ID   B2RZ21_RAT              Unreviewed;       334 AA.
AC   B2RZ21;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Acyltransferase {ECO:0000256|RuleBase:RU367023};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU367023};
GN   Name=Mogat2 {ECO:0000313|Ensembl:ENSRNOP00000036315.2,
GN   ECO:0000313|RGD:1598060};
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:ENSRNOP00000036315.2, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000036315.2, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000036315.2,
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:ENSRNOP00000036315.2}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000036315.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367023}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU367023}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the diacylglycerol acyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00005420, ECO:0000256|RuleBase:RU367023}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU367023}.
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DR   RefSeq; NP_001102906.2; NM_001109436.2.
DR   AlphaFoldDB; B2RZ21; -.
DR   STRING; 10116.ENSRNOP00000036315; -.
DR   PaxDb; 10116-ENSRNOP00000036315; -.
DR   Ensembl; ENSRNOT00000035774.3; ENSRNOP00000036315.2; ENSRNOG00000027228.3.
DR   GeneID; 681211; -.
DR   KEGG; rno:681211; -.
DR   UCSC; RGD:1598060; rat.
DR   AGR; RGD:1598060; -.
DR   CTD; 80168; -.
DR   RGD; 1598060; Mogat2.
DR   eggNOG; KOG0831; Eukaryota.
DR   GeneTree; ENSGT01030000234582; -.
DR   HOGENOM; CLU_023995_0_1_1; -.
DR   OMA; KVFKFTL; -.
DR   OrthoDB; 601258at2759; -.
DR   TreeFam; TF314707; -.
DR   Reactome; R-RNO-75109; Triglyceride biosynthesis.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000027228; Expressed in duodenum and 14 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; ISO:RGD.
DR   GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; ISO:RGD.
DR   GO; GO:0016407; F:acetyltransferase activity; ISO:RGD.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006651; P:diacylglycerol biosynthetic process; ISO:RGD.
DR   GO; GO:0050892; P:intestinal absorption; ISO:RGD.
DR   GO; GO:0006629; P:lipid metabolic process; ISO:RGD.
DR   GO; GO:0006640; P:monoacylglycerol biosynthetic process; ISO:RGD.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; ISO:RGD.
DR   CDD; cd07987; LPLAT_MGAT-like; 1.
DR   InterPro; IPR007130; DAGAT.
DR   PANTHER; PTHR12317:SF74; 2-ACYLGLYCEROL O-ACYLTRANSFERASE 2; 1.
DR   PANTHER; PTHR12317; DIACYLGLYCEROL O-ACYLTRANSFERASE; 1.
DR   Pfam; PF03982; DAGAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU367023};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367023};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU367023};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU367023}.
FT   TRANSMEM        20..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367023"
SQ   SEQUENCE   334 AA;  38553 MW;  7F2F8E29BB3826D9 CRC64;
     MVEFAPLLVP WERRLQTFAV LQWVFSFLAL AQLCIFIFIG LLFTRFWLFS VLYATWWYLD
     WDRPRQGGRP IQFFRRMAIW KYMKDFFPVS LVKTAELDPS RNYIAGFHPH GVLAAGAFLN
     LCTESTGFTS LFPGIRSYLM MLTVWFRAPI FRDYIMSGGL VSSEKVSADH ILSRKGGGNL
     LAIIVGGAQE ALDARPGAYR LLLKNRKGFI RLALTHGAAL VPIFSFGENN LFNQVENTPG
     TWLRWIQNWL QKIMGISLPL FHGRGVFQYS FGLVPFRQPI TTVVGKPIEV QMIPHPSEEE
     VNRLHQLYIK ELCKLFEEHK LKFNVPEDQH LEFC
//