ID   G3V7N6_RAT              Unreviewed;       473 AA.
AC   G3V7N6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Lysophospholipid acyltransferase 7 {ECO:0000256|ARBA:ARBA00039722};
DE   AltName: Full=Leukocyte receptor cluster member 4 {ECO:0000256|ARBA:ARBA00041667};
DE   AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 7 {ECO:0000256|ARBA:ARBA00041626};
GN   Name=Mboat7 {ECO:0000313|Ensembl:ENSRNOP00000069855.1,
GN   ECO:0000313|RGD:1306945};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000069855.1, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000069855.1, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069855.1,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000069855.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069855.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00035964};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36000;
CC         Evidence={ECO:0000256|ARBA:ARBA00035964};
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:0000256|ARBA:ARBA00037016};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36836;
CC         Evidence={ECO:0000256|ARBA:ARBA00037016};
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:0000256|ARBA:ARBA00035860};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37016;
CC         Evidence={ECO:0000256|ARBA:ARBA00035860};
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:0000256|ARBA:ARBA00036730};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33196;
CC         Evidence={ECO:0000256|ARBA:ARBA00036730};
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00005074}.
CC   -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00010323}.
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DR   RefSeq; NP_001300869.1; NM_001313940.1.
DR   AlphaFoldDB; G3V7N6; -.
DR   STRING; 10116.ENSRNOP00000069855; -.
DR   PaxDb; 10116-ENSRNOP00000017002; -.
DR   Ensembl; ENSRNOT00000090873.2; ENSRNOP00000069855.1; ENSRNOG00000052600.2.
DR   GeneID; 308309; -.
DR   AGR; RGD:1306945; -.
DR   CTD; 79143; -.
DR   RGD; 1306945; Mboat7.
DR   eggNOG; KOG2706; Eukaryota.
DR   GeneTree; ENSGT01030000234564; -.
DR   HOGENOM; CLU_011340_1_1_1; -.
DR   OMA; TNMIQML; -.
DR   OrthoDB; 2874769at2759; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000052600; Expressed in frontal cortex and 18 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:RGD.
DR   GO; GO:0071617; F:lysophospholipid acyltransferase activity; ISO:RGD.
DR   GO; GO:0008374; F:O-acyltransferase activity; ISO:RGD.
DR   GO; GO:0021819; P:layer formation in cerebral cortex; ISO:RGD.
DR   GO; GO:0030258; P:lipid modification; IBA:GO_Central.
DR   GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; ISO:RGD.
DR   GO; GO:0036149; P:phosphatidylinositol acyl-chain remodeling; ISO:RGD.
DR   GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISO:RGD.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; ISO:RGD.
DR   GO; GO:0090207; P:regulation of triglyceride metabolic process; ISO:RGD.
DR   GO; GO:0021591; P:ventricular system development; ISO:RGD.
DR   InterPro; IPR004299; MBOAT_fam.
DR   PANTHER; PTHR13906:SF16; LYSOPHOSPHOLIPID ACYLTRANSFERASE 7; 1.
DR   PANTHER; PTHR13906; PORCUPINE; 1.
DR   Pfam; PF03062; MBOAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ   SEQUENCE   473 AA;  53380 MW;  D39F0D7C8D55236B CRC64;
     MTPEEWTYLM VLLISIPVGF LFKKAGPGLK RWGAAAVGLG LTLFTCGPHS LHSLITILGT
     WALIQAQPCS CHALALAWTF SYLLFFRALS LLGLPTPTPF TNAVQLLLTL KLVSLASEVQ
     DLHLAQRKEM ASGFSKEPTL GLLPDVPSLM ETLSYSYCYV GIMTGPFFRY RTYLDWLEQP
     FPEAVPSLRP LLRRAWPAPL FGLLFLLSSH LFPLEAVRED AFYARPLPTR LFYMIPVFFA
     FRMRFYVAWI AAECGCIAAG FGAYPVAAKA RAGGGPTLQC PPPSSPEIAA SLEYDYEAIR
     NIDCYGTDFC VRVRDGMRYW NMTVQWWLAQ YIYKSAPFRS YVLRSAWTML LSAYWHGLHP
     GYYLSFMTIP LCLAAEGYLE SALRRHLSPG GQKAWDWFHW FLKMRAYDYM CMGFVLLSMG
     DTLRYWASIY FWVHFLALAC LGLGLALGGG SPSKRKTPSQ ATTSQAKEKL REE
//