ID   B4FXY5_MAIZE            Unreviewed;       692 AA.
AC   B4FXY5;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 {ECO:0000256|RuleBase:RU366029};
DE   AltName: Full=Ribophorin-2 {ECO:0000256|RuleBase:RU366029};
GN   Name=100273881 {ECO:0000313|EnsemblPlants:Zm00001eb143710_P001};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577 {ECO:0000313|EMBL:ACF86978.1};
RN   [1] {ECO:0000313|EMBL:ACF86978.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B73 {ECO:0000313|EMBL:ACF86978.1};
RX   PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA   Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA   Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA   Walbot V., Yu Y.;
RT   "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL   PLoS Genet. 5:E1000740-E1000740(2009).
RN   [2] {ECO:0000313|EnsemblPlants:Zm00001eb143710_P001, ECO:0000313|Proteomes:UP000007305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb143710_P001,
RC   ECO:0000313|Proteomes:UP000007305};
RG   Maize Genome Sequencing Project;
RA   Ware D.;
RT   "Update maize B73 reference genome by single molecule sequencing
RT   technologies.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:Zm00001eb143710_P001}
RP   IDENTIFICATION.
RC   STRAIN=cv. B73 {ECO:0000313|EnsemblPlants:Zm00001eb143710_P001};
RG   EnsemblPlants;
RL   Submitted (MAY-2021) to UniProtKB.
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|RuleBase:RU366029}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|RuleBase:RU366029}.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC       {ECO:0000256|RuleBase:RU366029}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU366029}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC       ECO:0000256|RuleBase:RU366029}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SWP1 family.
CC       {ECO:0000256|RuleBase:RU366029}.
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DR   EMBL; BT041973; ACF86978.1; -; mRNA.
DR   RefSeq; NP_001141747.1; NM_001148275.1.
DR   AlphaFoldDB; B4FXY5; -.
DR   EnsemblPlants; Zm00001eb143710_T001; Zm00001eb143710_P001; Zm00001eb143710.
DR   GeneID; 100273881; -.
DR   Gramene; Zm00001eb143710_T001; Zm00001eb143710_P001; Zm00001eb143710.
DR   KEGG; zma:100273881; -.
DR   OrthoDB; 2877438at2759; -.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000007305; Chromosome 3.
DR   ExpressionAtlas; B4FXY5; baseline and differential.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0006487; P:protein N-linked glycosylation; IEA:UniProtKB-UniRule.
DR   InterPro; IPR008814; Swp1.
DR   PANTHER; PTHR12640:SF0; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT 2; 1.
DR   PANTHER; PTHR12640; RIBOPHORIN II; 1.
DR   Pfam; PF05817; Ribophorin_II; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU366029};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU366029};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:B4FXY5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007305};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366029};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU366029};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU366029}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|RuleBase:RU366029"
FT   CHAIN           26..692
FT                   /note="Dolichyl-diphosphooligosaccharide--protein
FT                   glycosyltransferase subunit 2"
FT                   /evidence="ECO:0000256|RuleBase:RU366029"
FT                   /id="PRO_5034217084"
FT   TRANSMEM        595..619
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366029"
FT   TRANSMEM        631..651
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366029"
FT   TRANSMEM        663..682
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU366029"
SQ   SEQUENCE   692 AA;  74629 MW;  C9532FB614C84413 CRC64;
     MAGRRPAPVA ILLLLAAAFA PISSAVRPVS DAHRSAAVEL FAPSADGSFG DLESTYEAVR
     TFQILGLENY KSLSGKACKF AAENLASPGS TTKDLFHAVR ISGALGCAVD AGVYDGVVAR
     LKAVIQDTNS LLELYYPVGG LLGIKEQGHN VVLSDAEGTF HATKALSQSD GRWRYDTDSA
     ESSTFAAGIA LEALAGIVSL ADAAVDPSMM GVVKNDVVKL FDTIKSYNDG TFYFDEKHVD
     ATEYKGPIIT SASVVRGVTS FAAVVSGKLN IPAEKILGLA KFFLGIGLPG SAKDCFNQIE
     SLSFLENNRV FVPLILSLSS KVFSLTSKDQ LKVEVTSVFG SAAPSLKVNL VQVLGSDSKV
     ITSENKELQY DLDNNVHYLD IAPLKIDVGK YSIVFEISLQ EPEQETVYAT GGRNTESVIV
     TGLIKVDKAE IGISDNDAGA VESVQKLDLL KDTKVSLSAN HLQKLCLSFQ LTTPLGHTFK
     PHQVFLKLRH ESKVEHLFVV PGSARQFKIV LDFLGLVEKF YYLSGRYDLE LTVGDAVMEN
     SFLRPLGHLE LDLPDAPEKA PRPPAQAVDP FSKFGPKAEI SHIFRAPEKR PPKELSLAFT
     GLTLLPFIGF LIGLVRLGVN LKNFPSLPGP AAFASLFHAG IGAVLMLYVL FWIKLDLFTT
     LKYLGFLGIF LVFVGHRALS YLSSVSTKQK TA
//