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Database: UniProt
Entry: A0A182JNX5_9DIPT
LinkDB: A0A182JNX5_9DIPT
Original site: A0A182JNX5_9DIPT 
ID   A0A182JNX5_9DIPT        Unreviewed;       488 AA.
AC   A0A182JNX5;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Lysophospholipid acyltransferase 5 {ECO:0000256|ARBA:ARBA00039721};
DE            EC=2.3.1.23 {ECO:0000256|ARBA:ARBA00026120};
DE            EC=2.3.1.n6 {ECO:0000256|ARBA:ARBA00038923};
OS   Anopheles christyi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR000209-PA, ECO:0000313|Proteomes:UP000075881};
RN   [1] {ECO:0000313|Proteomes:UP000075881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles christyi ACHKN1017.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:ACHR000209-PA}
RP   IDENTIFICATION.
RC   STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR000209-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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}.
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DR   AlphaFoldDB; A0A182JNX5; -.
DR   STRING; 43041.A0A182JNX5; -.
DR   EnsemblMetazoa; ACHR000209-RA; ACHR000209-PA; ACHR000209.
DR   VEuPathDB; VectorBase:ACHR000209; -.
DR   OrthoDB; 5297955at2759; -.
DR   Proteomes; UP000075881; 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:SF14; LYSOPHOSPHOLIPID ACYLTRANSFERASE 5; 1.
DR   PANTHER; PTHR13906; PORCUPINE; 1.
DR   Pfam; PF03062; MBOAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        47..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        250..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        337..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        389..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        430..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          455..488
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  54996 MW;  CE1B6EDB029FD3F7 CRC64;
     MMNPVEALAS VSGASVPAIR LILSVLLAYP IGLLYRQLKG GPTQRNLYIA FTGLSIVVFN
     YGTDIYHSLL AVAVSFLCNA FLGTSKLLVP VSFTYHMGYL LIGYYYTTSD TYDIKWTMPH
     CVLVLRLIGL AFDLSDSRKK EAEGKPDAKC IPAPSLLELI AFTYFPATVL VGPQFSFLRY
     QRFISGAYEP HTQNAPAYAM KKFLQGVFYL VVNQVGTQYV SDAYLMSGEF EQESLFMKHI
     YLGCWGRITL YKYISIWLLA EGAAVIYGLT YIDAKPGERE YCSDELSGCS NIKVGVFENT
     SKYGHYVESF NVQTNTWVAN YVYKRLRFLN NRMLSHLGAL FFLAIWHGFH SGYYITFLLE
     FMCIRMEKEV EPIFARSEKL QQLLQQQPLL RALVFVALKY YTIVWAGWCL VPFVFLSFHK
     WWHIYTVVRF SGFILFIGGN IFLAPVLRAL LPRSSSSSST KTSNIGASSS SAPTGAATAA
     TTEVKKDN
//
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