ID A0A8C4ZV54_GADMO Unreviewed; 626 AA.
AC A0A8C4ZV54;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 08-OCT-2025, sequence version 3.
DT 28-JAN-2026, entry version 16.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2 {ECO:0000256|ARBA:ARBA00017612, ECO:0000256|RuleBase:RU366029};
DE AltName: Full=Ribophorin-2 {ECO:0000256|RuleBase:RU366029};
GN Name=rpn2 {ECO:0000313|Ensembl:ENSGMOP00000022743.1};
OS Gadus morhua (Atlantic cod).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Gadidae; Gadus.
OX NCBI_TaxID=8049 {ECO:0000313|Ensembl:ENSGMOP00000022743.1, ECO:0000313|Proteomes:UP000694546};
RN [1] {ECO:0000313|Ensembl:ENSGMOP00000022743.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSGMOP00000022743.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) 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|ARBA:ARBA00002791,
CC ECO:0000256|RuleBase:RU366029}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU366029}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex. OST
CC exists in two different complex forms which contain common core
CC subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258, either STT3A or
CC STT3B as catalytic subunits, and form-specific accessory subunits.
CC STT3A complex assembly occurs through the formation of 3 subcomplexes.
CC Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the
CC STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core
CC subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The
CC STT3A complex can form stable complexes with the Sec61 complex or with
CC both the Sec61 and TRAP complexes. Interacts with DDI2. Interacts with
CC TMEM35A/NACHO. {ECO:0000256|ARBA:ARBA00046750}.
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}.
CC -!- SIMILARITY: Belongs to the SWP1 family. {ECO:0000256|ARBA:ARBA00009038,
CC ECO:0000256|RuleBase:RU366029}.
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DR AlphaFoldDB; A0A8C4ZV54; -.
DR Ensembl; ENSGMOT00000047509.1; ENSGMOP00000022743.1; ENSGMOG00000014382.2.
DR GeneTree; ENSGT00390000002635; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000694546; Chromosome 13.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:UniProtKB-UniRule.
DR InterPro; IPR055375; Ribophorin_II_2nd.
DR InterPro; IPR055374; Ribophorin_II_3rd.
DR InterPro; IPR056790; Ribophorin_II_C.
DR InterPro; IPR055373; Ribophorin_II_N.
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.
DR Pfam; PF23861; Ribophorin_II_2nd; 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 ECO:0000256|RuleBase:RU366029};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU366029};
KW Reference proteome {ECO:0000313|Proteomes:UP000694546};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU366029};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU366029}.
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366029"
FT TRANSMEM 570..591
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366029"
FT TRANSMEM 603..620
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366029"
FT DOMAIN 30..263
FT /note="Ribophorin II N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05817"
FT DOMAIN 272..367
FT /note="Ribophorin II second"
FT /evidence="ECO:0000259|Pfam:PF23861"
FT DOMAIN 375..500
FT /note="Ribophorin II third"
FT /evidence="ECO:0000259|Pfam:PF23860"
FT DOMAIN 528..626
FT /note="Ribophorin II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF25147"
SQ SEQUENCE 626 AA; 68362 MW; 012416BC06096B32 CRC64;
MAQTSKTIPS LFLTTSVYLC SQALTPSHYL SLSDVARLQT FLGQHFTDLQ SAYYSIVGLA
KLGAGVADQD EACQFLKAQL DPTSVDSLFY AAVASQALAG CEIPLSNETR DILLAAVSED
STVAQIHHAV GALTALGLPL ASQEVVTALR VRINKEENVV AITLALQTAA RLSQQAELGG
FVEEIEDLTA RLDDLGGLYL QFEEGLEATA DFVVAAYGLS DHLDVEPPLK EEQVIQLVNS
IFSKKSWDSM SEAFSVAGAA VALSSNRFHV PVVVRAEGPA TVSHSKPTLQ VRPANHPLSC
MSSSARLANA SFSRVTLQLR ATFSPTNGLF ELNFMSSQPA SGYYQFTVAV TGDSRLVANH
VELKVKVSTE VAITNMDLSI VDKDQSIGTK TSRVEFPSKS KDSFTADSHQ NFAMAFQLVD
VNTGVELTPH QTFVRLLNQK TGQEVVFVAE PDSKNLYKFE LDMVERKSEF DSMSGTYSLH
LMVGDATLEN PILWNVADVI LKFLDEEAPA VIQPKTLYIP KPEIQHLFRE PEKKPPTVVS
NAFTALILSP FLLLLILWMK LGANISNFTM SPSAVLFHIG HAAMLGLMYV YWTHLDMFQT
LKYLAIIGSL TFLAGNRMLA QKAVKR
//
