ID   S4R7T3_PETMA            Unreviewed;       456 AA.
AC   S4R7T3;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Glycerol-3-phosphate acyltransferase 4 {ECO:0000313|Ensembl:ENSPMAP00000001263.1};
OS   Petromyzon marinus (Sea lamprey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC   Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX   NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000001263.1, ECO:0000313|Proteomes:UP000245300};
RN   [1] {ECO:0000313|Ensembl:ENSPMAP00000001263.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   AlphaFoldDB; S4R7T3; -.
DR   STRING; 7757.ENSPMAP00000001263; -.
DR   Ensembl; ENSPMAT00000001268.1; ENSPMAP00000001263.1; ENSPMAG00000001118.1.
DR   GeneTree; ENSGT01030000234574; -.
DR   HOGENOM; CLU_031080_0_1_1; -.
DR   OMA; QIFQWAT; -.
DR   Proteomes; UP000245300; Unplaced.
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:SF37; GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE 4; 1.
DR   PANTHER; PTHR23063; PHOSPHOLIPID ACYLTRANSFERASE; 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:UP000245300};
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        12..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        152..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          242..353
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   456 AA;  51190 MW;  881824226523EFB0 CRC64;
     LLGWEAPGLQ GALVAALGLS LSVWLTILLV FIVVPATFGI SFGIRTIYMR SLLKIFEWAT
     LRIERGIKES KHRAYNTNSN GILVKVEESS LGEEIAKGRL AVGGEPAPEF GLADTFYFCR
     KGLEAIVEDD VTKRFTAEEI ESWNLLTRTN NYFQYISVRL TVLWGLGVAV RYGFLLPLRV
     TLAFIGIGWL VVSTTLLGYF PEGKMKEWLS DQVHLMSMRI CARALTAIIS YHNRENMPKK
     GGICVANHTS PIDVIILAND RCYAMVGQKH GGLMGVIQRA IVKACPHVFF ERSEIKDRNL
     VTKRLSEHVA DKNKLPILIF PEGTCINNTS VMMFKKGSFE IQGTIYPVAI KYDPQFGDAF
     WNSSKYGMVN YLLRMMSSWA IVCNVWYLPP MTRREDEDAV QFANRVKAEI ASQGGLVDLL
     WDGGLKRGKV KNTFKEEQQK QYSKTICGEP SEQGTS
//