ID A0A2G8JUP9_STIJA Unreviewed; 392 AA.
AC A0A2G8JUP9;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=Lysophospholipid acyltransferase 7 {ECO:0000256|ARBA:ARBA00039722};
GN ORFNames=BSL78_23678 {ECO:0000313|EMBL:PIK39486.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK39486.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK39486.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK39486.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK39486.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000256|ARBA:ARBA00005074}.
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 membrane-bound acyltransferase family.
CC {ECO:0000256|ARBA:ARBA00010323}.
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:PIK39486.1}.
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DR EMBL; MRZV01001234; PIK39486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8JUP9; -.
DR STRING; 307972.A0A2G8JUP9; -.
DR Proteomes; UP000230750; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR004299; MBOAT_fam.
DR PANTHER; PTHR13906:SF16; LYSOPHOSPHOLIPID ACYLTRANSFERASE 7; 1.
DR PANTHER; PTHR13906; PORCUPINE; 1.
DR Pfam; PF03062; MBOAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000313|EMBL:PIK39486.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PIK39486.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 34..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 392 AA; 45835 MW; 6DDAF78BEDAFDAA1 CRC64;
MITYCHICSF IFNFSYVTFF RAGSYFGLKQ PTGFSNVVML LLTLKLVGIA YEVHDSNKIR
RNRENGVPDP VDRNGKPRYQ PIIDDPSAVD IVHYSFCFIG LFTGPYFKFR TYRDWVHNDN
SKDVPLMGPL MARLKVLPLI AALFLGCSYF FNANMKEEAF YQHPLWYRLG YMVPAFTIFR
MRMYSAWILS ECVCIMSALG AYPSELKSRC GQGPTVDPAK IQLNDTKEYD FETIHNIDPY
KCDFTPTFRD AMRGWNMTVQ WWLKNHVFIR FPIKPLSTLV TMLVSAYWHG IYGSYYLSLL
TVPIILIAED LMMKAFRTEE NKVTYDWFNW LFRMRGFEYL SIAFLVLTGA ALWTYWSSIY
FIGHILTFTF IAVGSLYRPK KKTKNEESTK DK
//
