ID A0A150GZF5_GONPE Unreviewed; 801 AA.
AC A0A150GZF5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=diacylglycerol O-acyltransferase {ECO:0000256|ARBA:ARBA00013244};
DE EC=2.3.1.20 {ECO:0000256|ARBA:ARBA00013244};
GN ORFNames=GPECTOR_3g256 {ECO:0000313|EMBL:KXZ55102.1};
OS Gonium pectorale (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ55102.1, ECO:0000313|Proteomes:UP000075714};
RN [1] {ECO:0000313|Proteomes:UP000075714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX PubMed=27102219; DOI=10.1038/ncomms11370;
RA Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT "The Gonium pectorale genome demonstrates co-option of cell cycle
RT regulation during the evolution of multicellularity.";
RL Nat. Commun. 7:11370-11370(2016).
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004771}.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC Sterol o-acyltransferase subfamily. {ECO:0000256|ARBA:ARBA00009010}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXZ55102.1}.
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 EMBL; LSYV01000004; KXZ55102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150GZF5; -.
DR STRING; 33097.A0A150GZF5; -.
DR OrthoDB; 9612at2759; -.
DR UniPathway; UPA00282; -.
DR Proteomes; UP000075714; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00821; PH; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR004299; MBOAT_fam.
DR InterPro; IPR014371; Oat_ACAT_DAG_ARE.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR10408:SF7; DIACYLGLYCEROL O-ACYLTRANSFERASE 1; 1.
DR PANTHER; PTHR10408; STEROL O-ACYLTRANSFERASE; 1.
DR Pfam; PF03062; MBOAT; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000075714};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 373..391
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 489..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 518..535
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 609..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 663..681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 732..750
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..152
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 158..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 13..47
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 214..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 86436 MW; C912DC73CAF6DDA9 CRC64;
MVGIPFLGRA GRRGRTDEDR SELERLHKEL EQLRAANEQL KEQLSARSVH LGEYLYKWKT
VALPLLGSEW ELRYLVLSGT NLSYYRSARD TAFSPREEIS VLSCFVSWEG LRSGRYWTFS
VSDCGGALLV RLAALSRDAA ERWLAALEAA GCARDDSLVA PAGPKGSRES RTPSSRDVRD
LARSLSAPAP LPPGRAAAAA AAAAAAAAQP PERQAGARRR RQERQPLQAL RLAEEGDGSS
GSGATGSDSG TSGAALARAP SGPPAGRSSA ATPSSPSAAP AGAAPPPSSP SPAASSAVAV
SASAATAFAS TSTASAAPPA APARRSLGSR PGAGHGHGHG PERGPMRGST PVHTSSRFSL
LSSERVWHEK HTGLYNLALI ILVLTNFRLA LENALKYGWR LNPVRLAADM LAGRGGGPGG
VGGGLVNVPL VCCYPCLLAA SLLSLGIERA GHALLESELR LRETLSKRRD LSEAAAAAAL
ASRARAHEWL LFLLNVATTC TVIGLPWAVI SLTRAEPVSG GILITLSMVL WMKLVSYHHC
CFDLRAARRC GEVRPGERGC PDTPAEDWGP LARYPENLTL RNLLYFLAVP TLTYQVNFPR
SRSLRGRWLL RRCFELAITL TAMAILVGQY IQPTVSNSLA PLRQMDLPRV AERVLKLALP
STYAWLLGFY GLFHLWLNVL AELTQFGDRE FYKDWWNAGT VGEYWKLWNM PVHKWLLRHV
YFPAIRAGTP RFHAVLLTFF VSAVFHELVL GVPLHLVRLW AFCGIMFQVP LIMATEKLQK
RLNRAELAVN GTIGAGASAL I
//
