ID G0MMF1_CAEBE Unreviewed; 515 AA.
AC G0MMF1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=CBN-ACL-5 protein {ECO:0000313|EMBL:EGT37449.1};
GN Name=Cbn-acl-5 {ECO:0000313|EMBL:EGT37449.1};
GN ORFNames=CAEBREN_01515 {ECO:0000313|EMBL:EGT37449.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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}.
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; GL379802; EGT37449.1; -; Genomic_DNA.
DR AlphaFoldDB; G0MMF1; -.
DR STRING; 135651.G0MMF1; -.
DR EnsemblMetazoa; CBN01515.1; CBN01515.1; WBGene00140240.
DR eggNOG; KOG2898; Eukaryota.
DR HOGENOM; CLU_031080_0_1_1; -.
DR InParanoid; G0MMF1; -.
DR OMA; WFERNEM; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR23063; PHOSPHOLIPID ACYLTRANSFERASE; 1.
DR PANTHER; PTHR23063:SF53; PLSC DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068};
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 152..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 239..350
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 48..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 59557 MW; BD664378031F40C8 CRC64;
MIFLLFWFLI LLLIYLAITG KTLGFRQLYV STLIRIFEWG ATLNVEEEWD GEEDDESTTT
TSQKKKKMRR SSSCSDLGTI NREKSEIIDA KLRETNIPES KKTTVSVLVD DTLDFITAGM
EAVIEDQVTN RFSAAQLPTW NFLSRTKYSF HFFNWQLTLL WIGGFIFRYL ILVPFRCALF
FIAIILMIIC ASIIGMAPDP KCRKVLNRRC MLMCMRIYSR AFSSVIRFHD KENRANNGGI
CVANHTSPID VMVLSCDNCY AMIGQKQGGF LGFLQNTLSR SEHHIWFERG EAADRKQVMD
RMREHVEDEN KLPIIIFPEG TCINNTSVMM FKKGSFEIGS TIYPIAVKYD TRLTDAFWNS
SAQSYGRYLW SMMTSWAIIC DVWYLPPMTR GDEEDSIGFA KRVKRAIAKK GGLIDLEWDG
ALKREKVSTK LVALQQKLYY ERLARTTTIN NMLEENETSD ILSIMQEITE EERNELLKQI
DEQDDDDEMI RKITSIKPRR SRIGNENETP KSKTE
//
