ID A0A132AM95_SARSC Unreviewed; 652 AA.
AC A0A132AM95;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN ORFNames=QR98_0101430 {ECO:0000313|EMBL:KPM11570.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM11570.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM11570.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM11570.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
CC -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363075}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU363075}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family. PIGZ
CC subfamily. {ECO:0000256|ARBA:ARBA00038466}.
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:KPM11570.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JXLN01017472; KPM11570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A132AM95; -.
DR VEuPathDB; VectorBase:SSCA001176; -.
DR OMA; YRICRLY; -.
DR OrthoDB; 7417at2759; -.
DR Proteomes; UP000616769; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 1.
DR PANTHER; PTHR22760:SF3; GPI MANNOSYLTRANSFERASE 4; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU363075};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU363075,
KW ECO:0000313|EMBL:KPM11570.1};
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363075};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363075};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363075}.
FT TRANSMEM 13..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 164..182
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 217..233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 253..270
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 317..338
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 430..449
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
SQ SEQUENCE 652 AA; 76909 MW; F9E64985474C184B CRC64;
MDRNKNYVKN QRFYLKIFTK ILFAIRILIV LLPQTGYIQP DEFHQFTEPL ARKIFNVKTL
IVWEFHQDHL LRSMVFPQIF CGLVFKLINY FYSQDPSSIS SYGILIVPRL IMALFSFLID
FSLIRIAKLF QMNRRLSQNI PNLIDWLGLI HSSMYLTMTY YNRTFTNTIE TVLFSLLLWI
VFESISRHHS VKVQSNRTAI YLGMILAAGF FNRPTFAIFA FVPISYWIVM FRFKRNQIPS
FWNERIRIVI ENVLKLSPSF LMVSIVFIIF DSNFYDRLKW SINLPKLISL DLVITPWNFI
RYNIDRDNLS NHGLHPFYFH TLICFPLIFT FLALINYLEW LRLLCKILRN NNRMYALLQF
FSPSSSSNNA NDDSSSFLII VLHLTILFSL LGFSLIPHQE PRFLMPLVVA VIVVSGPRLI
RIVQSNHTKF FISLWFLTQL PLTIFYGFLH QSGVTQSLLY LRANHHKELY DSKQNITILF
NQMYLPPQHL LLLSHSSNVI IKDYSIEPFL SSITSTLNES FEKLRRAERI KLFIILPSYF
DQLLQAVIDQ LCQINQISDC FLKPLRNFLH FSGENFHQSI SLLQGREPEF DLEEYKIFRK
QFKISDTKLQ KSLERFLSFA NKSNRITKLK RAFGMSVWMI DLIHIGANKN GP
//
