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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 1) (LPIAT1) (Membrane-bound O-acyltransferase domain-containing protein 7) (O-acyltransferase domain-containing protein 7) (m-mboa-7)

 MBOA7_MOUSE             Reviewed;         473 AA.
Q8CHK3; Q3UDM6; Q8R1P9; Q9CY76;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
07-JUN-2017, entry version 103.
RecName: Full=Lysophospholipid acyltransferase 7 {ECO:0000305};
Short=LPLAT 7 {ECO:0000305};
EC=2.3.1.- {ECO:0000250|UniProtKB:Q96N66};
AltName: Full=1-acylglycerophosphatidylinositol O-acyltransferase {ECO:0000250|UniProtKB:Q96N66};
EC=2.3.1.n4 {ECO:0000250|UniProtKB:Q96N66};
AltName: Full=Bladder and breast carcinoma-overexpressed gene 1 protein {ECO:0000305};
AltName: Full=Leukocyte receptor cluster member 4 {ECO:0000305};
AltName: Full=Lysophosphatidylinositol acyltransferase 1 {ECO:0000303|PubMed:23097495};
Short=LPIAT1 {ECO:0000303|PubMed:23097495};
AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 7 {ECO:0000305};
Short=O-acyltransferase domain-containing protein 7 {ECO:0000305};
Short=m-mboa-7 {ECO:0000305};
Name=Mboat7 {ECO:0000312|MGI:MGI:1924832};
Synonyms=Bb1, Leng4, Lpiat1 {ECO:0000303|PubMed:23097495}, Oact7;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=W/Wv;
PubMed=15065000; DOI=10.1007/s00535-003-1283-8;
Daigo Y., Takayama I., Ward S.M., Sanders K.M., Fujino M.A.;
"Isolation of novel mouse genes that were differentially expressed in
W/W(v) mouse fundus.";
J. Gastroenterol. 39:238-241(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23097495; DOI=10.1091/mbc.E12-09-0673;
Lee H.C., Inoue T., Sasaki J., Kubo T., Matsuda S., Nakasaki Y.,
Hattori M., Tanaka F., Udagawa O., Kono N., Itoh T., Ogiso H.,
Taguchi R., Arita M., Sasaki T., Arai H.;
"LPIAT1 regulates arachidonic acid content in phosphatidylinositol and
is required for cortical lamination in mice.";
Mol. Biol. Cell 23:4689-4700(2012).
-!- 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
(PubMed:23097495). Lysophospholipid acyltransferases (LPLATs)
catalyze the reacylation step of the phospholipid remodeling
pathway also known as the Lands cycle (By similarity). Required
for cortical lamination during brain development
(PubMed:23097495). {ECO:0000250|UniProtKB:Q96N66,
ECO:0000269|PubMed:23097495}.
-!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-
phosphatidylinositol = CoA + 1,2-diacyl-sn-glycero-3-
phosphatidylinositol. {ECO:0000250|UniProtKB:Q96N66}.
-!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + 1-acyl-sn-
glycerol 3-phosphate = [acyl-carrier-protein] + 1,2-diacyl-sn-
glycerol 3-phosphate. {ECO:0000250|UniProtKB:Q96N66}.
-!- PATHWAY: Lipid metabolism; phospholipid metabolism.
{ECO:0000250|UniProtKB:Q96N66}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- DISRUPTION PHENOTYPE: Knockout mice die within a month and show
atrophy of the cerebral cortex and hippocampus. Embryos at E18.5
have a forebrain smaller in size and show disordered cortical
lamination and delayed neuronal migration in the cortex.
{ECO:0000269|PubMed:23097495}.
-!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB055410; BAC53808.1; -; mRNA.
EMBL; EU016380; ABV66272.1; -; mRNA.
EMBL; AK019981; BAB31950.1; -; mRNA.
EMBL; AK150010; BAE29235.1; -; mRNA.
EMBL; AK154606; BAE32708.1; -; mRNA.
EMBL; AK170124; BAE41580.1; -; mRNA.
EMBL; BC023417; AAH23417.1; -; mRNA.
EMBL; BC118958; AAI18959.1; -; mRNA.
CCDS; CCDS20724.1; -.
RefSeq; NP_084210.2; NM_029934.3.
RefSeq; XP_006540495.1; XM_006540432.3.
UniGene; Mm.397541; -.
STRING; 10090.ENSMUSP00000037107; -.
SwissLipids; SLP:000000285; -.
iPTMnet; Q8CHK3; -.
PhosphoSitePlus; Q8CHK3; -.
EPD; Q8CHK3; -.
MaxQB; Q8CHK3; -.
PaxDb; Q8CHK3; -.
PeptideAtlas; Q8CHK3; -.
PRIDE; Q8CHK3; -.
Ensembl; ENSMUST00000038608; ENSMUSP00000037107; ENSMUSG00000035596.
GeneID; 77582; -.
KEGG; mmu:77582; -.
UCSC; uc009evq.1; mouse.
CTD; 79143; -.
MGI; MGI:1924832; Mboat7.
eggNOG; KOG2706; Eukaryota.
eggNOG; COG5202; LUCA.
GeneTree; ENSGT00550000074565; -.
HOGENOM; HOG000045421; -.
HOVERGEN; HBG105712; -.
InParanoid; Q8CHK3; -.
KO; K13516; -.
OMA; LSECVCT; -.
OrthoDB; EOG091G074Q; -.
PhylomeDB; Q8CHK3; -.
TreeFam; TF320024; -.
Reactome; R-MMU-1482922; Acyl chain remodelling of PI.
UniPathway; UPA00085; -.
PRO; PR:Q8CHK3; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000035596; -.
ExpressionAtlas; Q8CHK3; baseline and differential.
Genevisible; Q8CHK3; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0071617; F:lysophospholipid acyltransferase activity; IMP:MGI.
GO; GO:0021819; P:layer formation in cerebral cortex; IMP:MGI.
GO; GO:0046488; P:phosphatidylinositol metabolic process; IMP:MGI.
GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0021591; P:ventricular system development; IMP:MGI.
InterPro; IPR004299; MBOAT_fam.
Pfam; PF03062; MBOAT; 1.
1: Evidence at protein level;
Acyltransferase; Complete proteome; Glycoprotein; Lipid biosynthesis;
Lipid metabolism; Membrane; Phospholipid biosynthesis;
Phospholipid metabolism; Reference proteome; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 473 Lysophospholipid acyltransferase 7.
/FTId=PRO_0000317458.
TRANSMEM 9 29 Helical. {ECO:0000255}.
TRANSMEM 44 64 Helical. {ECO:0000255}.
TRANSMEM 74 94 Helical. {ECO:0000255}.
TRANSMEM 197 217 Helical. {ECO:0000255}.
TRANSMEM 247 267 Helical. {ECO:0000255}.
TRANSMEM 355 375 Helical. {ECO:0000255}.
TRANSMEM 429 449 Helical. {ECO:0000255}.
CARBOHYD 321 321 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 335 335 S -> R (in Ref. 3; BAB31950).
{ECO:0000305}.
CONFLICT 339 339 R -> C (in Ref. 3; BAE41580 and 4;
AAI18959/AAH23417). {ECO:0000305}.
CONFLICT 341 341 Y -> C (in Ref. 3; BAE29235).
{ECO:0000305}.
CONFLICT 386 386 H -> Q (in Ref. 3; BAE29235).
{ECO:0000305}.
SEQUENCE 473 AA; 53436 MW; CFB4FE0DB2951C4F CRC64;
MTPEEWTYLM VLLISIPVGF LFKKAGPGLK RWGAAAVGLG LTLFTCGPHS LHSLITILGT
WALIQAQPCS CHALALAWTF SYLLFFRALS LLGLPTPTPF TNAVQLLLTL KLVSLASEVQ
DLHLAQRKEI ASGFHKEPTL GLLPEVPSLM ETLSYSYCYV GIMTGPFFRY RTYLDWLEQP
FPEAVPSLRP LLRRAWPAPL FGLLFLLSSH LFPLEAVRED AFYARPLPTR LFYMIPVFFA
FRMRFYVAWI AAECGCIAAG FGAYPVAAKA RAGGGPTLQC PPPSSPEIAA SLEYDYETIR
NIDCYGTDFC VRVRDGMRYW NMTVQWWLAQ YIYKSAPFRS YVLRSAWTML LSAYWHGLHP
GYYLSFMTIP LCLAAEGYLE SALRRHLSPG GQKAWDWVHW FLKMRAYDYM CMGFVLLSMA
DTLRYWASIY FWVHFLALAC LGLGLVLGGG SPSKRKTPSQ ATSSQAKEKL REE


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