D2HBV9 (PORED_AILME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polyprenol reductase
EC=1.3.1.94

Alternative name(s):
3-oxo-5-alpha-steroid 4-dehydrogenase 3
EC=1.3.1.22
Steroid 5-alpha-reductase 3
Short name=S5AR 3
Short name=SR type 3

Gene names

Name:	SRD5A3
ORF Names:	PANDA_008038

Organism

Ailuropoda melanoleuca (Giant panda) [Reference proteome]

Taxonomic identifier

9646 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Carnivora › Caniformia › Ursidae › Ailuropoda

Protein attributes

Sequence length	318 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. Also able to convert testosterone (T) into 5-alpha-dihydrotestosterone (DHT) By similarity.
Catalytic activity	Ditrans,polycis-dolichol + NADP+ = ditrans,polycis-polyprenol + NADPH. A 3-oxo-5-alpha-steroid + NADP+ = a 3-oxo-Delta(4)-steroid + 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 Inferred from sequence or structural similarity. Source: UniProtKB endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	3-oxo-5-alpha-steroid 4-dehydrogenase activity Inferred from sequence or structural similarity. Source: UniProtKB cholestenone 5-alpha-reductase activity Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 318	318	Polyprenol reductase		PRO_0000398648
Regions
	Topological domain	1 – 19	19	Cytoplasmic Potential
	Transmembrane	20 – 40	21	Helical; Potential
	Topological domain	41 – 80	40	Lumenal Potential
	Transmembrane	81 – 101	21	Helical; Potential
	Topological domain	102 – 119	18	Cytoplasmic Potential
	Transmembrane	120 – 140	21	Helical; Potential
	Topological domain	141 – 156	16	Lumenal Potential
	Transmembrane	157 – 177	21	Helical; Potential
	Topological domain	178 – 194	17	Cytoplasmic Potential
	Transmembrane	195 – 215	21	Helical; Potential
	Topological domain	216 – 265	50	Lumenal Potential
	Transmembrane	266 – 286	21	Helical; Potential
	Topological domain	287 – 318	32	Cytoplasmic Potential

Sequences

	Sequence		Length	Mass (Da)
	D2HBV9 [UniParc]. Last modified February 9, 2010. Version 1. Checksum: B0CD88A5D8E2667D	FASTA	318	36,775
	10 20 30 40 50 60 MAPWAAAQLW ALNPLRALWL TLAAAFLLTL LLQLVPPGLL PGCALFQDLI RYGKTKREGQ 70 80 90 100 110 120 SRPAVCRVFD VPKRYFSHFY IISALWNGFL LWHLTQSVFL GVPFPNWLHG LLRILGASQF 130 140 150 160 170 180 QGGELALSAF LVLVFLWLHS LRRLFECFYV SVFSNTVIHI VQYCFGLVYY VLTGLTVLSQ 190 200 210 220 230 240 VPMDGRNAYV IGKNLLMQAR WFHILGMLMF IWSSVHQYKC HVILGNLRKN KAGVVIHCNH 250 260 270 280 290 300 RIPFGDWFEY VSSPNYLAEL MIYISMAVTF GFHNLTWWLV VTYVFFSQAL SAFLSHKFYK 310 SKFVSYPKHR KAFLPFLF

References

[1]

"The sequence and de novo assembly of the giant panda genome." Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J. , Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J., Wang J. Nature 463:311-317(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	GL192668 Genomic DNA. Translation: EFB15787.1.
RefSeq	XP_002919412.1. XM_002919366.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100463734.
KEGG	aml:100463734.
Organism-specific databases
CTD	79644.
Phylogenomic databases
HOGENOM	HOG000018885.
KO	K12345.
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_AILME

Accession

Primary (citable) accession number: D2HBV9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	February 9, 2010
Last modified:	February 6, 2013
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program