ID A0A182XNS4_ANOQN Unreviewed; 772 AA.
AC A0A182XNS4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 03-MAY-2023, entry version 27.
DE RecName: Full=Sphingomyelin synthase-like domain-containing protein {ECO:0000259|Pfam:PF14360};
OS Anopheles quadriannulatus (Mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34691 {ECO:0000313|EnsemblMetazoa:AQUA011524-PA, ECO:0000313|Proteomes:UP000076407};
RN [1] {ECO:0000313|Proteomes:UP000076407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SANGQUA {ECO:0000313|Proteomes:UP000076407};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., 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 quadriannulatus QUAD4_A.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AQUA011524-PA}
RP IDENTIFICATION.
RC STRAIN=SANGQUA {ECO:0000313|EnsemblMetazoa:AQUA011524-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sphingomyelin synthase family.
CC {ECO:0000256|ARBA:ARBA00005441}.
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DR AlphaFoldDB; A0A182XNS4; -.
DR STRING; 34691.A0A182XNS4; -.
DR EnsemblMetazoa; AQUA011524-RA; AQUA011524-PA; AQUA011524.
DR VEuPathDB; VectorBase:AQUA011524; -.
DR Proteomes; UP000076407; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR045221; Sphingomyelin_synth-like.
DR InterPro; IPR025749; Sphingomyelin_synth-like_dom.
DR PANTHER; PTHR21290:SF27; PHOSPHATIDYLCHOLINE:CERAMIDE CHOLINEPHOSPHOTRANSFERASE 1; 1.
DR PANTHER; PTHR21290; SPHINGOMYELIN SYNTHETASE; 1.
DR Pfam; PF14580; LRR_9; 1.
DR Pfam; PF14360; PAP2_C; 1.
DR SMART; SM00365; LRR_SD22; 3.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 3.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
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 96..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 238..310
FT /note="Sphingomyelin synthase-like"
FT /evidence="ECO:0000259|Pfam:PF14360"
FT REGION 30..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 772 AA; 88644 MW; A04C3C68F1E6547F CRC64;
MEVAIRNLIW TDRFFTDGVE MITEVPDSYD YNSPNAPNHH PSAYPHPGSP YHQQSHQPPP
SDTGSPSSDA VMIKIDTPSP LRDDQSRYPK EIGKTLLALL FLAGNFFLAT VSLSLVHDRV
PDRDVYGPLP DAFLDRVQPQ DWALDVSEIL IMVVVNSCVL LITFHKHRFI VMRRVFLLLS
ILYMMRSLTM YVTVLPVSSR TYYCSPKSNA SSAGVIVKRA FQLISGMGLS INGKQIYCGD
YIYSGHTVTL VLGYLVISEY SPKRFWPIHW IYWLASLTGV VMVLVAHGHY TVDVLIAYYA
TTRLFWTYHT LANNSLLLKQ NGNNYIGREW WYFAFRYFER NVRGPIPLQY DCPLSLPSSW
TKKSPKLPGR EITEQLIRKK SEHNELIIGT LEELSLHQED IERIEHIGHW CRELKILLLQ
SNLIPRLENL NRLKKLQYLN VAINNIERIE NLEALEALQK LDLTLNFIGE LTSVESLRAN
YNLRELFLTG NPCTDYPGYR EYVIIALPQL AHLDGKEITR SDRLLAAKQL PALRERIVQL
EALHKIERDE QRVRVQQSIE EQEASVRDLP DDDERRATTF WQQKSEHCPE TRIQMAKFSR
RAKEQAAAGG KNLDQPDGRK RTRRLFAECG RPYSLNEPRV NFEFRDEPDR FELDLHVYKY
LDTSLVEVDA QPNYVRVTIK GKVFQLALKQ DIQTDRSTCQ RSQTTGHMLI VMPKLNPERI
VAPAEEKRTS QVNQSQATGG GLKGPVDIRS ICGGSSQTKQ PRINEDEVPD LI
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