ID B5X0Q7_SALSA Unreviewed; 281 AA.
AC B5X0Q7;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyldiphosphate specific] {ECO:0000256|ARBA:ARBA00012596};
DE EC=2.5.1.87 {ECO:0000256|ARBA:ARBA00012596};
GN Name=NGBR {ECO:0000313|EMBL:ACI32888.1};
GN Synonyms=ngbr {ECO:0000313|RefSeq:NP_001133241.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|EMBL:ACI32888.1};
RN [1] {ECO:0000313|EMBL:ACI32888.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:ACI32888.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RA Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA Koop B.F.;
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACI32888.1, ECO:0000313|RefSeq:NP_001133241.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:ACI32888.1};
RX PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA Koop B.F.;
RT "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT evolutionary pressures on a post-tetraploidization genome.";
RL BMC Genomics 11:279-279(2010).
RN [3] {ECO:0000313|EMBL:ACI32888.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain {ECO:0000313|EMBL:ACI32888.1};
RG cGRASP (B.F. Koop & W.S. Davidson);
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:NP_001133241.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000976};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SIMILARITY: Belongs to the UPP synthase family.
CC {ECO:0000256|ARBA:ARBA00005432}.
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DR EMBL; BT044626; ACI32888.1; -; mRNA.
DR RefSeq; NP_001133241.1; NM_001139769.1.
DR STRING; 8030.ENSSSAP00000037257; -.
DR PaxDb; 8030-ENSSSAP00000037257; -.
DR Ensembl; ENSSSAT00000063011; ENSSSAP00000037248; ENSSSAG00000042933.
DR GeneID; 100194740; -.
DR KEGG; sasa:100194740; -.
DR CTD; 100194740; -.
DR OrthoDB; 444436at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000087266; Chromosome ssa15.
DR Bgee; ENSSSAG00000042933; Expressed in ovary and 15 other cell types or tissues.
DR GO; GO:1904423; C:dehydrodolichyl diphosphate synthase complex; IEA:InterPro.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0045547; F:dehydrodolichyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0019408; P:dolichol biosynthetic process; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.1180.10; Decaprenyl diphosphate synthase-like; 1.
DR InterPro; IPR038887; Nus1/NgBR.
DR InterPro; IPR001441; UPP_synth-like.
DR InterPro; IPR036424; UPP_synth-like_sf.
DR PANTHER; PTHR21528:SF0; DEHYDRODOLICHYL DIPHOSPHATE SYNTHASE COMPLEX SUBUNIT NUS1; 1.
DR PANTHER; PTHR21528; UNCHARACTERIZED; 1.
DR Pfam; PF01255; Prenyltransf; 1.
DR SUPFAM; SSF64005; Undecaprenyl diphosphate synthase; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Receptor {ECO:0000313|EMBL:ACI32888.1, ECO:0000313|RefSeq:NP_001133241.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ SEQUENCE 281 AA; 32269 MW; 9530DF3A3CF86DD7 CRC64;
MAIVYEFVWQ VLHVLLHIHR TLITWFRIRL RNWDGKLWSR ALTALIVPLA ISFPNQKNIV
PAPGKRVGRR YRWGADGKSL EKLPYHIGLL IAEEEPRFTD IANLVVWCMA VGISYVSVYD
NYGVFRRNNS RLMDEILKQQ QELLDLEGSK HLSVEFLNNG TDKQDQQVLS CQSVLKVLSP
DDGKLRIVQA AQQLCRAVEQ REKTSKDINV TVLDSLLRES KSTPDPDLVL KFGPVESTLG
FLPWHIRLTE FISLPSHVDV SYEDLFSALQ RYASCEQRLG K
//
