GenomeNet

Database: UniProt
Entry: A0A103YLQ4_CYNCS
LinkDB: A0A103YLQ4_CYNCS
Original site: A0A103YLQ4_CYNCS 
ID   A0A103YLQ4_CYNCS        Unreviewed;       420 AA.
AC   A0A103YLQ4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   22-FEB-2023, entry version 20.
DE   RecName: Full=1-acylglycerol-3-phosphate O-acyltransferase {ECO:0000256|ARBA:ARBA00013211};
DE            EC=2.3.1.51 {ECO:0000256|ARBA:ARBA00013211};
GN   ORFNames=Ccrd_010251 {ECO:0000313|EMBL:KVI11335.1};
OS   Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC   Carduinae; Cynara.
OX   NCBI_TaxID=59895 {ECO:0000313|EMBL:KVI11335.1, ECO:0000313|Proteomes:UP000243975};
RN   [1] {ECO:0000313|EMBL:KVI11335.1, ECO:0000313|Proteomes:UP000243975}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2C {ECO:0000313|EMBL:KVI11335.1};
RX   PubMed=26786968; DOI=10.1038/srep19427;
RA   Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA   Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA   Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT   "The genome sequence of the outbreeding globe artichoke constructed de novo
RT   incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL   Sci. Rep. 6:19427-19427(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC         sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC         ChEBI:CHEBI:58608; EC=2.3.1.51;
CC         Evidence={ECO:0000256|ARBA:ARBA00001141};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004728}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}.
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:KVI11335.1}.
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; LEKV01000326; KVI11335.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A103YLQ4; -.
DR   STRING; 59895.A0A103YLQ4; -.
DR   EnsemblPlants; KVI11335; KVI11335; Ccrd_010251.
DR   Gramene; KVI11335; KVI11335; Ccrd_010251.
DR   UniPathway; UPA00557; UER00613.
DR   Proteomes; UP000243975; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR   InterPro; IPR032098; Acyltransf_C.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR10983:SF67; 1-ACYLGLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE; 1.
DR   Pfam; PF16076; Acyltransf_C; 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   ECO:0000313|EMBL:KVI11335.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243975};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        77..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        345..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          121..243
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   UNSURE          99
FT                   /note="I or L"
FT                   /evidence="ECO:0000313|EMBL:KVI11335.1"
SQ   SEQUENCE   420 AA;  47209 MW;  30F8CA5652EBDFB3 CRC64;
     MAIAAAVVIV PIGVLFFVSG LIVNLIQALI FVIVRPFSKS IFRRINRMVA ELLWLELVWI
     VDWWAGVKVN LYTDPETLRM MGMLYTAFII VTLLRVKNLL LLTCCTIFSP NPVLFPGKEH
     ALVIANHKSD IDWLIGWVFA QRSGCLGSTL AVMKKSSKFL PVIGWSMWFS EYLFLERSWA
     KDESTLKSGL QSLKDYPQPF WLALFVEGTR FTKAKLLAAQ EYASSMGLPV PRNVLIPRTK
     GFVTSVSQMR SFVPAIIDMT VAIPKDSTPP TMLRLFKGQS SVVSLLDLKF WLCKDEIHVK
     VTRHSMKDLP ESDEAVAQWC KDKFIVKDDV LDQHKIADAF PDSELVVVSW ACLLVFGTFK
     FLQWSNLLSS WKGLTFAAVG LATVTILMQI LIQFSQAEHS TPAKVAPVLS SNGTVREKSQ
//
DBGET integrated database retrieval system