A8X8R3 (PORED_CAEBR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polyprenol reductase
EC=1.3.1.94

Gene names

ORF Names:

CBG09584

Organism

Caenorhabditis briggsae [Reference proteome]

Taxonomic identifier

6238 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Plays a key role in early steps of protein N-linked glycosylation by being required for the conversion of polyprenol into dolichol. Dolichols are required for the synthesis of dolichol-linked monosaccharides and the oligosaccharide precursor used for N-glycosylation. Acts as a polyprenol reductase that promotes the reduction of the alpha-isoprene unit of polyprenols into dolichols in a NADP-dependent mechanism By similarity.
Catalytic activity	Ditrans,polycis-dolichol + NADP+ = ditrans,polycis-polyprenol + NADPH.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the steroid 5-alpha reductase family. Polyprenol reductase subfamily.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dolichol metabolic process Inferred from sequence or structural similarity. Source: UniProtKB dolichol-linked oligosaccharide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB polyprenol catabolic process Inferred from sequence or structural similarity. Source: UniProtKB protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	oxidoreductase activity, acting on the CH-CH group of donors Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 309	309	Polyprenol reductase		PRO_0000398652
Regions
	Transmembrane	12 – 32	21	Helical; Potential
	Transmembrane	71 – 91	21	Helical; Potential
	Transmembrane	114 – 134	21	Helical; Potential
	Transmembrane	151 – 171	21	Helical; Potential
	Transmembrane	248 – 268	21	Helical; Potential
	Transmembrane	270 – 290	21	Helical; Potential

Sequences

	Sequence		Length	Mass (Da)
	A8X8R3 [UniParc]. Last modified January 15, 2008. Version 1. Checksum: 029B3D93687AA98B	FASTA	309	35,465
	10 20 30 40 50 60 MLENLWEVRQ ALPIYLLTAT IGLAVSCCFT LICPHVCRLI PALTTYGKAA DQLEENSLVA 70 80 90 100 110 120 RISVPKKWFK HFYALGLLTL LLCLHCIHSL IHNPDFLPTI PIKFLTILTR SYSIPPIAPS 130 140 150 160 170 180 TAVLALLLIT FHVARRLYET LFVSVYSDSR MNVFHYIVGI VHYIILPISI MCETQGVITK 190 200 210 220 230 240 KEIFHVSVDD ITLTQWAGAV LFWVCNWKQH QIAEQIANTR KGPRGLIRNY AYGICFGRWF 250 260 270 280 290 300 NLVSCPHFLF EICIYLSLLL VIPTAYVYRF VVLFVCVNQT FAALITHSWY HKTFPKYPKT RKALIPYVL

References

[1]

"The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W. , Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A., Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E., Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K., Durbin R.M., Waterston R.H. PLoS Biol. 1:166-192(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16.

Cross-references

Sequence databases
EMBL GenBank DDBJ	HE600998 Genomic DNA. Translation: CAP29024.1.
RefSeq	XP_002637085.1. XM_002637039.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	6238.CBG09584.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	CBG09584; CBG09584; CBG09584.
GeneID	8579081.
KEGG	cbr:CBG09584.
Organism-specific databases
CTD	8579081.
WormBase	CBG09584; CBP16536; WBGene00031145.
Phylogenomic databases
eggNOG	NOG330066.
HOGENOM	HOG000018885.
KO	K12345.
OMA	THKWYLQ.
Enzyme and pathway databases
UniPathway	UPA00378.
Family and domain databases
InterPro	IPR001104. 3-oxo-5_a-steroid_4-DH_C. [Graphical view]
Pfam	PF02544. Steroid_dh. 1 hit. [Graphical view]
PROSITE	PS50244. S5A_REDUCTASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PORED_CAEBR

Accession

Primary (citable) accession number: A8X8R3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	January 15, 2008
Last modified:	April 3, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Caenorhabditis annotation project