Q5RJM1 (PORED_RAT) 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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). Ref.3
Catalytic activity	Ditrans,polycis-dolichol + NADP+ = ditrans,polycis-polyprenol + NADPH. Ref.3 A 3-oxo-5-alpha-steroid + NADP+ = a 3-oxo-Delta(4)-steroid + NADPH. Ref.3
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.3.
Tissue specificity	Expressed in the 2 tissues tested i.e. testis and liver. Ref.3
Sequence similarities	Belongs to the steroid 5-alpha reductase family. Polyprenol reductase subfamily.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing
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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q5RJM1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q5RJM1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     262-330: YVSSANYLAE...HRKAFLPFLF → LYGEERSPGDRFPSSRR

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 330	330	Polyprenol reductase		PRO_0000398650
Regions
	Topological domain	1 – 16	16	Cytoplasmic Potential
	Transmembrane	17 – 37	21	Helical; Potential
	Topological domain	38 – 89	52	Lumenal Potential
	Transmembrane	90 – 110	21	Helical; Potential
	Topological domain	111 – 136	26	Cytoplasmic Potential
	Transmembrane	137 – 157	21	Helical; Potential
	Topological domain	158 – 169	12	Lumenal Potential
	Transmembrane	170 – 190	21	Helical; Potential
	Topological domain	191 – 206	16	Cytoplasmic Potential
	Transmembrane	207 – 227	21	Helical; Potential
	Topological domain	228 – 277	50	Lumenal Potential
	Transmembrane	278 – 298	21	Helical; Potential
	Topological domain	299 – 330	32	Cytoplasmic Potential
Natural variations
	Alternative sequence	262 – 330	69	YVSSA…LPFLF → LYGEERSPGDRFPSSRR in isoform 2.		VSP_039791
Experimental info
	Sequence conflict	134 – 136	3	GKK → AGE in AAH86584. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 5, 2010. Version 2. Checksum: EC97594D66A76543	FASTA	330	38,092
	10 20 30 40 50 60 MAGWAGAELS VLNPLRALWL LLAAAFLLAL LLQLAPARLL PSCALFQDLI RYGKTKQSGS 70 80 90 100 110 120 RRPAVCRAFD VPKRYFSHFY VVSVLWNGSL LWFLSQSLFL GAPFPSWLWA LLRTLGVTQF 130 140 150 160 170 180 QALGMESKAS RIQGKKLALS TFLVLVFLWV HSLRRLFECF YVSVFSNTAI HVVQYCFGLV 190 200 210 220 230 240 YYVLVGLTVL SQVPMNDKNV YALGKNLLLQ ARWFHILGMM MFFWSSAHQY KCHVILSNLR 250 260 270 280 290 300 RNKKGVVIHC QHRIPFGDWF EYVSSANYLA ELMIYISMAV TFGLHNVTWW LVVTYVFFSQ 310 320 330 ALSAFFNHRF YKSTFVSYPK HRKAFLPFLF
	Isoform 2 [UniParc]. Checksum: D1548EFDF67DD528	FASTA	278	31,886
	10 20 30 40 50 60 MAGWAGAELS VLNPLRALWL LLAAAFLLAL LLQLAPARLL PSCALFQDLI RYGKTKQSGS 70 80 90 100 110 120 RRPAVCRAFD VPKRYFSHFY VVSVLWNGSL LWFLSQSLFL GAPFPSWLWA LLRTLGVTQF 130 140 150 160 170 180 QALGMESKAS RIQGKKLALS TFLVLVFLWV HSLRRLFECF YVSVFSNTAI HVVQYCFGLV 190 200 210 220 230 240 YYVLVGLTVL SQVPMNDKNV YALGKNLLLQ ARWFHILGMM MFFWSSAHQY KCHVILSNLR 250 260 270 RNKKGVVIHC QHRIPFGDWF ELYGEERSPG DRFPSSRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Ovary.
[3]	"Formation of dolichol from dehydrodolichol is catalyzed by NADPH-dependent reductase localized in microsomes of rat liver." Sagami H., Kurisaki A., Ogura K. J. Biol. Chem. 268:10109-10113(1993) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC086584 mRNA. Translation: AAH86584.1.
IPI	IPI00948156. IPI00969761.
RefSeq	NP_001014012.1. NM_001013990.1.
UniGene	Rn.819.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000003021.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000003021; ENSRNOP00000003021; ENSRNOG00000002216. ENSRNOT00000059763; ENSRNOP00000056514; ENSRNOG00000002216.
GeneID	305291.
KEGG	rno:305291.
UCSC	RGD:1308828. rat.
Organism-specific databases
CTD	79644.
RGD	1308828. Srd5a3.
Phylogenomic databases
eggNOG	NOG330066.
GeneTree	ENSGT00500000044920.
HOGENOM	HOG000018885.
HOVERGEN	HBG057797.
KO	K12345.
OrthoDB	EOG47D9H9.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Genevestigator	Q5RJM1.
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...
Other
NextBio	654334.

Entry information

Entry name

PORED_RAT

Accession

Primary (citable) accession number: Q5RJM1
Secondary accession number(s): D3ZUS5, D4A5U7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 5, 2010
Last sequence update:	October 5, 2010
Last modified:	April 3, 2013
This is version 50 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program