ID A0A2I2YGK6_GORGO Unreviewed; 544 AA.
AC A0A2I2YGK6;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Lysophosphatidylcholine acyltransferase 2 {ECO:0000313|Ensembl:ENSGGOP00000034059.1};
GN Name=LPCAT2 {ECO:0000313|Ensembl:ENSGGOP00000034059.1};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000034059.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000034059.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000034059.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000034059.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000256|ARBA:ARBA00005074}.
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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DR EMBL; CABD030101135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030101136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030101137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004057710.1; XM_004057662.2.
DR AlphaFoldDB; A0A2I2YGK6; -.
DR STRING; 9593.ENSGGOP00000034059; -.
DR Ensembl; ENSGGOT00000059640.1; ENSGGOP00000034059.1; ENSGGOG00000005144.3.
DR GeneID; 101148534; -.
DR KEGG; ggo:101148534; -.
DR CTD; 54947; -.
DR GeneTree; ENSGT01030000234574; -.
DR InParanoid; A0A2I2YGK6; -.
DR OMA; FLYHKSE; -.
DR OrthoDB; 5471865at2759; -.
DR UniPathway; UPA00085; -.
DR Proteomes; UP000001519; Chromosome 16.
DR Bgee; ENSGGOG00000005144; Expressed in frontal cortex and 6 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0005795; C:Golgi stack; IEA:Ensembl.
DR GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:Ensembl.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:Ensembl.
DR GO; GO:0047192; F:1-alkylglycerophosphocholine O-acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IBA:GO_Central.
DR GO; GO:0061024; P:membrane organization; IEA:Ensembl.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IEA:Ensembl.
DR GO; GO:0006663; P:platelet activating factor biosynthetic process; IEA:Ensembl.
DR CDD; cd00051; EFh; 2.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR23063:SF21; LYSOPHOSPHATIDYLCHOLINE ACYLTRANSFERASE 2; 1.
DR PANTHER; PTHR23063; PHOSPHOLIPID ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF13202; EF-hand_5; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR PRINTS; PR00450; RECOVERIN.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 58..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 391..426
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 428..463
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 518..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 60196 MW; DD4CEEA59A159295 CRC64;
MSRCAQAAAV AATVPGAGVG NVGLRPPMVP RQASFFPPPV PNPFVQQTQI GSARRVQIFL
LGIILLPIRV LLVVLILLLA WPFAAISTVC CPEKLTHPIT GWRRKITQTA LKFLGRAMFF
SMGFIVAVKG KIASPLEAPV FVAAPHSTFF DGIACVVAGL PSMVSRNENA QVPLIGRLLR
AVQPVLVSRV DPDSRKNTIN EIIKRATSGG EWPQILVFPE GTCTNRSCLI TFKPGAFIPG
VPVQPVLLRY PNKLDTVTWT WQGYTFIQLC MLTFCQLFTK VEVEFMPVQV PNDEEKNDPV
LFANKVRNLM AEALGIPVTD HTYEDCRLMI SAGQLTLPME AGLVEFTKIS RKLKLDWDGV
RKHLDEYASI ASSSKGGRIG IEEFAKYLKL PVSDVLRQLF ALFDRNHDGS IDFREYVIGL
AVLCNPSNTE EIIQVAFKLF DVDEDGYITE EEFSTILQAS LGVPDLDVSG LFKEIAQGDS
ISYEEFKSFA LKHPEYAKIF TTYLDLQTCH VFSLPKEVQT TPSTASNKVS PEKHEESTSD
KKDD
//
