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Database: UniProt
Entry: H2NBL3_PONAB
LinkDB: H2NBL3_PONAB
Original site: H2NBL3_PONAB 
ID   H2NBL3_PONAB            Unreviewed;       828 AA.
AC   H2NBL3; A0A2J8W758;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase 1, mitochondrial {ECO:0000256|ARBA:ARBA00017577, ECO:0000256|PIRNR:PIRNR000437};
DE            EC=2.3.1.15 {ECO:0000256|ARBA:ARBA00013113, ECO:0000256|PIRNR:PIRNR000437};
GN   Name=GPAM {ECO:0000313|Ensembl:ENSPPYP00000003091.3};
GN   ORFNames=CR201_G0012853 {ECO:0000313|EMBL:PNJ65609.1};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000003091.3, ECO:0000313|Proteomes:UP000001595};
RN   [1] {ECO:0000313|Ensembl:ENSPPYP00000003091.3, ECO:0000313|Proteomes:UP000001595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilson R.K., Mardis E.;
RT   "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PNJ65609.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Susie {ECO:0000313|EMBL:PNJ65609.1};
RA   Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA   Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA   Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA   Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA   Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT   "High-resolution comparative analysis of great ape genomes.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSPPYP00000003091.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position of
CC       glycerol-3-phosphate, an essential step in glycerolipids biosynthesis
CC       such as triglycerides, phosphatidic acids and lysophosphatidic acids.
CC       {ECO:0000256|ARBA:ARBA00023435}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + sn-glycerol 3-phosphate = 1-(9Z-
CC         octadecenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37199,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:57597,
CC         ChEBI:CHEBI:74544; Evidence={ECO:0000256|ARBA:ARBA00023362};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37200;
CC         Evidence={ECO:0000256|ARBA:ARBA00023362};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoyl-CoA + sn-glycerol 3-phosphate = 1-
CC         (9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:37203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:74547;
CC         Evidence={ECO:0000256|ARBA:ARBA00023344};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37204;
CC         Evidence={ECO:0000256|ARBA:ARBA00023344};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol) + an acyl-CoA =
CC         1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + CoA;
CC         Xref=Rhea:RHEA:33203, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342,
CC         ChEBI:CHEBI:64716, ChEBI:CHEBI:64840;
CC         Evidence={ECO:0000256|ARBA:ARBA00023355};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33204;
CC         Evidence={ECO:0000256|ARBA:ARBA00023355};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acyl-CoA + sn-glycerol 3-phosphate = a 1-acyl-sn-glycero-3-
CC         phosphate + CoA; Xref=Rhea:RHEA:15325, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57597, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342; EC=2.3.1.15;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000437};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dodecanoyl-CoA + sn-glycerol 3-phosphate = 1-dodecanoyl-sn-
CC         glycerol 3-phosphate + CoA; Xref=Rhea:RHEA:35727, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57375, ChEBI:CHEBI:57597, ChEBI:CHEBI:72682;
CC         Evidence={ECO:0000256|ARBA:ARBA00023335};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35728;
CC         Evidence={ECO:0000256|ARBA:ARBA00023335};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-CoA + sn-glycerol 3-phosphate = 1-hexadecanoyl-
CC         sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35723,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:57518,
CC         ChEBI:CHEBI:57597; Evidence={ECO:0000256|ARBA:ARBA00023405};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35724;
CC         Evidence={ECO:0000256|ARBA:ARBA00023405};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=octadecanoyl-CoA + sn-glycerol 3-phosphate = 1-octadecanoyl-
CC         sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37195,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:57597,
CC         ChEBI:CHEBI:74565; Evidence={ECO:0000256|ARBA:ARBA00023374};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37196;
CC         Evidence={ECO:0000256|ARBA:ARBA00023374};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC       {ECO:0000256|ARBA:ARBA00004765, ECO:0000256|PIRNR:PIRNR000437}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane
CC       protein {ECO:0000256|ARBA:ARBA00004374}.
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC       {ECO:0000256|ARBA:ARBA00007937, ECO:0000256|PIRNR:PIRNR000437}.
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DR   EMBL; NDHI03003398; PNJ65609.1; -; Genomic_DNA.
DR   Ensembl; ENSPPYT00000003197.3; ENSPPYP00000003091.3; ENSPPYG00000002655.3.
DR   eggNOG; KOG3729; Eukaryota.
DR   GeneTree; ENSGT00520000055570; -.
DR   HOGENOM; CLU_016910_1_1_1; -.
DR   OMA; RCKHTNE; -.
DR   TreeFam; TF313360; -.
DR   UniPathway; UPA00557; UER00612.
DR   Proteomes; UP000001595; Chromosome 10.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050798; P:activated T cell proliferation; IEA:Ensembl.
DR   GO; GO:0006924; P:activation-induced cell death of T cells; IEA:Ensembl.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; IEA:Ensembl.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR   GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl.
DR   GO; GO:0070236; P:negative regulation of activation-induced cell death of T cells; IEA:Ensembl.
DR   GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:Ensembl.
DR   GO; GO:0055091; P:phospholipid homeostasis; IEA:Ensembl.
DR   GO; GO:0042104; P:positive regulation of activated T cell proliferation; IEA:Ensembl.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0001817; P:regulation of cytokine production; IEA:Ensembl.
DR   GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IEA:Ensembl.
DR   CDD; cd07993; LPLAT_DHAPAT-like; 1.
DR   InterPro; IPR022284; GPAT/DHAPAT.
DR   InterPro; IPR045520; GPAT/DHAPAT_C.
DR   InterPro; IPR041728; GPAT/DHAPAT_LPLAT.
DR   InterPro; IPR028354; GPAT_PlsB.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR12563:SF16; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF19277; GPAT_C; 1.
DR   PIRSF; PIRSF500064; GPAT; 1.
DR   PIRSF; PIRSF000437; GPAT_DHAPAT; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|PIRNR:PIRNR000437};
KW   Lipid biosynthesis {ECO:0000256|PIRNR:PIRNR000437};
KW   Lipid metabolism {ECO:0000256|PIRNR:PIRNR000437};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR000437};
KW   Mitochondrion {ECO:0000256|PIRNR:PIRNR000437};
KW   Phospholipid biosynthesis {ECO:0000256|PIRNR:PIRNR000437};
KW   Phospholipid metabolism {ECO:0000256|PIRNR:PIRNR000437};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000437};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          224..357
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          435..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        439..455
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   828 AA;  93758 MW;  1B542B361C8A660C CRC64;
     MDESALTLGT IDVSYLPNSS EYSVGRCKHT SEEWGECGFR PTVFRSATLK WKESLMSRKR
     PFVGRCCYSC TPQSWDKFFN PSIPSLGLRN VIYINETHTR HRGWLARRLS YVLFIQERDV
     HKGMFATNVI ENVLNSSRVQ EAIAEVAAEL NPDGSAQQQS KAVNKVKKKA KRILQEMVAT
     VSPAMIRLTG WVLLKLFNSF FWNIQIHKGQ LEMVKAATET NLPLLFLPVH RSHIDYLLLT
     FILFCHNIKA PYIASGNNLN IPIFSTLIHK LGGFFIRRRL DETPDGRKDV LYRALLHGHI
     VELLRQQQFL EIFLEGTRSR SGKTSCARAG LLSVVVDTLS TNVIPDILII PVGISYDRII
     EGHYNGEQLG KPKKNESLWS VARGVIRMLR KNYGCVRVDF AQPFSLKEYL ESQSQKPVSA
     TLSLEQALLP AILPSRPSDA ADEGRDTSIN ESRNATDESL RRRLIANLAE HILFTASKSC
     AIMSTHIVAC LLLYRHRQGI DLSTLVEDFF VMKEEVLARD FDLGFSGNSE DVVMHAIQLL
     GNCVTITHTS RNDEFFITPS TTVPSVFELN FYSNGVLHVF IMEAIIACSL YAVLNKRGLG
     GPTSTPPNLI SQEQLVRKAA SLCYLLSNEG TISLPCQTFY QVCHETVGKF IQYGILTVAE
     HDDQEDISPS LAEQQWDKKL PEPLSWRSDE EDEDSDFGEE QRDCYLKVSQ SKEHQQFITF
     LQRLLGPLLE AYSSAAIFVH NFSGPVPEPE YLQKLHKYLI TRTERNVAVY AESATYCLVK
     NAVKMFKDIG VFKETKQKRV SVLELSSTFL PQCNRQKLLE YILSFVVL
//
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