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Protein

Polyprenol reductase

Gene

Srd5a3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.
A 3-oxo-5-alpha-steroid + NADP+ = a 3-oxo-Delta(4)-steroid + NADPH.

Pathway:iprotein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.1 Publication
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

  • dolichol-linked oligosaccharide biosynthetic process Source: UniProtKB
  • dolichol metabolic process Source: UniProtKB
  • polyprenol catabolic process Source: UniProtKB
  • protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BRENDAi1.3.1.94. 3474.
ReactomeiREACT_272160. Synthesis of Dolichyl-phosphate.
REACT_305222. 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 2-like
Steroid 5-alpha-reductase 3
Short name:
S5AR 3
Short name:
SR type 3
Gene namesi
Name:Srd5a3
Synonyms:Srd5a2l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1930252. Srd5a3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1616CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei17 – 3721HelicalSequence AnalysisAdd
BLAST
Topological domaini38 – 8043LumenalSequence AnalysisAdd
BLAST
Transmembranei81 – 10121HelicalSequence AnalysisAdd
BLAST
Topological domaini102 – 13231CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei133 – 15321HelicalSequence AnalysisAdd
BLAST
Topological domaini154 – 16916LumenalSequence 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

Pathology & Biotechi

Disruption phenotypei

Death by E12.5. At E10.5, embryos are smaller and fail to undergo axial rotation observed at E8.5 in wild-types and present dilated hearts and open neural tubes.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 330330Polyprenol reductasePRO_0000317704Add
BLAST

Proteomic databases

MaxQBiQ9WUP4.
PaxDbiQ9WUP4.
PRIDEiQ9WUP4.

PTM databases

PhosphoSiteiQ9WUP4.

Expressioni

Gene expression databases

BgeeiQ9WUP4.
CleanExiMM_SRD5A3.
ExpressionAtlasiQ9WUP4. baseline and differential.
GenevisibleiQ9WUP4. MM.

Interactioni

Protein-protein interaction databases

BioGridi208270. 1 interaction.
STRINGi10090.ENSMUSP00000031143.

Structurei

3D structure databases

ProteinModelPortaliQ9WUP4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG330066.
GeneTreeiENSGT00500000044920.
HOGENOMiHOG000018885.
HOVERGENiHBG057797.
InParanoidiQ9WUP4.
KOiK12345.
OMAiLVFVWLH.
OrthoDBiEOG72ZCFT.
PhylomeDBiQ9WUP4.
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: Q9WUP4-1) [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
MAGWAGFELS ALNPLRTLWL ALAAAFLFAL LLQLAPARLL PSCALFQDLL
60 70 80 90 100
RYGKTKQSGS RRPAVCRAFD VPKRYFSHFY VISVVWNGSL LWLLSQSLFL
110 120 130 140 150
GAPFPNWLSA LLRTLGATQF QALEMESKAS RMPAAELALS AFLVLVFLWV
160 170 180 190 200
HSLRRLFECF YVSVFSNAAI HVVQYCFGLV YYVLVGLTVL SQVPMDDKNV
210 220 230 240 250
YVLGKNLLIQ ARWFHILGMV MFFWSSAHQY KCHVILSNLR RNKKGVVIHC
260 270 280 290 300
QHRIPFGDWF EYVSSANYLA ELMIYISMAV TFGLHNLTWW LVVTYVFSSQ
310 320 330
ALSAFFNHKF YRSTFVSYPK HRKAFLPFLF
Length:330
Mass (Da):37,936
Last modified:October 5, 2010 - v2
Checksum:iA26CAB23B295D75C
GO
Isoform 2 (identifier: Q9WUP4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     200-330: VYVLGKNLLI...HRKAFLPFLF → GKWPCQ

Note: No experimental confirmation available.
Show »
Length:205
Mass (Da):23,032
Checksum:iFEFAA6DDA00C20D8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti109 – 1091S → G in AAD30567 (PubMed:11116088).Curated
Sequence conflicti109 – 1091S → G in AAI45648 (PubMed:15489334).Curated
Sequence conflicti298 – 2981S → F in AAD30567 (PubMed:11116088).Curated
Sequence conflicti298 – 2981S → F in AAI45648 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei200 – 330131VYVLG…LPFLF → GKWPCQ in isoform 2. 1 PublicationVSP_039779Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF146793 Genomic DNA. Translation: AAD30567.1.
AK040198 mRNA. Translation: BAC30537.1.
AK075635 mRNA. Translation: BAC35871.1.
AK138681 mRNA. Translation: BAE23745.1.
AK139290 mRNA. Translation: BAE23944.1.
AK162527 mRNA. Translation: BAE36955.1.
AC147239 Genomic DNA. No translation available.
BC145647 mRNA. Translation: AAI45648.1.
CCDSiCCDS19358.1. [Q9WUP4-1]
RefSeqiNP_065636.2. NM_020611.4. [Q9WUP4-1]
UniGeneiMm.289446.

Genome annotation databases

EnsembliENSMUST00000031143; ENSMUSP00000031143; ENSMUSG00000029233. [Q9WUP4-1]
GeneIDi57357.
KEGGimmu:57357.
UCSCiuc008xun.2. mouse. [Q9WUP4-2]
uc008xuo.2. mouse. [Q9WUP4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF146793 Genomic DNA. Translation: AAD30567.1.
AK040198 mRNA. Translation: BAC30537.1.
AK075635 mRNA. Translation: BAC35871.1.
AK138681 mRNA. Translation: BAE23745.1.
AK139290 mRNA. Translation: BAE23944.1.
AK162527 mRNA. Translation: BAE36955.1.
AC147239 Genomic DNA. No translation available.
BC145647 mRNA. Translation: AAI45648.1.
CCDSiCCDS19358.1. [Q9WUP4-1]
RefSeqiNP_065636.2. NM_020611.4. [Q9WUP4-1]
UniGeneiMm.289446.

3D structure databases

ProteinModelPortaliQ9WUP4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208270. 1 interaction.
STRINGi10090.ENSMUSP00000031143.

PTM databases

PhosphoSiteiQ9WUP4.

Proteomic databases

MaxQBiQ9WUP4.
PaxDbiQ9WUP4.
PRIDEiQ9WUP4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031143; ENSMUSP00000031143; ENSMUSG00000029233. [Q9WUP4-1]
GeneIDi57357.
KEGGimmu:57357.
UCSCiuc008xun.2. mouse. [Q9WUP4-2]
uc008xuo.2. mouse. [Q9WUP4-1]

Organism-specific databases

CTDi79644.
MGIiMGI:1930252. Srd5a3.

Phylogenomic databases

eggNOGiNOG330066.
GeneTreeiENSGT00500000044920.
HOGENOMiHOG000018885.
HOVERGENiHBG057797.
InParanoidiQ9WUP4.
KOiK12345.
OMAiLVFVWLH.
OrthoDBiEOG72ZCFT.
PhylomeDBiQ9WUP4.
TreeFamiTF315011.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi1.3.1.94. 3474.
ReactomeiREACT_272160. Synthesis of Dolichyl-phosphate.
REACT_305222. Androgen biosynthesis.

Miscellaneous databases

NextBioi313740.
PROiQ9WUP4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WUP4.
CleanExiMM_SRD5A3.
ExpressionAtlasiQ9WUP4. baseline and differential.
GenevisibleiQ9WUP4. MM.

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. "The mouse Clock locus: sequence and comparative analysis of 204 kb from mouse chromosome 5."
    Wilsbacher L.D., Sangoram A.M., Antoch M.P., Takahashi J.S.
    Genome Res. 10:1928-1940(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Cerebellum, Thymus and Urinary bladder.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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 1).
    Tissue: Brain.
  5. Cited for: FUNCTION, PATHWAY, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiPORED_MOUSE
AccessioniPrimary (citable) accession number: Q9WUP4
Secondary accession number(s): D3YZB6
, D3Z3J5, Q3UU82, Q8BGE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 5, 2010
Last modified: July 22, 2015
This is version 93 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.