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KTAP2_DROME
ID   KTAP2_DROME             Reviewed;         141 AA.
AC   Q8INQ7; Q8IGM0;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Protein KRTCAP2 homolog;
DE   AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit KCP2;
DE            Short=Oligosaccharyl transferase subunit KCP2;
GN   ORFNames=CG31460;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN71467.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014297; AAN13389.1; -; Genomic_DNA.
DR   EMBL; BT001712; AAN71467.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001287236.1; NM_001300307.1.
DR   RefSeq; NP_731253.1; NM_169227.2.
DR   AlphaFoldDB; Q8INQ7; -.
DR   BioGRID; 77046; 6.
DR   IntAct; Q8INQ7; 4.
DR   STRING; 7227.FBpp0081362; -.
DR   PaxDb; Q8INQ7; -.
DR   PRIDE; Q8INQ7; -.
DR   DNASU; 318747; -.
DR   EnsemblMetazoa; FBtr0081873; FBpp0081362; FBgn0051460.
DR   EnsemblMetazoa; FBtr0339327; FBpp0308428; FBgn0051460.
DR   GeneID; 318747; -.
DR   KEGG; dme:Dmel_CG31460; -.
DR   UCSC; CG31460-RA; d. melanogaster.
DR   FlyBase; FBgn0051460; CG31460.
DR   VEuPathDB; VectorBase:FBgn0051460; -.
DR   eggNOG; KOG4615; Eukaryota.
DR   GeneTree; ENSGT00390000003552; -.
DR   HOGENOM; CLU_109648_2_0_1; -.
DR   InParanoid; Q8INQ7; -.
DR   OMA; EMVVFGQ; -.
DR   OrthoDB; 1561955at2759; -.
DR   PhylomeDB; Q8INQ7; -.
DR   BioGRID-ORCS; 318747; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 318747; -.
DR   PRO; PR:Q8INQ7; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0051460; Expressed in eye disc (Drosophila) and 21 other tissues.
DR   ExpressionAtlas; Q8INQ7; baseline and differential.
DR   Genevisible; Q8INQ7; DM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042543; P:protein N-linked glycosylation via arginine; IBA:GO_Central.
DR   InterPro; IPR018614; KRTCAP2.
DR   PANTHER; PTHR32001; PTHR32001; 1.
DR   Pfam; PF09775; Keratin_assoc; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..141
FT                   /note="Protein KRTCAP2 homolog"
FT                   /id="PRO_0000327902"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   141 AA;  15392 MW;  D47B7554A3BA2722 CRC64;
     MSASVSSKST VVSSIISGLL SIVLFGTLRF CSEWFNDSQL RVLLGGYLFS WVFILSLTCV
     SNAEMVVFGQ DFQAKLLPEI IFCLSLTVAA AGLVHRVCAT TSVLFSLVGL YFLNRISTKY
     YSVQVPSVDA PTTRKGGKKF K
 
 
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