
-!- SEQUENCE CAUTION:
Sequence=AAB37433.1; Type=Frameshift; Positions=63, 93, 144, 186; Evidence={ECO:0000320};
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EMBL; EU016381; ABV66273.1; -; mRNA.
EMBL; AK055908; BAB71043.1; -; mRNA.
EMBL; AK298689; BAG60849.1; -; mRNA.
EMBL; CU151838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CU457734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471135; EAW72199.1; -; Genomic_DNA.
EMBL; CH471135; EAW72202.1; -; Genomic_DNA.
EMBL; BC002512; AAH02512.2; -; mRNA.
EMBL; BC003164; AAH03164.2; -; mRNA.
EMBL; BC006309; AAH06309.1; -; mRNA.
EMBL; BC015857; AAH15857.1; -; mRNA.
EMBL; S82470; AAB37433.1; ALT_FRAME; mRNA.
CCDS; CCDS12883.1; -. [Q96N66-1]
CCDS; CCDS54315.1; -. [Q96N66-2]
CCDS; CCDS54316.1; -. [Q96N66-3]
RefSeq; NP_001139528.1; NM_001146056.2. [Q96N66-2]
RefSeq; NP_001139554.1; NM_001146082.2. [Q96N66-3]
RefSeq; NP_001139555.1; NM_001146083.2. [Q96N66-2]
RefSeq; NP_077274.3; NM_024298.4. [Q96N66-1]
RefSeq; XP_011525601.1; XM_011527299.2. [Q96N66-1]
RefSeq; XP_011525602.1; XM_011527300.2. [Q96N66-1]
UniGene; Hs.467279; -.
ProteinModelPortal; Q96N66; -.
BioGrid; 122562; 56.
IntAct; Q96N66; 33.
MINT; MINT-4991231; -.
STRING; 9606.ENSP00000245615; -.
SwissLipids; SLP:000000131; -.
iPTMnet; Q96N66; -.
PhosphoSitePlus; Q96N66; -.
SwissPalm; Q96N66; -.
DMDM; 167008974; -.
EPD; Q96N66; -.
MaxQB; Q96N66; -.
PaxDb; Q96N66; -.
PeptideAtlas; Q96N66; -.
PRIDE; Q96N66; -.
DNASU; 79143; -.
Ensembl; ENST00000245615; ENSP00000245615; ENSG00000125505. [Q96N66-1]
Ensembl; ENST00000338624; ENSP00000344377; ENSG00000125505. [Q96N66-2]
Ensembl; ENST00000391754; ENSP00000375634; ENSG00000125505. [Q96N66-3]
Ensembl; ENST00000431666; ENSP00000410503; ENSG00000125505. [Q96N66-2]
Ensembl; ENST00000610862; ENSP00000481119; ENSG00000276935. [Q96N66-3]
Ensembl; ENST00000611239; ENSP00000481947; ENSG00000277025. [Q96N66-2]
Ensembl; ENST00000611602; ENSP00000482369; ENSG00000278322. [Q96N66-2]
Ensembl; ENST00000612053; ENSP00000482884; ENSG00000278519. [Q96N66-2]
Ensembl; ENST00000612567; ENSP00000483526; ENSG00000277733. [Q96N66-2]
Ensembl; ENST00000613506; ENSP00000478965; ENSG00000274194. [Q96N66-1]
Ensembl; ENST00000613746; ENSP00000484933; ENSG00000275118. [Q96N66-1]
Ensembl; ENST00000614279; ENSP00000480894; ENSG00000276935. [Q96N66-2]
Ensembl; ENST00000615282; ENSP00000483987; ENSG00000275118. [Q96N66-2]
Ensembl; ENST00000615453; ENSP00000482625; ENSG00000278519. [Q96N66-1]
Ensembl; ENST00000617012; ENSP00000484199; ENSG00000276935. [Q96N66-1]
Ensembl; ENST00000617656; ENSP00000481864; ENSG00000274194. [Q96N66-2]
Ensembl; ENST00000617772; ENSP00000480575; ENSG00000274194. [Q96N66-2]
Ensembl; ENST00000618378; ENSP00000482252; ENSG00000277025. [Q96N66-1]
Ensembl; ENST00000618826; ENSP00000483839; ENSG00000277923. [Q96N66-2]
Ensembl; ENST00000618899; ENSP00000480531; ENSG00000273592. [Q96N66-3]
Ensembl; ENST00000619670; ENSP00000479750; ENSG00000275118. [Q96N66-3]
Ensembl; ENST00000619745; ENSP00000481544; ENSG00000277025. [Q96N66-2]
Ensembl; ENST00000619842; ENSP00000481455; ENSG00000277923. [Q96N66-1]
Ensembl; ENST00000619855; ENSP00000484954; ENSG00000273592. [Q96N66-1]
Ensembl; ENST00000620311; ENSP00000478522; ENSG00000277923. [Q96N66-2]
Ensembl; ENST00000620371; ENSP00000479760; ENSG00000273592. [Q96N66-2]
Ensembl; ENST00000620636; ENSP00000482742; ENSG00000278322. [Q96N66-2]
Ensembl; ENST00000621146; ENSP00000481758; ENSG00000277733. [Q96N66-2]
Ensembl; ENST00000621455; ENSP00000477891; ENSG00000278519. [Q96N66-2]
Ensembl; ENST00000621612; ENSP00000478088; ENSG00000278322. [Q96N66-1]
Ensembl; ENST00000621875; ENSP00000478041; ENSG00000277733. [Q96N66-1]
GeneID; 79143; -.
KEGG; hsa:79143; -.
UCSC; uc032icm.2; human. [Q96N66-1]
CTD; 79143; -.
DisGeNET; 79143; -.
EuPathDB; HostDB:ENSG00000125505.16; -.
GeneCards; MBOAT7; -.
HGNC; HGNC:15505; MBOAT7.
HPA; HPA055967; -.
MalaCards; MBOAT7; -.
MIM; 606048; gene.
MIM; 617188; phenotype.
neXtProt; NX_Q96N66; -.
OpenTargets; ENSG00000125505; -.
PharmGKB; PA162395057; -.
eggNOG; KOG2706; Eukaryota.
eggNOG; COG5202; LUCA.
GeneTree; ENSGT00550000074565; -.
HOVERGEN; HBG105712; -.
InParanoid; Q96N66; -.
KO; K13516; -.
OMA; LSECVCT; -.
OrthoDB; EOG091G074Q; -.
PhylomeDB; Q96N66; -.
TreeFam; TF320024; -.
Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
UniPathway; UPA00085; -.
ChiTaRS; MBOAT7; human.
GenomeRNAi; 79143; -.
PRO; PR:Q96N66; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000125505; -.
CleanEx; HS_MBOAT7; -.
ExpressionAtlas; Q96N66; baseline and differential.
Genevisible; Q96N66; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:Reactome.
GO; GO:0016021; C:integral component of membrane; RCA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HTP:UniProtKB.
GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IBA:Reactome.
GO; GO:0047144; F:2-acylglycerol-3-phosphate O-acyltransferase activity; IBA:Reactome.
GO; GO:0071617; F:lysophospholipid acyltransferase activity; HMP:UniProtKB.
GO; GO:0021819; P:layer formation in cerebral cortex; HMP:UniProtKB.
GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; IBA:Reactome.
GO; GO:0008654; P:phospholipid biosynthetic process; RCA:UniProtKB-KW.
GO; GO:0021591; P:ventricular system development; RCA:Ensembl.
InterPro; IPR004299; MBOAT_fam.
Pfam; PF03062; MBOAT; 1.
1: Evidence at protein level;
Acyltransferase; Alternative splicing; Complete proteome;
Disease mutation; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
Membrane; Mental retardation; Phospholipid biosynthesis;
Phospholipid metabolism; Polymorphism; Reference proteome;
Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 472 Lysophospholipid acyltransferase 7.
/FTId=PRO_0000317457.
TRANSMEM 9 29 Helical. {ECO:0000270}.
TRANSMEM 44 64 Helical. {ECO:0000270}.
TRANSMEM 74 94 Helical. {ECO:0000270}.
TRANSMEM 197 217 Helical. {ECO:0000270}.
TRANSMEM 247 267 Helical. {ECO:0000270}.
TRANSMEM 355 375 Helical. {ECO:0000270}.
TRANSMEM 429 449 Helical. {ECO:0000270}.
CARBOHYD 321 321 N-linked (GlcNAc...) asparagine.
{ECO:0000270}.
VAR_SEQ 1 111 MSPEEWTYLVVLLISIPIGFLFKKAGPGLKRWGAAAVGLGL
TLFTCGPHTLHSLVTILGTWALIQAQPCSCHALALAWTFSY
LLFFRALSLLGLPTPTPFTNAVQLLLTLK -> MGSSRCGP
GAHPVHLWPPHFAFSGHHPRDLGPHSGPAL (in
isoform 2). {ECO:0000319|PubMed:14702039,
ECO:0000319|PubMed:15489334}.
/FTId=VSP_030967.
VAR_SEQ 345 472 Missing (in isoform 3).
{ECO:0000319|PubMed:15489334}.
/FTId=VSP_030968.
VARIANT 253 259 Missing (in MRT57).
{ECO:0000269|PubMed:27616480}.
/FTId=VAR_078044.
VARIANT 261 261 F -> L (in dbSNP:rs17855385).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_038526.
VARIANT 415 415 V -> L (in dbSNP:rs35909464).
/FTId=VAR_038527.
CONFLICT 70 70 S -> P (in Ref. 2; BAB71043).
{ECO:0000320}.
CONFLICT 345 345 S -> T (in Ref. 6; AAB37433).
{ECO:0000320}.
SEQUENCE 472 AA; 52765 MW; 1743F924468D3D2D CRC64;
MSPEEWTYLV VLLISIPIGF LFKKAGPGLK RWGAAAVGLG LTLFTCGPHT LHSLVTILGT
WALIQAQPCS CHALALAWTF SYLLFFRALS LLGLPTPTPF TNAVQLLLTL KLVSLASEVQ
DLHLAQRKEM ASGFSKGPTL GLLPDVPSLM ETLSYSYCYV GIMTGPFFRY RTYLDWLEQP
FPGAVPSLRP LLRRAWPAPL FGLLFLLSSH LFPLEAVRED AFYARPLPAR LFYMIPVFFA
FRMRFYVAWI AAECGCIAAG FGAYPVAAKA RAGGGPTLQC PPPSSPEKAA SLEYDYETIR
NIDCYSTDFC VRVRDGMRYW NMTVQWWLAQ YIYKSAPARS YVLRSAWTML LSAYWHGLHP
GYYLSFLTIP LCLAAEGRLE SALRGRLSPG GQKAWDWVHW FLKMRAYDYM CMGFVLLSLA
DTLRYWASIY FCIHFLALAA LGLGLALGGG SPSRRKAASQ PTSLAPEKLR EE


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EIAAB25115 2-acylglycerol O-acyltransferase 2,Acyl-CoA monoacylglycerol acyltransferase 2,DC5,DGAT2L5,Diacylglycerol acyltransferase 2-like protein 5,Diacylglycerol O-acyltransferase candidate 5,hDC5,hMGAT2,Homo
EIAAB25111 2-acylglycerol O-acyltransferase 1,Acyl-CoA monoacylglycerol acyltransferase 1,DC2,DGAT2L1,Diacylglycerol acyltransferase 2-like protein 1,Diacylglycerol O-acyltransferase candidate 2,hDC2,Homo sapien
EIAAB25112 2-acylglycerol O-acyltransferase 1,Acyl-CoA monoacylglycerol acyltransferase 1,Dgat2l1,Diacylglycerol acyltransferase 2-like protein 1,MGAT1,Mogat1,Monoacylglycerol O-acyltransferase 1,Mouse,Mus muscu
EIAAB25116 2-acylglycerol O-acyltransferase 3,Acyl-CoA monoacylglycerol acyltransferase 3,DC7,DGAT2L7,Diacylglycerol acyltransferase 2-like protein 7,Diacylglycerol O-acyltransferase candidate 7,hDC7,Homo sapien
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,
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
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
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
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
U2114h CLIA 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 kit LCAT,Lecithin-cholesterol acyltransferase,Oryctolagus cuniculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rabbit 96T
E2114Rb ELISA LCAT,Lecithin-cholesterol acyltransferase,Oryctolagus cuniculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rabbit 96T
U2114Rb CLIA 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
U2114h CLIA kit Homo sapiens,Human,LCAT,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase 96T
E2114h ELISA 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
EIAAB39181 ACACT2,ACAT2,ACAT-2,Acyl-coenzyme A cholesterol acyltransferase 2,Cholesterol acyltransferase 2,Homo sapiens,Human,SOAT2,Sterol O-acyltransferase 2
E2114r ELISA kit Lcat,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rat,Rattus norvegicus 96T
U2114r CLIA kit Lcat,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rat,Rattus norvegicus 96T
U2114m CLIA Lcat,Lecithin-cholesterol acyltransferase,Mouse,Mus musculus,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase 96T
U2114r CLIA Lcat,Lecithin-cholesterol acyltransferase,Phosphatidylcholine-sterol acyltransferase,Phospholipid-cholesterol acyltransferase,Rat,Rattus norvegicus 96T
EIAAB39177 Acact,ACAT-1,Acyl-coenzyme A cholesterol acyltransferase 1,Cholesterol acyltransferase 1,Mouse,Mus musculus,Soat1,Sterol O-acyltransferase 1


 

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