RPN2_DICDI
ID RPN2_DICDI Reviewed; 685 AA.
AC Q54HG9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit swp1;
DE Short=Oligosaccharyl transferase subunit swp1;
DE AltName: Full=Ribophorin II;
DE Short=RPN-II;
DE AltName: Full=Ribophorin-2;
DE Flags: Precursor;
GN Name=swp1; Synonyms=rpn2; ORFNames=DDB_G0289479;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(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:Q02795}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC {ECO:0000250|UniProtKB:Q02795}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SWP1 family. {ECO:0000305}.
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; AAFI02000141; EAL62719.1; -; Genomic_DNA.
DR RefSeq; XP_636216.1; XM_631124.1.
DR AlphaFoldDB; Q54HG9; -.
DR SMR; Q54HG9; -.
DR STRING; 44689.DDB0233147; -.
DR PaxDb; Q54HG9; -.
DR EnsemblProtists; EAL62719; EAL62719; DDB_G0289479.
DR GeneID; 8627154; -.
DR KEGG; ddi:DDB_G0289479; -.
DR dictyBase; DDB_G0289479; swp1.
DR eggNOG; KOG2447; Eukaryota.
DR HOGENOM; CLU_401957_0_0_1; -.
DR InParanoid; Q54HG9; -.
DR OMA; TTWSART; -.
DR PhylomeDB; Q54HG9; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q54HG9; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:dictyBase.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR InterPro; IPR008814; Swp1.
DR PANTHER; PTHR12640; PTHR12640; 1.
DR Pfam; PF05817; Ribophorin_II; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..685
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit swp1"
FT /id="PRO_0000328636"
FT TOPO_DOM 19..590
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..611
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 612..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 621..641
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 642..646
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..685
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 685 AA; 75616 MW; 816D42023DC15FE4 CRC64;
MKLIILIVLS ILISIVISGS VQSKITTTRG ISNVYSKNDI NNIKQFISSK YNGNTKLYGE
SLKDTFYGVG VLTRIGETNI EATKDICKQT KEQLKQNKFT DIELVFNGVT ILSELKCLQG
ESSSSLGNEQ QLQDLLKNKL ENGSLLEKTQ AINIYFTLSS AKAIDSKTVS IIDPLLIQAV
NSMVSLMDED GTFKSVSTDD EGNLQNTAAA YFALARLSHR LKSNEVDKLV AKVVNKVDTV
LASADETTDS LYFNDLSTTS SLLHGLLSLA SVNDKVADVI SNKQINQISE YLLRQKNVES
LSDAYHLIVA LKRCQKNSIS QPISLALVKS IYSPSGLNDI RVRVTDIFDQ PIEASIVINK
VVSSKNPRST PILSGKEMKF QSSDNSFVAD LSNENLKLGS YNFEFKVQPV DTDSYKSITN
IQIITITGAV TVNDMKLSYA PKSDQLGSPK TTNEVQFGQK LPLIEIPSNN IARIFFRIAS
EAQPYQAQQV GIRFYSPARE AVVPATYSAD AYSYTFTNKD ACKILGCQSG NYQLDLIIGD
QSITPLQWNF GEINLKFNQS TIPTNRYPEQ LPISHNFRVA EKRPPQSISS LFTLLVLSPI
AIFVIGLLFV GTNLGRFPTG MGFIYTIGFL GCISATGLLI VNYWLHSTMD VTLKNLALLM
IPLVFFGHKS MSYYSNLSSS NIKKD
