ID A0A232EY42_9HYME Unreviewed; 598 AA.
AC A0A232EY42;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TSAR_010887 {ECO:0000313|EMBL:OXU23243.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU23243.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU23243.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU23243.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU23243.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
CC -!- FUNCTION: Vesicular soluble NSF attachment protein receptor (v-SNARE)
CC mediating vesicle docking and fusion to a specific acceptor cellular
CC compartment. Functions in endoplasmic reticulum to Golgi transport; as
CC part of a SNARE complex composed of GOSR1, GOSR2 and STX5. Functions in
CC early/recycling endosome to TGN transport; as part of a SNARE complex
CC composed of BET1L, GOSR1 and STX5. Has a S-palmitoyl transferase
CC activity. {ECO:0000256|ARBA:ARBA00025256}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00025701}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00025701}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00025701}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004444}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004444}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004444}. Membrane
CC {ECO:0000256|ARBA:ARBA00004423}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004423}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004423}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family.
CC {ECO:0000256|ARBA:ARBA00008025}.
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:OXU23243.1}.
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DR EMBL; NNAY01001679; OXU23243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A232EY42; -.
DR STRING; 543379.A0A232EY42; -.
DR Proteomes; UP000215335; Unassembled WGS sequence.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR CDD; cd14824; Longin; 1.
DR CDD; cd07990; LPLAT_LCLAT1-like; 1.
DR CDD; cd15867; R-SNARE_YKT6; 1.
DR Gene3D; 1.20.5.110; -; 1.
DR Gene3D; 3.30.450.50; Longin domain; 1.
DR InterPro; IPR032098; Acyltransf_C.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR010908; Longin_dom.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR045848; R-SNARE_YKT6.
DR InterPro; IPR042855; V_SNARE_CC.
DR PANTHER; PTHR45806; SYNAPTOBREVIN HOMOLOG YKT6; 1.
DR PANTHER; PTHR45806:SF1; SYNAPTOBREVIN HOMOLOG YKT6; 1.
DR Pfam; PF16076; Acyltransf_C; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR SMART; SM01270; Longin; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF58038; SNARE fusion complex; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
DR PROSITE; PS50859; LONGIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU00290};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Prenylation {ECO:0000256|ARBA:ARBA00023289};
KW Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 58..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 407..526
FT /note="Longin"
FT /evidence="ECO:0000259|PROSITE:PS50859"
FT DOMAIN 537..597
FT /note="V-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50892"
SQ SEQUENCE 598 AA; 68671 MW; D183FA4894B9583F CRC64;
MSGESEVNAA SARPPYNSSF PSSKMNAVET TTSTLLADSA FLRLLITLGN FLKCVARIGF
VLVNNMYCIP TYVIWMMLLS PVKVYYPQIY WRIEGLFFHW LLAMVSMWTW SAGYDVIEQG
DDINRIISDR TLVIANHQST GDVPILMTTF NAKPNALPNL MWIMDRVFKF TNFGIVSLLH
KDFFISSGRK RREESLRQLE KHLKEAYIPL ERKWMVLFPE GGFLCKRRET SQKYAKKNNL
PILENVSLPR VGALQTIFDV VGPVQNNNSS EQQLNSRTNM AVTKPEIRWI LDITIAYPQG
KPLDLPTIIT GSRPPCETVL FYRLFPTSMV PKEPEQLSRW LYDRWAEKEA LLENFYKHGT
FVGTQPLEPE DSKIQQDPLR FLVLHLFFMT SSYIHYNRMV KLYALTILYK GPTSATALKT
AYDVDSFSYF QRGSVREFMA FVSKTITERT QIAARQSVKE GEYMCHVYVR GDSLAGVLIS
DHEYPNRVSH TLITRVLDEF AAKYPAHTWP TLREATTDFQ QVNVYLAKYQ NPREADALTK
MQEDLDETKI ILHNTLEAVL QRGEKLDDLV QKSEGLSIQS KAFYKTARKT NSCCSLTA
//
