MBOA7_MOUSE
ID MBOA7_MOUSE Reviewed; 473 AA.
AC Q8CHK3; Q3UDM6; Q8R1P9; Q9CY76;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Lysophospholipid acyltransferase 7 {ECO:0000305};
DE Short=LPLAT 7 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:23097495, ECO:0000269|PubMed:23472195};
DE AltName: Full=1-acylglycerophosphatidylinositol O-acyltransferase {ECO:0000305};
DE AltName: Full=Bladder and breast carcinoma-overexpressed gene 1 protein {ECO:0000305};
DE AltName: Full=Leukocyte receptor cluster member 4 {ECO:0000305};
DE AltName: Full=Lysophosphatidylinositol acyltransferase 1 {ECO:0000303|PubMed:23097495};
DE Short=LPIAT1 {ECO:0000303|PubMed:23097495};
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 7 {ECO:0000305};
DE Short=O-acyltransferase domain-containing protein 7 {ECO:0000305};
DE Short=m-mboa-7 {ECO:0000305};
GN Name=Mboat7 {ECO:0000312|MGI:MGI:1924832};
GN Synonyms=Bb1, Leng4, Lpiat1 {ECO:0000303|PubMed:23097495}, Oact7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=W/Wv;
RX PubMed=15065000; DOI=10.1007/s00535-003-1283-8;
RA Daigo Y., Takayama I., Ward S.M., Sanders K.M., Fujino M.A.;
RT "Isolation of novel mouse genes that were differentially expressed in
RT W/W(v) mouse fundus.";
RL J. Gastroenterol. 39:238-241(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=18094042; DOI=10.1091/mbc.e07-09-0893;
RA Lee H.C., Inoue T., Imae R., Kono N., Shirae S., Matsuda S.,
RA Gengyo-Ando K., Mitani S., Arai H.;
RT "Caenorhabditis elegans mboa-7, a member of the MBOAT family, is required
RT for selective incorporation of polyunsaturated fatty acids into
RT phosphatidylinositol.";
RL Mol. Biol. Cell 19:1174-1184(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=23097495; DOI=10.1091/mbc.e12-09-0673;
RA Lee H.C., Inoue T., Sasaki J., Kubo T., Matsuda S., Nakasaki Y.,
RA Hattori M., Tanaka F., Udagawa O., Kono N., Itoh T., Ogiso H., Taguchi R.,
RA Arita M., Sasaki T., Arai H.;
RT "LPIAT1 regulates arachidonic acid content in phosphatidylinositol and is
RT required for cortical lamination in mice.";
RL Mol. Biol. Cell 23:4689-4700(2012).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23472195; DOI=10.1371/journal.pone.0058425;
RA Anderson K.E., Kielkowska A., Durrant T.N., Juvin V., Clark J.,
RA Stephens L.R., Hawkins P.T.;
RT "Lysophosphatidylinositol-acyltransferase-1 (LPIAT1) is required to
RT maintain physiological levels of PtdIns and PtdInsP(2) in the mouse.";
RL PLoS ONE 8:e58425-e58425(2013).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=32253259; DOI=10.1136/gutjnl-2020-320646;
RA Tanaka Y., Shimanaka Y., Caddeo A., Kubo T., Mao Y., Kubota T., Kubota N.,
RA Yamauchi T., Mancina R.M., Baselli G., Luukkonen P., Pihlajamaeki J.,
RA Yki-Jaervinen H., Valenti L., Arai H., Romeo S., Kono N.;
RT "LPIAT1/MBOAT7 depletion increases triglyceride synthesis fueled by high
RT phosphatidylinositol turnover.";
RL Gut 70:180-193(2021).
CC -!- FUNCTION: Acyltransferase which catalyzes the transfert of an acyl
CC group from an acyl-CoA to a lysophosphatidylinositol (1-
CC acylglycerophosphatidylinositol or LPI) leading to the production of a
CC phosphatidylinositol (1,2-diacyl-sn-glycero-3-phosphoinositol or PI)
CC and participates in the reacylation step of the phospholipid remodeling
CC pathway also known as the Lands cycle (PubMed:23097495,
CC PubMed:23472195, PubMed:32253259). Prefers arachidonoyl-CoA as the acyl
CC donor, thus contributing to the regulation of free levels arachidonic
CC acid in cell (PubMed:23097495, PubMed:23472195). In liver, participates
CC in the regulation of triglyceride metabolism through the
CC phosphatidylinositol acyl-chain remodeling regulation
CC (PubMed:32253259). {ECO:0000269|PubMed:23097495,
CC ECO:0000269|PubMed:23472195, ECO:0000269|PubMed:32253259}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-(1D-myo-inositol) + an acyl-CoA
CC = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CoA;
CC Xref=Rhea:RHEA:33195, ChEBI:CHEBI:57287, ChEBI:CHEBI:57880,
CC ChEBI:CHEBI:58342, ChEBI:CHEBI:64771;
CC Evidence={ECO:0000269|PubMed:23097495, ECO:0000269|PubMed:23472195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33196;
CC Evidence={ECO:0000269|PubMed:23097495, ECO:0000269|PubMed:23472195};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-octadecanoyl-sn-
CC glycero-3-phospho-(1D-myo-inositol) = 1-octadecanoyl-2-
CC (5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-
CC inositol) + CoA; Xref=Rhea:RHEA:36835, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57368, ChEBI:CHEBI:74243, ChEBI:CHEBI:133606;
CC Evidence={ECO:0000269|PubMed:23097495, ECO:0000269|PubMed:23472195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36836;
CC Evidence={ECO:0000269|PubMed:23097495, ECO:0000269|PubMed:23472195};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + a 1-acyl-sn-glycero-3-
CC phospho-(1D-myo-inositol) = a 1-acyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol) + CoA;
CC Xref=Rhea:RHEA:37015, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:64771, ChEBI:CHEBI:75243;
CC Evidence={ECO:0000269|PubMed:23097495, ECO:0000269|PubMed:23472195};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37016;
CC Evidence={ECO:0000269|PubMed:23097495, ECO:0000269|PubMed:23472195};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:35999, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000250|UniProtKB:Q96N66};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36000;
CC Evidence={ECO:0000250|UniProtKB:Q96N66};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:23097495, ECO:0000269|PubMed:23472195}.
CC -!- SUBUNIT: Interacts with SPTSSA; the interaction facilitates MBOAT7
CC location to mitochondria-associated membranes (MAMs).
CC {ECO:0000250|UniProtKB:Q96N66}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96N66}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96N66}. Note=Localized in specific membrane
CC structures termed mitochondria-associated membranes (MAMs) which
CC connect the endoplasmic reticulum (ER) and the mitochondria.
CC {ECO:0000250|UniProtKB:Q96N66}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice die within a month and show atrophy
CC of the cerebral cortex and hippocampus. Embryos at 18.5 dpc have a
CC forebrain smaller in size and show disordered cortical lamination and
CC delayed neuronal migration in the cortex (PubMed:23097495,
CC PubMed:23472195). Mice with conditional knockout in hepatocyte develop
CC hepatic steatosis spontaneously, and hepatic fibrosis on high fat diet
CC feeding (PubMed:32253259). {ECO:0000269|PubMed:23097495,
CC ECO:0000269|PubMed:23472195, ECO:0000269|PubMed:32253259}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB055410; BAC53808.1; -; mRNA.
DR EMBL; EU016380; ABV66272.1; -; mRNA.
DR EMBL; AK019981; BAB31950.1; -; mRNA.
DR EMBL; AK150010; BAE29235.1; -; mRNA.
DR EMBL; AK154606; BAE32708.1; -; mRNA.
DR EMBL; AK170124; BAE41580.1; -; mRNA.
DR EMBL; BC023417; AAH23417.1; -; mRNA.
DR EMBL; BC118958; AAI18959.1; -; mRNA.
DR CCDS; CCDS20724.1; -.
DR RefSeq; NP_084210.2; NM_029934.3.
DR RefSeq; XP_006540495.1; XM_006540432.3.
DR AlphaFoldDB; Q8CHK3; -.
DR SMR; Q8CHK3; -.
DR BioGRID; 218777; 2.
DR STRING; 10090.ENSMUSP00000037107; -.
DR SwissLipids; SLP:000000285; -.
DR GlyGen; Q8CHK3; 1 site.
DR iPTMnet; Q8CHK3; -.
DR PhosphoSitePlus; Q8CHK3; -.
DR EPD; Q8CHK3; -.
DR jPOST; Q8CHK3; -.
DR MaxQB; Q8CHK3; -.
DR PaxDb; Q8CHK3; -.
DR PeptideAtlas; Q8CHK3; -.
DR PRIDE; Q8CHK3; -.
DR ProteomicsDB; 295972; -.
DR Antibodypedia; 32830; 121 antibodies from 20 providers.
DR Ensembl; ENSMUST00000038608; ENSMUSP00000037107; ENSMUSG00000035596.
DR GeneID; 77582; -.
DR KEGG; mmu:77582; -.
DR UCSC; uc009evq.1; mouse.
DR CTD; 79143; -.
DR MGI; MGI:1924832; Mboat7.
DR VEuPathDB; HostDB:ENSMUSG00000035596; -.
DR eggNOG; KOG2706; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_1_1_1; -.
DR InParanoid; Q8CHK3; -.
DR OMA; EVERCWT; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q8CHK3; -.
DR TreeFam; TF320024; -.
DR BRENDA; 2.3.1.B46; 3474.
DR Reactome; R-MMU-1482922; Acyl chain remodelling of PI.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 77582; 7 hits in 76 CRISPR screens.
DR ChiTaRS; Mboat7; mouse.
DR PRO; PR:Q8CHK3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8CHK3; protein.
DR Bgee; ENSMUSG00000035596; Expressed in granulocyte and 250 other tissues.
DR ExpressionAtlas; Q8CHK3; baseline and differential.
DR Genevisible; Q8CHK3; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IMP:MGI.
DR GO; GO:0008374; F:O-acyltransferase activity; IMP:UniProtKB.
DR GO; GO:0021819; P:layer formation in cerebral cortex; IMP:MGI.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; IMP:UniProtKB.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IMP:MGI.
DR GO; GO:0090207; P:regulation of triglyceride metabolic process; IMP:UniProtKB.
DR GO; GO:0021591; P:ventricular system development; IMP:MGI.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..473
FT /note="Lysophospholipid acyltransferase 7"
FT /id="PRO_0000317458"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 23..33
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 34..57
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 58..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 74..93
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 94..194
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 195..212
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 213..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 232..261
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 262..426
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT TOPO_DOM 448..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96N66"
FT REGION 451..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 335
FT /note="S -> R (in Ref. 3; BAB31950)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="R -> C (in Ref. 3; BAE41580 and 4; AAI18959/
FT AAH23417)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="Y -> C (in Ref. 3; BAE29235)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="H -> Q (in Ref. 3; BAE29235)"
FT /evidence="ECO:0000305"
SQ 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
