NGBR_DANRE
ID NGBR_DANRE Reviewed; 274 AA.
AC Q6DHR8; B0V3G6; B0V3G7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Dehydrodolichyl diphosphate synthase complex subunit nus1 {ECO:0000305};
DE EC=2.5.1.87 {ECO:0000250|UniProtKB:Q96E22};
DE AltName: Full=Di-trans,poly-cis-decaprenylcistransferase {ECO:0000305};
DE AltName: Full=Nogo-B receptor {ECO:0000250|UniProtKB:Q96E22};
DE Short=NgBR {ECO:0000250|UniProtKB:Q96E22};
DE AltName: Full=Nuclear undecaprenyl pyrophosphate synthase 1 homolog {ECO:0000305};
GN Name=nus1; Synonyms=ngbr; ORFNames=si:ch211-102b16.1, zgc:92136;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: With DHDDS, forms the dehydrodolichyl diphosphate synthase
CC (DDS) complex, an essential component of the dolichol monophosphate
CC (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl
CC pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce
CC dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which
CC is utilized as a sugar carrier in protein glycosylation in the
CC endoplasmic reticulum (ER). Regulates the glycosylation and stability
CC of nascent NPC2, thereby promoting trafficking of LDL-derived
CC cholesterol. Acts as a specific receptor for the N-terminus of Nogo-B,
CC a neural and cardiovascular regulator. {ECO:0000250|UniProtKB:Q96E22}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-
CC trans,poly-cis-polyprenyl diphosphate + n diphosphate;
CC Xref=Rhea:RHEA:53008, Rhea:RHEA-COMP:13431, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:136960, ChEBI:CHEBI:175763;
CC EC=2.5.1.87; Evidence={ECO:0000250|UniProtKB:Q96E22};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q86SQ9};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96E22}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q96E22}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6DHR8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6DHR8-2; Sequence=VSP_034839;
CC -!- MISCELLANEOUS: Nus1 seems to exist in two topological orientations, a
CC minor glycosylated species with its C-terminus oriented towards the
CC lumen regulating NPC2 stability, and a major fraction oriented with its
CC C-terminus directed towards the cytosol where it regulates cis-IPTase
CC activity. {ECO:0000250|UniProtKB:Q96E22}.
CC -!- SIMILARITY: Belongs to the UPP synthase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAQ13477.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CU138502; CAQ13476.1; -; Genomic_DNA.
DR EMBL; CU138502; CAQ13477.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC075899; AAH75899.1; -; mRNA.
DR RefSeq; NP_001002356.1; NM_001002356.1. [Q6DHR8-1]
DR AlphaFoldDB; Q6DHR8; -.
DR SMR; Q6DHR8; -.
DR STRING; 7955.ENSDARP00000034808; -.
DR PaxDb; Q6DHR8; -.
DR Ensembl; ENSDART00000034054; ENSDARP00000034808; ENSDARG00000027813. [Q6DHR8-1]
DR GeneID; 436629; -.
DR KEGG; dre:436629; -.
DR CTD; 116150; -.
DR ZFIN; ZDB-GENE-040718-48; nus1.
DR eggNOG; KOG2818; Eukaryota.
DR GeneTree; ENSGT00390000003223; -.
DR HOGENOM; CLU_051870_2_1_1; -.
DR InParanoid; Q6DHR8; -.
DR OMA; MPRVYEA; -.
DR OrthoDB; 1448374at2759; -.
DR PhylomeDB; Q6DHR8; -.
DR TreeFam; TF332448; -.
DR Reactome; R-DRE-446199; Synthesis of Dolichyl-phosphate.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q6DHR8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000027813; Expressed in swim bladder and 33 other tissues.
DR ExpressionAtlas; Q6DHR8; baseline and differential.
DR GO; GO:1904423; C:dehydrodolichyl diphosphate synthase complex; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR GO; GO:0019408; P:dolichol biosynthetic process; IBA:GO_Central.
DR GO; GO:0006486; P:protein glycosylation; IBA:GO_Central.
DR GO; GO:0002040; P:sprouting angiogenesis; IMP:ZFIN.
DR Gene3D; 3.40.1180.10; -; 1.
DR InterPro; IPR038887; Nus1/NgBR.
DR InterPro; IPR001441; UPP_synth-like.
DR InterPro; IPR036424; UPP_synth-like_sf.
DR PANTHER; PTHR21528; PTHR21528; 2.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF64005; SSF64005; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Magnesium;
KW Membrane; Receptor; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..274
FT /note="Dehydrodolichyl diphosphate synthase complex subunit
FT nus1"
FT /id="PRO_0000273169"
FT TRANSMEM 1..23
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:Q96E22"
FT TRANSMEM 33..49
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:Q96E22"
FT TRANSMEM 95..113
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:Q96E22"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 245..274
FT /note="ISMPSHIDASYDDLYDALQRFAGCEQRLGK -> MYMFLGFKGTMEL (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034839"
SQ SEQUENCE 274 AA; 31276 MW; 2D59395686C9E2C0 CRC64;
MASLYEMVWR FLHALLYLQR AIVAWFRVHI WRWKLAVVDL LLPLALGFHN QKKTGPKGTR
TSRRVRWGAD GRTLEKLPLH VGLLVTEEEI HYTDIANLVV WCMAVGISYV SVYDNQGVFK
RNNSRLMEEI LKQQQELLGM GSSKYSVEIL KNGTNKQEHQ VLSCQSMVKV LSPDDGRLSI
VQAAQQLCRA VEQKEKTSKD INVSVLDSLL KESKNIPDPD LVLKFGTVQS TLGFLPWHIR
LTEIISMPSH IDASYDDLYD ALQRFAGCEQ RLGK
