MBOA1_HUMAN
ID MBOA1_HUMAN Reviewed; 495 AA.
AC Q6ZNC8; A9EDQ5; B4DL59; B4E3J4; Q86XC2; Q8N9R5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Lysophospholipid acyltransferase 1 {ECO:0000305};
DE Short=LPLAT 1;
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.23 {ECO:0000269|PubMed:18772128};
DE AltName: Full=1-acylglycerophosphoethanolamine O-acyltransferase {ECO:0000250|UniProtKB:Q8BH98};
DE EC=2.3.1.n7 {ECO:0000250|UniProtKB:Q8BH98};
DE AltName: Full=1-acylglycerophosphoserine O-acyltransferase MBOAT1 {ECO:0000305};
DE EC=2.3.1.n6 {ECO:0000269|PubMed:18772128};
DE AltName: Full=Lysophosphatidylserine acyltransferase;
DE Short=LPSAT;
DE Short=Lyso-PS acyltransferase;
DE AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 1;
DE Short=O-acyltransferase domain-containing protein 1;
GN Name=MBOAT1 {ECO:0000312|HGNC:HGNC:21579}; Synonyms=OACT1;
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).
RX PubMed=17890783; DOI=10.1074/jbc.m704509200;
RA Tamaki H., Shimada A., Itoh Y., Ohya M., Takase J., Miyashita M.,
RA Miyagawa H., Nozaki H., Nakayama R., Kumagai H.;
RT "LPT1 encodes a membrane-bound O-acyltransferase involved in the acylation
RT of lysophospholipids in the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 282:34288-34298(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Tongue, and Uterus;
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=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
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 FUNCTION, TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY, AND CATALYTIC
RP ACTIVITY.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Acyltransferase which catalyzes the transfert of an acyl
CC group from an acyl-CoA towards a lysophospholipid producing a
CC phospholipid and participates in the reacylation step of the
CC phospholipid remodeling pathway also known as the Lands cycle
CC (PubMed:18772128). Acts on lysophosphatidylserine (1-acyl-2-hydroxy-sn-
CC glycero-3-phospho-L-serine or LPS) and lysophosphatidylethanolamine (1-
CC acyl-sn-glycero-3-phosphoethanolamine or LPE), and to a lesser extend
CC lysophosphatidylcholine (PubMed:18772128). Prefers oleoyl-CoA as the
CC acyl donor and 1-oleoyl-LPE as acceptor (PubMed:18772128). May play a
CC role in neurite outgrowth during neuronal differentiation (By
CC similarity). {ECO:0000250|UniProtKB:Q8BH98,
CC ECO:0000269|PubMed:18772128}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phospho-L-serine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:33191,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64379; EC=2.3.1.n6;
CC Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33192;
CC Evidence={ECO:0000269|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC Evidence={ECO:0000269|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphoethanolamine + an acyl-CoA = a
CC 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CoA;
CC Xref=Rhea:RHEA:32995, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; EC=2.3.1.n7;
CC Evidence={ECO:0000250|UniProtKB:Q8BH98};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC Evidence={ECO:0000250|UniProtKB:Q8BH98};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-L-serine = 1,2-di-(9Z)-octadecenoyl-sn-glycero-3-phospho-L-
CC serine + CoA; Xref=Rhea:RHEA:37407, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74617, ChEBI:CHEBI:74905;
CC Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37408;
CC Evidence={ECO:0000269|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine +
CC octadecanoyl-CoA = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-
CC phospho-L-serine + CoA; Xref=Rhea:RHEA:37403, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57394, ChEBI:CHEBI:74617, ChEBI:CHEBI:74902;
CC Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37404;
CC Evidence={ECO:0000269|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-hexadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phospho-L-serine = 1-(9Z-octadecenoyl)-2-(9Z-hexadecenoyl)-sn-
CC glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:37399,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:61540, ChEBI:CHEBI:74617,
CC ChEBI:CHEBI:74901; Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37400;
CC Evidence={ECO:0000269|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC 3-phospho-L-serine = 1-(9Z-octadecenoyl)-2-(9Z,12Z-octadienoyl)-sn-
CC glycero-3-phospho-L-serine + CoA; Xref=Rhea:RHEA:37375,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:74617,
CC ChEBI:CHEBI:74892; Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37376;
CC Evidence={ECO:0000269|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphocholine + CoA; Xref=Rhea:RHEA:35991, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:72998, ChEBI:CHEBI:73001;
CC Evidence={ECO:0000269|PubMed:18772128};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC Evidence={ECO:0000269|PubMed:18772128};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-O-(1Z-alkenyl)-sn-glycero-3-
CC phosphoethanolamine = 1-O-(1Z)-alkenyl-2-(9Z)-octadecenoyl-sn-
CC glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37631,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:77288,
CC ChEBI:CHEBI:77291; Evidence={ECO:0000250|UniProtKB:Q8BH98};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37632;
CC Evidence={ECO:0000250|UniProtKB:Q8BH98};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37523, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:75036, ChEBI:CHEBI:75038;
CC Evidence={ECO:0000250|UniProtKB:Q8BH98};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37524;
CC Evidence={ECO:0000250|UniProtKB:Q8BH98};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:37499, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:74971, ChEBI:CHEBI:74986;
CC Evidence={ECO:0000250|UniProtKB:Q8BH98};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37500;
CC Evidence={ECO:0000250|UniProtKB:Q8BH98};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:36015, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:73004, ChEBI:CHEBI:73007;
CC Evidence={ECO:0000250|UniProtKB:Q8BH98};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36016;
CC Evidence={ECO:0000250|UniProtKB:Q8BH98};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(10Z-heptadecenoyl)-sn-glycero-3-phosphoethanolamine +
CC hexadecanoyl-CoA = 1-(10Z-heptadecenoyl)-2-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine + CoA; Xref=Rhea:RHEA:65128, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57379, ChEBI:CHEBI:149768, ChEBI:CHEBI:156345;
CC Evidence={ECO:0000250|UniProtKB:Q8BH98};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65129;
CC Evidence={ECO:0000250|UniProtKB:Q8BH98};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoyl-CoA + 1-(10Z-heptadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1-(10Z-heptadecenoyl)-2-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:65136,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:149768,
CC ChEBI:CHEBI:156344; Evidence={ECO:0000250|UniProtKB:Q8BH98};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65137;
CC Evidence={ECO:0000250|UniProtKB:Q8BH98};
CC -!- ACTIVITY REGULATION: Partially inhibited by thimerosal.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000269|PubMed:18772128}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6ZNC8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZNC8-2; Sequence=VSP_036729;
CC Name=3;
CC IsoId=Q6ZNC8-3; Sequence=VSP_036730, VSP_036731;
CC -!- TISSUE SPECIFICITY: Expressed in neutrophils.
CC {ECO:0000269|PubMed:18772128}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AB305043; BAF93899.1; -; mRNA.
DR EMBL; AK093994; BAC04264.1; -; mRNA.
DR EMBL; AK131269; BAD18447.1; -; mRNA.
DR EMBL; AK296857; BAG59421.1; -; mRNA.
DR EMBL; AK304748; BAG65506.1; -; mRNA.
DR EMBL; AL008627; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355139; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150650; AAI50651.1; -; mRNA.
DR EMBL; BC150652; AAI50653.1; -; mRNA.
DR CCDS; CCDS34346.1; -. [Q6ZNC8-1]
DR RefSeq; NP_001073949.1; NM_001080480.2. [Q6ZNC8-1]
DR RefSeq; XP_011512615.1; XM_011514313.2. [Q6ZNC8-3]
DR AlphaFoldDB; Q6ZNC8; -.
DR SMR; Q6ZNC8; -.
DR BioGRID; 127537; 31.
DR IntAct; Q6ZNC8; 31.
DR STRING; 9606.ENSP00000324944; -.
DR SwissLipids; SLP:000000133; -.
DR iPTMnet; Q6ZNC8; -.
DR PhosphoSitePlus; Q6ZNC8; -.
DR BioMuta; MBOAT1; -.
DR DMDM; 74749574; -.
DR EPD; Q6ZNC8; -.
DR jPOST; Q6ZNC8; -.
DR MassIVE; Q6ZNC8; -.
DR MaxQB; Q6ZNC8; -.
DR PaxDb; Q6ZNC8; -.
DR PeptideAtlas; Q6ZNC8; -.
DR PRIDE; Q6ZNC8; -.
DR ProteomicsDB; 68012; -. [Q6ZNC8-1]
DR ProteomicsDB; 68013; -. [Q6ZNC8-2]
DR ProteomicsDB; 68014; -. [Q6ZNC8-3]
DR Antibodypedia; 25215; 29 antibodies from 13 providers.
DR DNASU; 154141; -.
DR Ensembl; ENST00000324607.8; ENSP00000324944.7; ENSG00000172197.11. [Q6ZNC8-1]
DR GeneID; 154141; -.
DR KEGG; hsa:154141; -.
DR MANE-Select; ENST00000324607.8; ENSP00000324944.7; NM_001080480.3; NP_001073949.1.
DR UCSC; uc003ncx.4; human. [Q6ZNC8-1]
DR CTD; 154141; -.
DR DisGeNET; 154141; -.
DR GeneCards; MBOAT1; -.
DR HGNC; HGNC:21579; MBOAT1.
DR HPA; ENSG00000172197; Low tissue specificity.
DR MIM; 611732; gene.
DR neXtProt; NX_Q6ZNC8; -.
DR OpenTargets; ENSG00000172197; -.
DR PharmGKB; PA134979205; -.
DR VEuPathDB; HostDB:ENSG00000172197; -.
DR eggNOG; KOG2704; Eukaryota.
DR GeneTree; ENSGT01030000234564; -.
DR HOGENOM; CLU_011340_3_0_1; -.
DR InParanoid; Q6ZNC8; -.
DR OMA; WHGTRPG; -.
DR OrthoDB; 881262at2759; -.
DR PhylomeDB; Q6ZNC8; -.
DR TreeFam; TF314906; -.
DR PathwayCommons; Q6ZNC8; -.
DR Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
DR Reactome; R-HSA-1482839; Acyl chain remodelling of PE.
DR SignaLink; Q6ZNC8; -.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 154141; 18 hits in 1078 CRISPR screens.
DR ChiTaRS; MBOAT1; human.
DR GenomeRNAi; 154141; -.
DR Pharos; Q6ZNC8; Tdark.
DR PRO; PR:Q6ZNC8; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q6ZNC8; protein.
DR Bgee; ENSG00000172197; Expressed in oviduct epithelium and 150 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; TAS:Reactome.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; IMP:UniProtKB.
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:0030258; P:lipid modification; IBA:GO_Central.
DR GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; ISS:UniProtKB.
DR GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010975; P:regulation of neuron projection development; ISS:UniProtKB.
DR InterPro; IPR004299; MBOAT_fam.
DR Pfam; PF03062; MBOAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Lipid biosynthesis;
KW Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..495
FT /note="Lysophospholipid acyltransferase 1"
FT /id="PRO_0000273018"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 350
FT /evidence="ECO:0000250"
FT ACT_SITE 381
FT /evidence="ECO:0000250"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..158
FT /note="MAAEPQPSSLSYRTTGSTYLHPLSELLGIPLDQVNFVVCQLVALFAAFWFRI
FT YLRPGTTSSDVRHAVATIFGIYFVIFCFGWYSVHLFVLVLMCYAIMVTASVSNIHRYSF
FT FVAMGYLTICHISRIYIFHYGILTTDFSGPLMIVTQKITTLAFQVHD -> MEFSLRIF
FT L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036729"
FT VAR_SEQ 240..241
FT /note="AV -> HL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036730"
FT VAR_SEQ 242..495
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036731"
FT VARIANT 450
FT /note="I -> V (in dbSNP:rs2065649)"
FT /id="VAR_050025"
FT CONFLICT 170
FT /note="E -> G (in Ref. 2; BAG59421)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="S -> P (in Ref. 2; BAG59421)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="V -> I (in Ref. 2; BAC04264)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 56557 MW; 8666D7068D46FCD5 CRC64;
MAAEPQPSSL SYRTTGSTYL HPLSELLGIP LDQVNFVVCQ LVALFAAFWF RIYLRPGTTS
SDVRHAVATI FGIYFVIFCF GWYSVHLFVL VLMCYAIMVT ASVSNIHRYS FFVAMGYLTI
CHISRIYIFH YGILTTDFSG PLMIVTQKIT TLAFQVHDGL GRRAEDLSAE QHRLAIKVKP
SFLEYLSYLL NFMSVIAGPC NNFKDYIAFI EGKHIHMKLL EVNWKRKGFH SLPEPSPTGA
VIHKLGITLV SLLLFLTLTK TFPVTCLVDD WFVHKASFPA RLCYLYVVMQ ASKPKYYFAW
TLADAVNNAA GFGFSGVDKN GNFCWDLLSN LNIWKIETAT SFKMYLENWN IQTATWLKCV
CYQRVPWYPT VLTFILSALW HGVYPGYYFT FLTGILVTLA ARAVRNNYRH YFLSSRALKA
VYDAGTWAVT QLAVSYTVAP FVMLAVEPTI SLYKSMYFYL HIISLLIILF LPMKPQAHTQ
RRPQTLNSIN KRKTD
