ID A0A8H3XEI7_GIGMA Unreviewed; 289 AA.
AC A0A8H3XEI7;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=Ribophorin II {ECO:0000256|ARBA:ARBA00032139};
DE AltName: Full=Ribophorin-2 {ECO:0000256|ARBA:ARBA00030078};
GN ORFNames=F8M41_001407 {ECO:0000313|EMBL:KAF0455822.1};
OS Gigaspora margarita.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Diversisporales; Gigasporaceae; Gigaspora.
OX NCBI_TaxID=4874 {ECO:0000313|EMBL:KAF0455822.1, ECO:0000313|Proteomes:UP000439903};
RN [1] {ECO:0000313|EMBL:KAF0455822.1, ECO:0000313|Proteomes:UP000439903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BEG34 {ECO:0000313|EMBL:KAF0455822.1,
RC ECO:0000313|Proteomes:UP000439903};
RX PubMed=31621176;
RA Venice F., Ghignone S., Salvioli di Fossalunga A., Amselem J., Novero M.,
RA Xianan X., Sedzielewska Toro K., Morin E., Lipzen A., Grigoriev I.V.,
RA Henrissat B., Martin F.M., Bonfante P.;
RT "At the nexus of three kingdoms: the genome of the mycorrhizal fungus
RT Gigaspora margarita provides insights into plant, endobacterial and fungal
RT interactions.";
RL Environ. Microbiol. 0:0-0(2019).
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 -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}.
CC -!- SIMILARITY: Belongs to the SWP1 family.
CC {ECO:0000256|ARBA:ARBA00009038}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF0455822.1}.
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DR EMBL; WTPW01001109; KAF0455822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8H3XEI7; -.
DR OrthoDB; 432292at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000439903; Unassembled WGS sequence.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:InterPro.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:TreeGrafter.
DR InterPro; IPR055374; Ribophorin_II_3rd.
DR InterPro; IPR056790; Ribophorin_II_C.
DR InterPro; IPR008814; Swp1.
DR PANTHER; PTHR12640:SF0; DOLICHYL-DIPHOSPHOOLIGOSACCHARIDE--PROTEIN GLYCOSYLTRANSFERASE SUBUNIT 2; 1.
DR PANTHER; PTHR12640; RIBOPHORIN II; 1.
DR Pfam; PF23860; Ribophorin_II_3rd; 1.
DR Pfam; PF25147; Ribophorin_II_C; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000439903};
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..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..289
FT /note="Ribophorin II"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044338248"
FT TRANSMEM 192..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..158
FT /note="Ribophorin II third"
FT /evidence="ECO:0000259|Pfam:PF23860"
FT DOMAIN 182..284
FT /note="Ribophorin II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF25147"
SQ SEQUENCE 289 AA; 32471 MW; 7F04453A03A82F3F CRC64;
MIRSLINIIS WRAFLLVLLT SVLVQADDFV ISDVKIAVTT SESVRKLYES IPYPSSFDKP
IQLTSGDDFK MIFVVNDKQT QKGVQPHQAF LTLTSEKNGN QIPIIIRVRE NGKSKVELDM
KSAPDELLSS PGNYSLDLII GTFSYNDPLK YHVGTLEIDV PIQSSGPSPV VYGPKPEIHH
IFRPDEKLPP IWLSYSFMAI VLIPWVFLIG AWAYIGVNVS LLARAPESSL MSILFLGSLL
AIEILFYNYW THLNIFQTLT WLTGLSIVAF ITGQKALSDV QKWRSLGLR
//
