MBOA7_HUMAN
ID MBOA7_HUMAN Reviewed; 472 AA.
AC Q96N66; A9C4B6; B0V3I5; B4DQ87; Q05DF0; Q7L5N2; Q99908; Q9BPV2; Q9BRE9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Lysophospholipid acyltransferase 7 {ECO:0000305};
DE Short=LPLAT 7 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000269|PubMed:18094042, ECO:0000269|PubMed:18772128};
DE AltName: Full=1-acylglycerophosphatidylinositol O-acyltransferase {ECO:0000305};
DE AltName: Full=Bladder and breast carcinoma-overexpressed gene 1 protein;
DE AltName: Full=Leukocyte receptor cluster member 4;
DE AltName: Full=Lysophosphatidylinositol acyltransferase {ECO:0000303|PubMed:18094042, ECO:0000303|PubMed:18772128};
DE Short=LPIAT {ECO:0000303|PubMed:18094042};
DE Short=Lyso-PI acyltransferase {ECO:0000303|PubMed:18094042};
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 7 {ECO:0000303|PubMed:18094042};
DE Short=O-acyltransferase domain-containing protein 7 {ECO:0000303|PubMed:18094042};
DE Short=h-mboa-7 {ECO:0000303|PubMed:18094042};
GN Name=MBOAT7 {ECO:0000312|HGNC:HGNC:15505}; Synonyms=BB1, LENG4, OACT7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 2-472 (ISOFORM 1), AND VARIANT LEU-261.
RC TISSUE=Colon, Kidney, Lung, and Muscle;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-472 (ISOFORM 1).
RX PubMed=8702217;
RA Fukunaga-Johnson N., Lee S.W., Liebert M., Grossman H.B.;
RT "Molecular analysis of a gene, BB1, overexpressed in bladder and breast
RT carcinoma.";
RL Anticancer Res. 16:1085-1090(1996).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY,
RP AND ACTIVITY REGULATION.
RX PubMed=18772128; DOI=10.1074/jbc.m806194200;
RA Gijon M.A., Riekhof W.R., Zarini S., Murphy R.C., Voelker D.R.;
RT "Lysophospholipid acyltransferases and arachidonate recycling in human
RT neutrophils.";
RL J. Biol. Chem. 283:30235-30245(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SPTSSA.
RX PubMed=23510452; DOI=10.1111/gtc.12046;
RA Hirata Y., Yamamori N., Kono N., Lee H.C., Inoue T., Arai H.;
RT "Identification of small subunit of serine palmitoyltransferase a as a
RT lysophosphatidylinositol acyltransferase 1-interacting protein.";
RL Genes Cells 18:397-409(2013).
RN [11]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=30959108; DOI=10.1016/j.jsb.2019.04.006;
RA Caddeo A., Jamialahmadi O., Solinas G., Pujia A., Mancina R.M.,
RA Pingitore P., Romeo S.;
RT "MBOAT7 is anchored to endomembranes by six transmembrane domains.";
RL J. Struct. Biol. 206:349-360(2019).
RN [12]
RP 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).
RN [13]
RP INVOLVEMENT IN MRT57, AND VARIANT MRT57 253-GLU--ALA-259 DEL.
RX PubMed=27616480; DOI=10.1016/j.ajhg.2016.07.019;
RA Johansen A., Rosti R.O., Musaev D., Sticca E., Harripaul R., Zaki M.,
RA Caglayan A.O., Azam M., Sultan T., Froukh T., Reis A., Popp B., Ahmed I.,
RA John P., Ayub M., Ben-Omran T., Vincent J.B., Gleeson J.G., Abou Jamra R.;
RT "Mutations in MBOAT7, Encoding Lysophosphatidylinositol Acyltransferase I,
RT Lead to Intellectual Disability Accompanied by Epilepsy and Autistic
RT Features.";
RL Am. J. Hum. Genet. 99:912-916(2016).
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:18772128,
CC PubMed:18094042). Prefers arachidonoyl-CoA as the acyl donor, thus
CC contributing to the regulation of free levels arachidonic acid in cell
CC (PubMed:18772128, PubMed:18094042). In liver, participates in the
CC regulation of triglyceride metabolism through the phosphatidylinositol
CC acyl-chain remodeling regulation (PubMed:32253259).
CC {ECO:0000269|PubMed:18094042, ECO:0000269|PubMed:18772128,
CC ECO:0000269|PubMed:32253259}.
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:18094042, ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37016;
CC Evidence={ECO:0000269|PubMed:18772128};
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:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36000;
CC Evidence={ECO:0000269|PubMed:18772128};
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:18094042, ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33196;
CC Evidence={ECO:0000269|PubMed:18772128};
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:0000250|UniProtKB:Q8CHK3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36836;
CC Evidence={ECO:0000250|UniProtKB:Q8CHK3};
CC -!- ACTIVITY REGULATION: Activity is inhibited by thimerosal.
CC {ECO:0000269|PubMed:18772128}.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:18094042, ECO:0000269|PubMed:18772128}.
CC -!- SUBUNIT: Interacts with SPTSSA; the interaction facilitates MBOAT7
CC location to mitochondria-associated membranes (MAMs).
CC {ECO:0000269|PubMed:23510452}.
CC -!- INTERACTION:
CC Q96N66; Q86WV6: STING1; NbExp=2; IntAct=EBI-6116499, EBI-2800345;
CC Q96N66; Q8VCW4: Unc93b1; Xeno; NbExp=2; IntAct=EBI-6116499, EBI-6116986;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23510452, ECO:0000269|PubMed:30959108}; Multi-pass
CC membrane protein {ECO:0000305|PubMed:30959108}. Note=Localized in
CC specific membrane structures termed mitochondria-associated membranes
CC (MAMs) which connect the endoplasmic reticulum (ER) and the
CC mitochondria. {ECO:0000269|PubMed:23510452}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96N66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96N66-2; Sequence=VSP_030967;
CC Name=3;
CC IsoId=Q96N66-3; Sequence=VSP_030968;
CC -!- TISSUE SPECIFICITY: Overexpressed in metastatic breast and bladder
CC carcinomas relative to normal breast epithelium and urothelium.
CC {ECO:0000269|PubMed:18772128}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 57
CC (MRT57) [MIM:617188]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRT57
CC patients have moderate to severe intellectual disability, and delayed
CC psychomotor development with poor or absent speech. Some patients
CC manifest seizures and autistic features. {ECO:0000269|PubMed:27616480}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB37433.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; EU016381; ABV66273.1; -; mRNA.
DR EMBL; AK055908; BAB71043.1; -; mRNA.
DR EMBL; AK298689; BAG60849.1; -; mRNA.
DR EMBL; CU151838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU457734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72199.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72202.1; -; Genomic_DNA.
DR EMBL; BC002512; AAH02512.2; -; mRNA.
DR EMBL; BC003164; AAH03164.2; -; mRNA.
DR EMBL; BC006309; AAH06309.1; -; mRNA.
DR EMBL; BC015857; AAH15857.1; -; mRNA.
DR EMBL; S82470; AAB37433.1; ALT_FRAME; mRNA.
DR CCDS; CCDS12883.1; -. [Q96N66-1]
DR CCDS; CCDS54315.1; -. [Q96N66-2]
DR CCDS; CCDS54316.1; -. [Q96N66-3]
DR RefSeq; NP_001139528.1; NM_001146056.2. [Q96N66-2]
DR RefSeq; NP_001139554.1; NM_001146082.2. [Q96N66-3]
DR RefSeq; NP_001139555.1; NM_001146083.2. [Q96N66-2]
DR RefSeq; NP_077274.3; NM_024298.4. [Q96N66-1]
DR RefSeq; XP_011525601.1; XM_011527299.2. [Q96N66-1]
DR RefSeq; XP_011525602.1; XM_011527300.2. [Q96N66-1]
DR AlphaFoldDB; Q96N66; -.
DR SMR; Q96N66; -.
DR BioGRID; 122562; 202.
DR IntAct; Q96N66; 71.
DR MINT; Q96N66; -.
DR STRING; 9606.ENSP00000245615; -.
DR SwissLipids; SLP:000000131; -.
DR TCDB; 2.A.50.2.5; the glycerol uptake (gup) or membrane-bound acyl transferase (mboat) family.
DR GlyGen; Q96N66; 1 site.
DR iPTMnet; Q96N66; -.
DR PhosphoSitePlus; Q96N66; -.
DR SwissPalm; Q96N66; -.
DR BioMuta; MBOAT7; -.
DR DMDM; 167008974; -.
DR CPTAC; CPTAC-540; -.
DR CPTAC; CPTAC-541; -.
DR EPD; Q96N66; -.
DR jPOST; Q96N66; -.
DR MassIVE; Q96N66; -.
DR MaxQB; Q96N66; -.
DR PaxDb; Q96N66; -.
DR PeptideAtlas; Q96N66; -.
DR PRIDE; Q96N66; -.
DR ProteomicsDB; 77470; -. [Q96N66-1]
DR ProteomicsDB; 77471; -. [Q96N66-2]
DR ProteomicsDB; 77472; -. [Q96N66-3]
DR Antibodypedia; 32830; 121 antibodies from 20 providers.
DR DNASU; 79143; -.
DR Ensembl; ENST00000245615.6; ENSP00000245615.1; ENSG00000125505.17. [Q96N66-1]
DR Ensembl; ENST00000338624.10; ENSP00000344377.5; ENSG00000125505.17. [Q96N66-2]
DR Ensembl; ENST00000391754.5; ENSP00000375634.1; ENSG00000125505.17. [Q96N66-3]
DR Ensembl; ENST00000431666.6; ENSP00000410503.2; ENSG00000125505.17. [Q96N66-2]
DR Ensembl; ENST00000610862.4; ENSP00000481119.1; ENSG00000276935.4. [Q96N66-3]
DR Ensembl; ENST00000611239.1; ENSP00000481947.1; ENSG00000277025.4. [Q96N66-2]
DR Ensembl; ENST00000611602.4; ENSP00000482369.1; ENSG00000278322.4. [Q96N66-2]
DR Ensembl; ENST00000612053.1; ENSP00000482884.1; ENSG00000278519.4. [Q96N66-2]
DR Ensembl; ENST00000612567.1; ENSP00000483526.1; ENSG00000277733.4. [Q96N66-2]
DR Ensembl; ENST00000613506.4; ENSP00000478965.1; ENSG00000274194.4. [Q96N66-1]
DR Ensembl; ENST00000613746.4; ENSP00000484933.1; ENSG00000275118.4. [Q96N66-1]
DR Ensembl; ENST00000614279.1; ENSP00000480894.1; ENSG00000276935.4. [Q96N66-2]
DR Ensembl; ENST00000615282.4; ENSP00000483987.1; ENSG00000275118.4. [Q96N66-2]
DR Ensembl; ENST00000615453.4; ENSP00000482625.1; ENSG00000278519.4. [Q96N66-1]
DR Ensembl; ENST00000617012.4; ENSP00000484199.1; ENSG00000276935.4. [Q96N66-1]
DR Ensembl; ENST00000617656.4; ENSP00000481864.1; ENSG00000274194.4. [Q96N66-2]
DR Ensembl; ENST00000617772.1; ENSP00000480575.1; ENSG00000274194.4. [Q96N66-2]
DR Ensembl; ENST00000618378.4; ENSP00000482252.1; ENSG00000277025.4. [Q96N66-1]
DR Ensembl; ENST00000618826.4; ENSP00000483839.1; ENSG00000277923.4. [Q96N66-2]
DR Ensembl; ENST00000618899.4; ENSP00000480531.1; ENSG00000273592.4. [Q96N66-3]
DR Ensembl; ENST00000619670.4; ENSP00000479750.1; ENSG00000275118.4. [Q96N66-3]
DR Ensembl; ENST00000619745.4; ENSP00000481544.1; ENSG00000277025.4. [Q96N66-2]
DR Ensembl; ENST00000619842.4; ENSP00000481455.1; ENSG00000277923.4. [Q96N66-1]
DR Ensembl; ENST00000619855.4; ENSP00000484954.1; ENSG00000273592.4. [Q96N66-1]
DR Ensembl; ENST00000620311.1; ENSP00000478522.1; ENSG00000277923.4. [Q96N66-2]
DR Ensembl; ENST00000620371.1; ENSP00000479760.1; ENSG00000273592.4. [Q96N66-2]
DR Ensembl; ENST00000620636.1; ENSP00000482742.1; ENSG00000278322.4. [Q96N66-2]
DR Ensembl; ENST00000621146.4; ENSP00000481758.1; ENSG00000277733.4. [Q96N66-2]
DR Ensembl; ENST00000621455.4; ENSP00000477891.1; ENSG00000278519.4. [Q96N66-2]
DR Ensembl; ENST00000621612.4; ENSP00000478088.1; ENSG00000278322.4. [Q96N66-1]
DR Ensembl; ENST00000621875.4; ENSP00000478041.1; ENSG00000277733.4. [Q96N66-1]
DR GeneID; 79143; -.
DR KEGG; hsa:79143; -.
DR MANE-Select; ENST00000245615.6; ENSP00000245615.1; NM_024298.5; NP_077274.3.
DR UCSC; uc032icm.2; human. [Q96N66-1]
DR CTD; 79143; -.
DR DisGeNET; 79143; -.
DR GeneCards; MBOAT7; -.
DR HGNC; HGNC:15505; MBOAT7.
DR HPA; ENSG00000125505; Tissue enhanced (adrenal).
DR MalaCards; MBOAT7; -.
DR MIM; 606048; gene.
DR MIM; 617188; phenotype.
DR neXtProt; NX_Q96N66; -.
DR OpenTargets; ENSG00000125505; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR PharmGKB; PA162395057; -.
DR VEuPathDB; HostDB:ENSG00000125505; -.
DR eggNOG; KOG2706; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_1_1_1; -.
DR InParanoid; Q96N66; -.
DR OMA; EVERCWT; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q96N66; -.
DR TreeFam; TF320024; -.
DR BRENDA; 2.3.1.B46; 2681.
DR PathwayCommons; Q96N66; -.
DR Reactome; R-HSA-1482922; Acyl chain remodelling of PI.
DR SignaLink; Q96N66; -.
DR SIGNOR; Q96N66; -.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 79143; 22 hits in 1080 CRISPR screens.
DR ChiTaRS; MBOAT7; human.
DR GenomeRNAi; 79143; -.
DR Pharos; Q96N66; Tbio.
DR PRO; PR:Q96N66; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q96N66; protein.
DR Bgee; ENSG00000125505; Expressed in blood and 98 other tissues.
DR ExpressionAtlas; Q96N66; baseline and differential.
DR Genevisible; Q96N66; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; TAS:Reactome.
DR GO; GO:0047144; F:2-acylglycerol-3-phosphate O-acyltransferase activity; TAS:Reactome.
DR GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008374; F:O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0021819; P:layer formation in cerebral cortex; ISS:UniProtKB.
DR GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IMP:UniProtKB.
DR GO; GO:0090207; P:regulation of triglyceride metabolic process; IMP:UniProtKB.
DR GO; GO:0021591; P:ventricular system development; IEA:Ensembl.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Disease variant;
KW Endoplasmic reticulum; Glycoprotein; Intellectual disability;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..472
FT /note="Lysophospholipid acyltransferase 7"
FT /id="PRO_0000317457"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30959108"
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:30959108"
FT TOPO_DOM 23..33
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:30959108"
FT TRANSMEM 34..57
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:30959108"
FT TOPO_DOM 58..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30959108"
FT TRANSMEM 74..93
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:30959108"
FT TOPO_DOM 94..194
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:30959108"
FT TRANSMEM 195..212
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:30959108"
FT TOPO_DOM 213..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30959108"
FT TRANSMEM 232..261
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:30959108"
FT TOPO_DOM 262..426
FT /note="Lumenal"
FT /evidence="ECO:0000305|PubMed:30959108"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:30959108"
FT TOPO_DOM 448..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:30959108"
FT REGION 453..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..111
FT /note="MSPEEWTYLVVLLISIPIGFLFKKAGPGLKRWGAAAVGLGLTLFTCGPHTLH
FT SLVTILGTWALIQAQPCSCHALALAWTFSYLLFFRALSLLGLPTPTPFTNAVQLLLTLK
FT -> MGSSRCGPGAHPVHLWPPHFAFSGHHPRDLGPHSGPAL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030967"
FT VAR_SEQ 345..472
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030968"
FT VARIANT 253..259
FT /note="Missing (in MRT57)"
FT /evidence="ECO:0000269|PubMed:27616480"
FT /id="VAR_078044"
FT VARIANT 261
FT /note="F -> L (in dbSNP:rs17855385)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038526"
FT VARIANT 415
FT /note="V -> L (in dbSNP:rs35909464)"
FT /id="VAR_038527"
FT CONFLICT 70
FT /note="S -> P (in Ref. 2; BAB71043)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="S -> T (in Ref. 6; AAB37433)"
FT /evidence="ECO:0000305"
SQ 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
