ID   KTAP2_DROPS             Reviewed;         140 AA.
AC   Q295N5;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 3.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Protein KRTCAP2 homolog;
DE   AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit KCP2;
DE            Short=Oligosaccharyl transferase subunit KCP2;
GN   ORFNames=GA16263;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
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:0000250|UniProtKB:Q8N6L1}.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC       {ECO:0000250|UniProtKB:P86229}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the KRTCAP2 family. {ECO:0000305}.
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DR   EMBL; CM000070; EAL28673.2; -; Genomic_DNA.
DR   RefSeq; XP_001359527.2; XM_001359490.3.
DR   AlphaFoldDB; Q295N5; -.
DR   STRING; 7237.FBpp0284553; -.
DR   EnsemblMetazoa; FBtr0286115; FBpp0284553; FBgn0076279.
DR   GeneID; 4802646; -.
DR   KEGG; dpo:Dpse_GA16263; -.
DR   eggNOG; KOG4615; Eukaryota.
DR   HOGENOM; CLU_109648_2_0_1; -.
DR   InParanoid; Q295N5; -.
DR   OMA; EMVVFGQ; -.
DR   Proteomes; UP000001819; Chromosome 2.
DR   Bgee; FBgn0076279; Expressed in female reproductive system and 2 other tissues.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR018614; KRTCAP2.
DR   PANTHER; PTHR32001; PTHR32001; 1.
DR   Pfam; PF09775; Keratin_assoc; 1.
PE   3: Inferred from homology;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..140
FT                   /note="Protein KRTCAP2 homolog"
FT                   /id="PRO_0000327903"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   140 AA;  15256 MW;  BB94856537B4BAD6 CRC64;
     MSVSTSSKNT LLSSIISGIL SLVIFATLRF CADWFNGSQL NVLVGGYLFS WLFILSLTCV
     SNAEMLIFGP DFQAKLVPEI LFCLSLTVAA AGIVHRVCAT TSVLFSLVGL YFLNRISIKY
     YSTSVVPVDA PARKTAKKFK