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Q9WUP4 (PORED_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Srd5a3
Synonyms:Srd5a2l
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length330 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.5

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. Ref.5

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Disruption phenotype

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. Ref.5

Sequence similarities

Belongs to the steroid 5-alpha reductase family. Polyprenol reductase subfamily.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9WUP4-1)

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: Q9WUP4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     200-330: VYVLGKNLLI...HRKAFLPFLF → GKWPCQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 330330Polyprenol reductase
PRO_0000317704

Regions

Topological domain1 – 1616Cytoplasmic Potential
Transmembrane17 – 3721Helical; Potential
Topological domain38 – 8043Lumenal Potential
Transmembrane81 – 10121Helical; Potential
Topological domain102 – 13231Cytoplasmic Potential
Transmembrane133 – 15321Helical; Potential
Topological domain154 – 16916Lumenal Potential
Transmembrane170 – 19021Helical; Potential
Topological domain191 – 20616Cytoplasmic Potential
Transmembrane207 – 22721Helical; Potential
Topological domain228 – 27750Lumenal Potential
Transmembrane278 – 29821Helical; Potential
Topological domain299 – 33032Cytoplasmic Potential

Natural variations

Alternative sequence200 – 330131VYVLG…LPFLF → GKWPCQ in isoform 2.
VSP_039779

Experimental info

Sequence conflict1091S → G in AAD30567. Ref.1
Sequence conflict1091S → G in AAI45648. Ref.4
Sequence conflict2981S → F in AAD30567. Ref.1
Sequence conflict2981S → F in AAI45648. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: A26CAB23B295D75C

FASTA33037,936
        10         20         30         40         50         60 
MAGWAGFELS ALNPLRTLWL ALAAAFLFAL LLQLAPARLL PSCALFQDLL RYGKTKQSGS 

        70         80         90        100        110        120 
RRPAVCRAFD VPKRYFSHFY VISVVWNGSL LWLLSQSLFL GAPFPNWLSA LLRTLGATQF 

       130        140        150        160        170        180 
QALEMESKAS RMPAAELALS AFLVLVFLWV HSLRRLFECF YVSVFSNAAI HVVQYCFGLV 

       190        200        210        220        230        240 
YYVLVGLTVL SQVPMDDKNV YVLGKNLLIQ ARWFHILGMV MFFWSSAHQY KCHVILSNLR 

       250        260        270        280        290        300 
RNKKGVVIHC QHRIPFGDWF EYVSSANYLA ELMIYISMAV TFGLHNLTWW LVVTYVFSSQ 

       310        320        330 
ALSAFFNHKF YRSTFVSYPK HRKAFLPFLF

« Hide

Isoform 2 [UniParc].

Checksum: FEFAA6DDA00C20D8
Show »

FASTA20523,032

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"SRD5A3 is required for converting polyprenol to dolichol and is mutated in a congenital glycosylation disorder."
Cantagrel V., Lefeber D.J., Ng B.G., Guan Z., Silhavy J.L., Bielas S.L., Lehle L., Hombauer H., Adamowicz M., Swiezewska E., De Brouwer A.P., Blumel P., Sykut-Cegielska J., Houliston S., Swistun D., Ali B.R., Dobyns W.B., Babovic-Vuksanovic D. expand/collapse author list , van Bokhoven H., Wevers R.A., Raetz C.R., Freeze H.H., Morava E., Al-Gazali L., Gleeson J.G.
Cell 142:203-217(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PATHWAY, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00221584.
IPI00885969.
RefSeqNP_065636.2. NM_020611.4.
UniGeneMm.289446.

3D structure databases

ProteinModelPortalQ9WUP4.
ModBaseSearch...

PTM databases

PhosphoSiteQ9WUP4.

Proteomic databases

PaxDbQ9WUP4.
PRIDEQ9WUP4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031143; ENSMUSP00000031143; ENSMUSG00000029233.
GeneID57357.
KEGGmmu:57357.
UCSCuc008xun.1. mouse.
uc008xuo.1. mouse.

Organism-specific databases

CTD79644.
MGIMGI:1930252. Srd5a3.

Phylogenomic databases

eggNOGNOG330066.
GeneTreeENSGT00500000044920.
HOGENOMHOG000018885.
HOVERGENHBG057797.
InParanoidQ3UU82.
KOK12345.
OMATHKWYLQ.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9WUP4.
BgeeQ9WUP4.
CleanExMM_SRD5A3.
GenevestigatorQ9WUP4.

Family and domain databases

InterProIPR001104. 3-oxo-5_a-steroid_4-DH_C.
[Graphical view]
PfamPF02544. Steroid_dh. 1 hit.
[Graphical view]
PROSITEPS50244. S5A_REDUCTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio313740.
SOURCESearch...

Entry information

Entry namePORED_MOUSE
AccessionPrimary (citable) accession number: Q9WUP4
Secondary accession number(s): D3YZB6 expand/collapse secondary AC list , D3Z3J5, Q3UU82, Q8BGE3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 5, 2010
Last modified: May 1, 2013
This is version 74 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents