ID A0A0V1A052_9BILA Unreviewed; 797 AA.
AC A0A0V1A052;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Glycerol-3-phosphate acyltransferase 3 {ECO:0000313|EMBL:KRY18207.1};
DE Flags: Fragment;
GN Name=ZDHHC16 {ECO:0000313|EMBL:KRY18207.1};
GN ORFNames=T12_158 {ECO:0000313|EMBL:KRY18207.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY18207.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY18207.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY18207.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KRY18207.1}.
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DR EMBL; JYDQ01000049; KRY18203.1; -; Genomic_DNA.
DR EMBL; JYDQ01000049; KRY18207.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1A052; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008374; F:O-acyltransferase activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR001958; Tet-R_TetA/multi-R_MdtG-like.
DR PANTHER; PTHR23063:SF2; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE 4, ISOFORM D-RELATED; 1.
DR PANTHER; PTHR23063; PHOSPHOLIPID ACYLTRANSFERASE; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF07690; MFS_1; 1.
DR PRINTS; PR01035; TCRTETA.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:KRY18207.1};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KRY18207.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 24..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 286..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..534
FT /note="Major facilitator superfamily (MFS) profile"
FT /evidence="ECO:0000259|PROSITE:PS50850"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY18207.1"
SQ SEQUENCE 797 AA; 89968 MW; 16D0AAB2B79AA0AC CRC64;
LYEILSNTIK SYCQAIGLPD NERLISVFFG GALGSLFSGL QFISSPWFGA MSDIYGRKWM
LLISLAGTFT SYLLWSCASS FGIFMLSRII GGLSKASTSI SIAIVADLFP PEERGKGMAF
VGLAFSSGFV IGPTLGAIAA YWNRMKTISI FTPAYLALLI TSIEFLWVWI FLKETLPEVK
KKKHKNLVFP QFFSYINPAS LFVFKPLEKR IEQKVHQKIK RTGLVYFLFL FIYSGLEFTL
TFFAHERFNF NSMQQGKMFF YIGIIMIIIQ GGYVRKIKTE KQKATASKGI TVSLISFLAI
SLAWNVYYFY GSLTLYSLAS GIVVPCLTTE VSSQVSPTEK GSVLGIFRAL GSLARAIGPV
CASTARNPRA EWVHWNIISS SQIYEKCDSS DEEFDENHER ASIFLNGSID AKQNHLIERE
ASEHLINKMY EEPSGCAVTT VVEDALDFTK AGIEAIIEDD VTSRFSAAEL TSWNLLTRSS
YGYHLLNWKL GLLWGFGLII RYFVIFPINL TILVIALFIL IATGCTITFI RDEEKKRKIS
RSMSLVCYRI LLQACSGVVT FHNRHNSAKP GGICVANHTS PIDALVLACD NCYAFVGQRQ
GGFLGFIQNS LLKLDAHIWF DREEGSDKLL VRNRLREHVQ DHSKLPILIF PEGTCINNTS
VMMFRKGSFE VGDVIYPVAI KYDARFGDAF WNSSKVSYFE YLMMMMTSWA LVCDVWYLPP
MVRQDGEDAI AFASRVKKAI AKAGGLVELE WDGQLKRHFV KSEVIDKQRQ KYSERIMRVQ
LDDDVSHMLH CKNSEEY
//
