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MBOA2_MOUSE
ID   MBOA2_MOUSE             Reviewed;         519 AA.
AC   Q8R3I2; A9EDS7; Q8BHH5; Q8BM56; Q8R192; Q9CZ73;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Lysophospholipid acyltransferase 2 {ECO:0000305};
DE            Short=LPLAT 2;
DE            EC=2.3.1.- {ECO:0000269|PubMed:18287005};
DE   AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE            EC=2.3.1.23 {ECO:0000269|PubMed:18287005};
DE   AltName: Full=1-acylglycerophosphoethanolamine O-acyltransferase;
DE            EC=2.3.1.n7 {ECO:0000269|PubMed:18287005};
DE   AltName: Full=Lysophosphatidylcholine acyltransferase;
DE            Short=LPCAT;
DE            Short=Lyso-PC acyltransferase;
DE   AltName: Full=Lysophosphatidylcholine acyltransferase 4 {ECO:0000303|PubMed:29196633};
DE            Short=Lyso-PC acyltransferase 4;
DE            Short=mLPCAT4;
DE   AltName: Full=Lysophosphatidylethanolamine acyltransferase;
DE            Short=LPEAT;
DE            Short=Lyso-PE acyltransferase;
DE   AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 2;
DE            Short=O-acyltransferase domain-containing protein 2;
GN   Name=Mboat2 {ECO:0000312|MGI:MGI:1914466};
GN   Synonyms=Lpcat4 {ECO:0000303|PubMed:29196633}, Oact2;
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] (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 [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=18287005; DOI=10.1073/pnas.0712245105;
RA   Hishikawa D., Shindou H., Kobayashi S., Nakanishi H., Taguchi R.,
RA   Shimizu T.;
RT   "Discovery of a lysophospholipid acyltransferase family essential for
RT   membrane asymmetry and diversity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2830-2835(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Embryoid bodies, Medulla oblongata, and Testis;
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] (ISOFORM 2).
RC   STRAIN=Czech II; TISSUE=Eye, and 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=Heart, Kidney, and Lung;
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, CATALYTIC ACTIVITY, AND INDUCTION.
RX   PubMed=29196633; DOI=10.1038/s41598-017-16902-4;
RA   Tabe S., Hikiji H., Ariyoshi W., Hashidate-Yoshida T., Shindou H.,
RA   Shimizu T., Okinaga T., Seta Y., Tominaga K., Nishihara T.;
RT   "Lysophosphatidylcholine acyltransferase 4 is involved in chondrogenic
RT   differentiation of ATDC5 cells.";
RL   Sci. Rep. 7:16701-16701(2017).
CC   -!- FUNCTION: Acyltransferase which catalyzes the transfert of an acyl
CC       group from an acyl-CoA to a lysophospholipid leading to the production
CC       of a phospholipid and participates in the reacylation step of the
CC       phospholipid remodeling pathway also known as the Lands cycle
CC       (PubMed:18287005, PubMed:29196633). Catalyzes the acylation of
CC       lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) and
CC       to a lesser extend lysophosphatidylethanolamine (1-acyl-sn-glycero-3-
CC       phosphoethanolamine or LPE) (PubMed:18287005, PubMed:29196633). Does
CC       not acylates lysophosphatidic acid (LPA) and lysophosphatidylserine
CC       (PubMed:18287005). Prefers oleoyl-CoA as the acyl donor
CC       (PubMed:18287005, PubMed:29196633). May be involved in chondrocyte
CC       differentiation (PubMed:29196633). {ECO:0000269|PubMed:18287005,
CC       ECO:0000269|PubMed:29196633}.
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:18287005};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12938;
CC         Evidence={ECO:0000269|PubMed:18287005};
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:0000269|PubMed:18287005};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32996;
CC         Evidence={ECO:0000269|PubMed:18287005};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-O-(1Z-alkenyl)-sn-glycero-3-
CC         phosphocholine = 1-O-(1Z)-alkenyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC         phosphocholine + CoA; Xref=Rhea:RHEA:37627, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57387, ChEBI:CHEBI:77287, ChEBI:CHEBI:77294;
CC         Evidence={ECO:0000269|PubMed:18287005};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37628;
CC         Evidence={ECO:0000269|PubMed:18287005};
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:0000269|PubMed:18287005};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37632;
CC         Evidence={ECO:0000269|PubMed:18287005};
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:0000269|PubMed:18287005};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37524;
CC         Evidence={ECO:0000269|PubMed:18287005};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-octadecanoyl-sn-glycero-3-
CC         phosphocholine = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphocholine + CoA; Xref=Rhea:RHEA:37519, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57387, ChEBI:CHEBI:73858, ChEBI:CHEBI:75034;
CC         Evidence={ECO:0000269|PubMed:18287005};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37520;
CC         Evidence={ECO:0000269|PubMed:18287005};
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:0000269|PubMed:18287005};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37500;
CC         Evidence={ECO:0000269|PubMed:18287005};
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:0000269|PubMed:18287005};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36016;
CC         Evidence={ECO:0000269|PubMed:18287005};
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:18287005, ECO:0000269|PubMed:29196633};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35992;
CC         Evidence={ECO:0000269|PubMed:18287005, ECO:0000269|PubMed:29196633};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC         phosphocholine = 1-hexadecanoyl-2-(9Z-hexadecenoyl)-sn-glycero-3-
CC         phosphocholine + CoA; Xref=Rhea:RHEA:37207, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:61540, ChEBI:CHEBI:72998, ChEBI:CHEBI:74000;
CC         Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37208;
CC         Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-hexadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC         phosphoethanolamine = 1-hexadecanoyl-2-(9Z)-hexadecenoyl-sn-glycero-
CC         3-phosphoethanolamine + CoA; Xref=Rhea:RHEA:37419, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:61540, ChEBI:CHEBI:73004, ChEBI:CHEBI:73999;
CC         Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37420;
CC         Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-hexadecanoyl-sn-glycero-3-
CC         phosphocholine = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC         glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:35995,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:72998,
CC         ChEBI:CHEBI:73002; Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35996;
CC         Evidence={ECO:0000250|UniProtKB:Q6ZWT7};
CC   -!- ACTIVITY REGULATION: Partially inhibited by thimerosal.
CC       {ECO:0000250|UniProtKB:Q6ZWT7}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.3 uM for oleoyl-CoA (in the presence of LPC C16:0 as
CC         cosubstrate) {ECO:0000269|PubMed:18287005};
CC         KM=48.15 uM for oleoyl-CoA (in the presence of LPE C16:0 as
CC         cosubstrate) {ECO:0000269|PubMed:18287005};
CC         KM=7.9 uM for LPC C16:0 (in the presence of oleoyl-CoA as
CC         cosubstrate) {ECO:0000269|PubMed:18287005};
CC         KM=27.7 uM for LPE C16:0 (in the presence of oleoyl-CoA as
CC         cosubstrate) {ECO:0000269|PubMed:18287005};
CC         Vmax=24.24 nmol/min/mg enzyme with oleoyl-CoA and LPC C16:0 as
CC         substrates {ECO:0000269|PubMed:18287005};
CC         Vmax=26.3 nmol/min/mg enzyme with oleoyl-CoA and LPE C16:0 as
CC         substrates {ECO:0000269|PubMed:18287005};
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC       {ECO:0000269|PubMed:18287005}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:18287005}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8R3I2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R3I2-2; Sequence=VSP_022458;
CC       Name=3;
CC         IsoId=Q8R3I2-3; Sequence=VSP_022457, VSP_022459;
CC   -!- TISSUE SPECIFICITY: Highly expressed in epididymis, brain, testis, and
CC       ovary. {ECO:0000269|PubMed:18287005}.
CC   -!- INDUCTION: Increased during chondrogenic differentiation.
CC       {ECO:0000269|PubMed:29196633}.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27567.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB305046; BAF93902.1; -; mRNA.
DR   EMBL; AB297383; BAG12122.1; -; mRNA.
DR   EMBL; AK012931; BAB28556.1; -; mRNA.
DR   EMBL; AK031824; BAC27567.1; ALT_INIT; mRNA.
DR   EMBL; AK033106; BAC28154.1; -; mRNA.
DR   EMBL; AK034873; BAC28863.1; -; mRNA.
DR   EMBL; AK076045; BAC36144.1; -; mRNA.
DR   EMBL; BC025020; AAH25020.1; -; mRNA.
DR   CCDS; CCDS25845.1; -. [Q8R3I2-1]
DR   CCDS; CCDS36423.1; -. [Q8R3I2-2]
DR   RefSeq; NP_001076810.1; NM_001083341.1. [Q8R3I2-2]
DR   RefSeq; NP_080313.2; NM_026037.3. [Q8R3I2-1]
DR   RefSeq; XP_006515232.1; XM_006515169.2.
DR   RefSeq; XP_006515233.1; XM_006515170.3. [Q8R3I2-3]
DR   AlphaFoldDB; Q8R3I2; -.
DR   SMR; Q8R3I2; -.
DR   STRING; 10090.ENSMUSP00000106567; -.
DR   ChEMBL; CHEMBL1255156; -.
DR   SwissLipids; SLP:000000287; -.
DR   iPTMnet; Q8R3I2; -.
DR   PhosphoSitePlus; Q8R3I2; -.
DR   SwissPalm; Q8R3I2; -.
DR   MaxQB; Q8R3I2; -.
DR   PaxDb; Q8R3I2; -.
DR   PeptideAtlas; Q8R3I2; -.
DR   PRIDE; Q8R3I2; -.
DR   ProteomicsDB; 293418; -. [Q8R3I2-1]
DR   ProteomicsDB; 293419; -. [Q8R3I2-2]
DR   ProteomicsDB; 293420; -. [Q8R3I2-3]
DR   Antibodypedia; 12361; 79 antibodies from 19 providers.
DR   Ensembl; ENSMUST00000110942; ENSMUSP00000106567; ENSMUSG00000020646. [Q8R3I2-1]
DR   Ensembl; ENSMUST00000221952; ENSMUSP00000152348; ENSMUSG00000020646. [Q8R3I2-2]
DR   GeneID; 67216; -.
DR   KEGG; mmu:67216; -.
DR   UCSC; uc007neu.1; mouse. [Q8R3I2-1]
DR   UCSC; uc007nev.1; mouse. [Q8R3I2-2]
DR   UCSC; uc007nex.1; mouse. [Q8R3I2-3]
DR   CTD; 129642; -.
DR   MGI; MGI:1914466; Mboat2.
DR   VEuPathDB; HostDB:ENSMUSG00000020646; -.
DR   eggNOG; KOG2704; Eukaryota.
DR   GeneTree; ENSGT01030000234564; -.
DR   HOGENOM; CLU_011340_3_0_1; -.
DR   InParanoid; Q8R3I2; -.
DR   OMA; WAISIFE; -.
DR   PhylomeDB; Q8R3I2; -.
DR   TreeFam; TF314906; -.
DR   BRENDA; 2.3.1.23; 3474.
DR   Reactome; R-MMU-1482788; Acyl chain remodelling of PC.
DR   Reactome; R-MMU-1482839; Acyl chain remodelling of PE.
DR   UniPathway; UPA00085; -.
DR   BioGRID-ORCS; 67216; 2 hits in 74 CRISPR screens.
DR   ChiTaRS; Mboat2; mouse.
DR   PRO; PR:Q8R3I2; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q8R3I2; protein.
DR   Bgee; ENSMUSG00000020646; Expressed in umbilical cord and 245 other tissues.
DR   ExpressionAtlas; Q8R3I2; baseline and differential.
DR   Genevisible; Q8R3I2; MM.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA: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:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0106262; F:1-acylglycerophosphoethanolamine O-acyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0106263; F:1-acylglycerophosphoserine O-acyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0016746; F:acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR   GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IMP:UniProtKB.
DR   GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; IMP:UniProtKB.
DR   GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; ISS:UniProtKB.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0032330; P:regulation of chondrocyte differentiation; IMP:UniProtKB.
DR   InterPro; IPR004299; MBOAT_fam.
DR   Pfam; PF03062; MBOAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alternative splicing; Endoplasmic reticulum;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..519
FT                   /note="Lysophospholipid acyltransferase 2"
FT                   /id="PRO_0000273021"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        365..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        443..463
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          497..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        341
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        372
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..141
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_022457"
FT   VAR_SEQ         100..132
FT                   /note="QCCFVFALGYLSVCQITRVYIFDYGQYSADFSG -> H (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_022458"
FT   VAR_SEQ         142..150
FT                   /note="TSLAYEIHD -> MDNILLIFQ (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_022459"
FT   CONFLICT        28
FT                   /note="F -> S (in Ref. 3; BAB28556)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        40
FT                   /note="V -> L (in Ref. 3; BAB28556)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   519 AA;  58995 MW;  A21F3947612314EE CRC64;
     MATTSTTGST LLQPLSNAVQ LPIDQVNFVV CQLFALLAAV WFRTYLHSSK TSSFIRHVVA
     TLLGLYLAFF CFGWYALHFL VQSGISYCIM IIAGVESMQQ CCFVFALGYL SVCQITRVYI
     FDYGQYSADF SGPMMIITQK ITSLAYEIHD GMFRKDEELT PSQRGLAVRR MPSLLEYVSY
     TCNFMGILAG PLCSYKDYIA FIEGRASHVA QPSENGKDEQ HGKADPSPNA AVTEKLLVCG
     LSLLFHLTIS NMLPVEYNID EHFQATASWP TKATYLYVSL LAARPKYYFA WTLADAINNA
     AGFGFRGYDK NGVARWDLIS NLRIQQIEMS TSFKMFLDNW NIQTALWLKR VCYERATFSP
     TIQTFFLSAI WHGVYPGYYL TFLTGVLMTL AARAVRNNFR HYFLEPPQLK LFYDLITWVA
     TQITISYTVV PFVLLSIKPS FTFYSSWYYC LHVCSILVLL LLPVKKSQRR TSTQENVHLS
     QAKKFDERDN PLGQNSFSTM NNVCNQNRDT GSRHSSLTQ
 
 
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