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Protein

Polyprenol reductase

Gene

Srd5a3

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

Ditrans,polycis-dolichol + NADP+ = ditrans,polycis-polyprenol + NADPH.1 Publication
A 3-oxo-5-alpha-steroid + NADP+ = a 3-oxo-Delta(4)-steroid + NADPH.1 Publication

Pathwayi

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

ReactomeiREACT_279437. Synthesis of Dolichyl-phosphate.
REACT_281422. Androgen biosynthesis.
UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Srd5a3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi1308828. Srd5a3.

Subcellular locationi

  • Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei17 – 3721HelicalSequence AnalysisAdd
BLAST
Topological domaini38 – 8952LumenalSequence AnalysisAdd
BLAST
Transmembranei90 – 11021HelicalSequence AnalysisAdd
BLAST
Topological domaini111 – 13626CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei137 – 15721HelicalSequence AnalysisAdd
BLAST
Topological domaini158 – 16912LumenalSequence AnalysisAdd
BLAST
Transmembranei170 – 19021HelicalSequence AnalysisAdd
BLAST
Topological domaini191 – 20616CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei207 – 22721HelicalSequence AnalysisAdd
BLAST
Topological domaini228 – 27750LumenalSequence AnalysisAdd
BLAST
Transmembranei278 – 29821HelicalSequence AnalysisAdd
BLAST
Topological domaini299 – 33032CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Polyprenol reductasePRO_0000398650Add
BLAST

Proteomic databases

PRIDEiQ5RJM1.

Expressioni

Tissue specificityi

Expressed in the 2 tissues tested i.e. testis and liver.1 Publication

Gene expression databases

GenevestigatoriQ5RJM1.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003021.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG330066.
GeneTreeiENSGT00500000044920.
HOGENOMiHOG000018885.
HOVERGENiHBG057797.
InParanoidiQ5RJM1.
KOiK12345.
OMAiSHFYIVS.
OrthoDBiEOG72ZCFT.
PhylomeDBiQ5RJM1.
TreeFamiTF315011.

Family and domain databases

InterProiIPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5RJM1-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAGWAGAELS VLNPLRALWL LLAAAFLLAL LLQLAPARLL PSCALFQDLI
60 70 80 90 100
RYGKTKQSGS RRPAVCRAFD VPKRYFSHFY VVSVLWNGSL LWFLSQSLFL
110 120 130 140 150
GAPFPSWLWA LLRTLGVTQF QALGMESKAS RIQGKKLALS TFLVLVFLWV
160 170 180 190 200
HSLRRLFECF YVSVFSNTAI HVVQYCFGLV YYVLVGLTVL SQVPMNDKNV
210 220 230 240 250
YALGKNLLLQ ARWFHILGMM MFFWSSAHQY KCHVILSNLR RNKKGVVIHC
260 270 280 290 300
QHRIPFGDWF EYVSSANYLA ELMIYISMAV TFGLHNVTWW LVVTYVFFSQ
310 320 330
ALSAFFNHRF YKSTFVSYPK HRKAFLPFLF
Length:330
Mass (Da):38,092
Last modified:October 5, 2010 - v2
Checksum:iEC97594D66A76543
GO
Isoform 2 (identifier: Q5RJM1-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.

Show »
Length:278
Mass (Da):31,886
Checksum:iD1548EFDF67DD528
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1363GKK → AGE in AAH86584 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei262 – 33069YVSSA…LPFLF → LYGEERSPGDRFPSSRR in isoform 2. 1 PublicationVSP_039791Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC086584 mRNA. Translation: AAH86584.1.
RefSeqiNP_001014012.1. NM_001013990.1.
UniGeneiRn.819.

Genome annotation databases

EnsembliENSRNOT00000059763; ENSRNOP00000056514; ENSRNOG00000002216. [Q5RJM1-2]
GeneIDi305291.
KEGGirno:305291.
UCSCiRGD:1308828. rat. [Q5RJM1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC086584 mRNA. Translation: AAH86584.1.
RefSeqiNP_001014012.1. NM_001013990.1.
UniGeneiRn.819.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003021.

Proteomic databases

PRIDEiQ5RJM1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000059763; ENSRNOP00000056514; ENSRNOG00000002216. [Q5RJM1-2]
GeneIDi305291.
KEGGirno:305291.
UCSCiRGD:1308828. rat. [Q5RJM1-1]

Organism-specific databases

CTDi79644.
RGDi1308828. Srd5a3.

Phylogenomic databases

eggNOGiNOG330066.
GeneTreeiENSGT00500000044920.
HOGENOMiHOG000018885.
HOVERGENiHBG057797.
InParanoidiQ5RJM1.
KOiK12345.
OMAiSHFYIVS.
OrthoDBiEOG72ZCFT.
PhylomeDBiQ5RJM1.
TreeFamiTF315011.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_279437. Synthesis of Dolichyl-phosphate.
REACT_281422. Androgen biosynthesis.

Miscellaneous databases

NextBioi654334.
PROiQ5RJM1.

Gene expression databases

GenevestigatoriQ5RJM1.

Family and domain databases

InterProiIPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamiPF02544. Steroid_dh. 1 hit.
[Graphical view]
PROSITEiPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiPORED_RAT
AccessioniPrimary (citable) accession number: Q5RJM1
Secondary accession number(s): D3ZUS5, D4A5U7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 5, 2010
Last sequence update: October 5, 2010
Last modified: April 1, 2015
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.