ID   F1LT39_RAT              Unreviewed;       326 AA.
AC   F1LT39;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 2.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Acyltransferase {ECO:0000256|RuleBase:RU367023};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU367023};
GN   Name=Mogat3 {ECO:0000313|Ensembl:ENSRNOP00000046989.4,
GN   ECO:0000313|RGD:1592588};
GN   Synonyms=LOC685560 {ECO:0000313|RGD:1592588};
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:ENSRNOP00000046989.4, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000046989.4, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000046989.4,
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:ENSRNOP00000046989.4}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000046989.4};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_001064308.1; XM_001064308.4.
DR   RefSeq; XP_003752649.1; XM_003752601.3.
DR   AlphaFoldDB; F1LT39; -.
DR   STRING; 10116.ENSRNOP00000046989; -.
DR   PaxDb; 10116-ENSRNOP00000046989; -.
DR   Ensembl; ENSRNOT00000050456.5; ENSRNOP00000046989.4; ENSRNOG00000029211.5.
DR   GeneID; 685560; -.
DR   KEGG; rno:685560; -.
DR   AGR; RGD:1592588; -.
DR   CTD; 346606; -.
DR   RGD; 1592588; Mogat3.
DR   eggNOG; KOG0831; Eukaryota.
DR   GeneTree; ENSGT01030000234582; -.
DR   HOGENOM; CLU_023995_0_2_1; -.
DR   InParanoid; F1LT39; -.
DR   OMA; MAAWANF; -.
DR   OrthoDB; 601258at2759; -.
DR   TreeFam; TF314707; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000029211; Expressed in duodenum and 3 other cell types or tissues.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:RGD.
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:0004144; F:diacylglycerol O-acyltransferase activity; ISO:RGD.
DR   GO; GO:0006651; P:diacylglycerol biosynthetic process; IBA:GO_Central.
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:SF10; ACYLTRANSFERASE; 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..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367023"
SQ   SEQUENCE   326 AA;  37028 MW;  5BFEC759E897D9A0 CRC64;
     MEVPSSPLHR SLQVFAVLQW VFSFLGLALL CLVTLILASL GRAWTLVVLY LLWLYQDRHT
     PRMGGRRSAW VRNWAVWRYF RDYFPIKLVK TAELDPSQNY LFGFHPHGVL VVGAFSNFCT
     EATGFSHLFP GLKPHLLMLP CWFQVPLFRD YIMTSGLVSS DKASTSYLLS HPEGGRVAVL
     AVGGPLEALE AKPGTVSLRL RNQKGFVKLS LEHGASLVPV FSFGENDLFQ QFPNPPGSWV
     RRMQEALQRI LSVALPLFHG RLGLLIPFRV PIHTVVGAPI PVQRSPRPTR EQVNRLHELY
     VERLTQLFEE HKMRYGVPAD QHLVFI
//