ID B6AJ32_CRYMR Unreviewed; 340 AA.
AC B6AJ32;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=OST3 / OST6 family protein {ECO:0000313|EMBL:EEA08223.1};
GN ORFNames=CMU_011750 {ECO:0000313|EMBL:EEA08223.1};
OS Cryptosporidium muris (strain RN66).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Cryptosporidiidae; Cryptosporidium.
OX NCBI_TaxID=441375 {ECO:0000313|Proteomes:UP000001460};
RN [1] {ECO:0000313|EMBL:EEA08223.1, ECO:0000313|Proteomes:UP000001460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN66 {ECO:0000313|EMBL:EEA08223.1,
RC ECO:0000313|Proteomes:UP000001460};
RA Lorenzi H., Inman J., Miller J., Schobel S., Amedeo P., Caler E.V.,
RA da Silva J.;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that
CC catalyzes the initial transfer of a defined glycan
CC (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-
CC pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr
CC consensus motif in nascent polypeptide chains, the first step in
CC protein N-glycosylation. N-glycosylation occurs cotranslationally and
CC the complex associates with the Sec61 complex at the channel-forming
CC translocon complex that mediates protein translocation across the
CC endoplasmic reticulum (ER). All subunits are required for a maximal
CC enzyme activity. {ECO:0000256|ARBA:ARBA00002791}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the OST3/OST6 family.
CC {ECO:0000256|ARBA:ARBA00009561}.
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DR EMBL; DS989737; EEA08223.1; -; Genomic_DNA.
DR RefSeq; XP_002142572.1; XM_002142536.1.
DR AlphaFoldDB; B6AJ32; -.
DR STRING; 441375.B6AJ32; -.
DR EnsemblProtists; EEA08223; EEA08223; CMU_011750.
DR GeneID; 6997617; -.
DR VEuPathDB; CryptoDB:CMU_011750; -.
DR eggNOG; KOG4474; Eukaryota.
DR OMA; KVPDYPY; -.
DR OrthoDB; 177223at2759; -.
DR Proteomes; UP000001460; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR021149; OligosaccharylTrfase_OST3/OST6.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12692; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE-RELATED; 1.
DR PANTHER; PTHR12692:SF0; GH11935P; 1.
DR Pfam; PF04756; OST3_OST6; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001460};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..340
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002842382"
FT TRANSMEM 185..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 340 AA; 39420 MW; 244B9942C9669A8A CRC64;
MMHFKNILIF SIIIILSQFL AKADKLEELI KFCDDNFNGL VIFNYTGYQY YVLNDSRPYD
LIILYTGTSK SCQGCIPSTT NYEKVARNYY NHEFKNNPKA IFAIVYVDRV ENIMAIHELR
NLPAIIYIES TKKFTSNSLT FRRDNQWRIP EQKDISTNAM LGFINKKTGM NITIYISSKE
KISRLISLFI GLILIIVIFW QLVLLIRKKP FIIMIITVII CSISMSGMVY SIQHGRKQAN
EFFVRNPRIQ NMTEGILASI LMTSASLILF LIPFLFSNKL NFKFFRIPRW LSPLFIAALV
STLISIHYAY TTKVGWYSPT FYPPEGYLKG PLIVDRGNSF
//
