ID A0A2B4S4T0_STYPI Unreviewed; 840 AA.
AC A0A2B4S4T0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 08-NOV-2023, entry version 21.
DE SubName: Full=Glycerol-3-phosphate acyltransferase 1, mitochondrial {ECO:0000313|EMBL:PFX25704.1};
GN Name=Gpam {ECO:0000313|EMBL:PFX25704.1};
GN ORFNames=AWC38_SpisGene9640 {ECO:0000313|EMBL:PFX25704.1};
OS Stylophora pistillata (Smooth cauliflower coral).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Pocilloporidae; Stylophora.
OX NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX25704.1, ECO:0000313|Proteomes:UP000225706};
RN [1] {ECO:0000313|Proteomes:UP000225706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA Tambutte S., Allemand D., Aranda M.;
RT "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT digitifera provides evidence for extensive differences between species of
RT corals.";
RL bioRxiv 0:0-0(2017).
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937}.
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:PFX25704.1}.
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DR EMBL; LSMT01000144; PFX25704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B4S4T0; -.
DR STRING; 50429.A0A2B4S4T0; -.
DR EnsemblMetazoa; XM_022934782.1; XP_022790517.1; LOC111330003.
DR OrthoDB; 2874405at2759; -.
DR Proteomes; UP000225706; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0044255; P:cellular lipid metabolic process; IEA:InterPro.
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; IPR002123; Plipid/glycerol_acylTrfase.
DR PANTHER; PTHR12563:SF23; BCDNA.GH07066; 1.
DR PANTHER; PTHR12563; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF19277; GPAT_C; 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:PFX25704.1}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PFX25704.1}.
FT DOMAIN 255..386
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 840 AA; 95616 MW; D208EE088D467FBF CRC64;
MDPKLEEVFK KWEAHSSGPS RAANDEESQR QREERQRKFR DNLEAPFRKP SRQRPRKRKS
KREDFSFKPL TEVKFSVPHA VIPSMYKRKR PLMGEACDRC CRESKILYEE GKVSWGIRNV
LSMDLFRKQN FLKRSFCHIA FVWNCDISHQ YPDVKKDVLH SARVKTSILS PAMQEPPSSG
QDIKTVENER WKRINTAEKK AVNILNGMAA VVYRKFVRFT TWFLFKLFKR LLFSIQIQRG
QIDILKEASQ DDKPLVFLPL HKSHMDYILL TFVLVTCDIK VPHVAAGDNL NIPFLGWILR
HLGGFFIKRK LDHSSGKDEL YKCILQEYVE QLLQNGQYLV FYIEGSRSRS GKAMVPKSGL
LSLVVNSVTE GVVPDVNVVP VNISYEKVVD SGYTRELLGE LKTPESFWST LKSIWHVIGT
RYGNVRLDFG QPFSLQEFSQ AMDQSQPMQE FAAKSLARAS DISSPKSSLV RNHSEVSLSE
LGDDKCFTLT KALGYHAIRD SANCSAVMST NMVAFLLMNS HRKGATFQEL CTSFDWLYRE
ITSRGRDVGF SGKTAAVVSH ALRLLDDDVT STESRTGPQK DTVEQVQPKN GLPHILNLAF
YSNQVVSVFS LDAVLACAII AAAEDSESFD INDIEGQKII TQTSIVGKAK HLCDVLQREF
ILIPPCVSLE SALTEGLDKF TSSETIKIIA ESNSTSSRGS QWGWDDDDEY MREFDVTEIE
YKLTNVDELL KKLKFLKSVV APLIESYWVA ACGLLWLRNQ TFSDTEFLTA LHSCAKERVN
EGVTMFPESC SLEPFRNAVR IFKEWKVIQV NAESRVALCD AYNSEDALFD VIEDINQFKL
//