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Reviewed, UniProtKB/Swiss-Prot Q8VC28 (AK1CD_MOUSE)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Aldo-keto reductase family 1 member C13
    EC=1.1.1.-
Gene names
Name: Akr1c13
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Sequence similarities

Belongs to the aldo/keto reductase family.

Ontologies

Keywords
   LigandNAD
NADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

xenobiotic metabolic process Ref.1

Traceable author statement. Source: MGI

   Molecular functionoxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 323323Aldo-keto reductase family 1 member C13
PRO_0000124644

Regions

Nucleotide binding13 – 2210NADP Potential
Nucleotide binding217 – 28064NADP By similarity

Sites

Active site551Proton donor By similarity
Binding site1171Substrate By similarity
Site841Lowers pKa of active site Tyr By similarity

Experimental info

Sequence conflict471R → L in BAA86850. Ref.1
Sequence conflict811I → V in AAH21937. Ref.3
Sequence conflict1831K → N in BAB25986. Ref.2
Sequence conflict2261E → K in BAA86850. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8VC28-1 [UniParc].

Last modified January 17, 2003. Version 2.
Checksum: 8B51A5820402AE5A

FASTA32337,058
        10         20         30         40         50         60 
MSSKQHCVKL NDGHLIPALG FGTYKPKEVP KSKSLEAACL ALDVGYRHVD TAYAYQVEEE 

        70         80         90        100        110        120 
IGQAIQSKIK AGVVKREDLF ITTKLWCTCF RPELVKPALE KSLKKLQLDY VDLYIMHYPV 

       130        140        150        160        170        180 
PMKSGDNDFP VNEQGKSLLD TVDFCDTWER LEECKDAGLV KSIGVSNFNH RQLERILNKP 

       190        200        210        220        230        240 
GLKYKPVCNQ VECHLYLNQR KLLDYCESKD IVLVAYGALG TQRYKEWVDQ NSPVLLNDPV 

       250        260        270        280        290        300 
LCDVAKKNKR SPALIALRYL IQRGIVPLAQ SFKENEMREN LQVFGFQLSP EDMKTLDGLN 

       310        320 
KNFRYLPAEF LVDHPEYPFV EEY 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of two novel aldo-keto reductases (AKR1C12 and AKR1C13) from mouse stomach."
Ikeda S., Okuda-Ashitaka E., Masu Y., Suzuki T., Watanabe K., Nakao M., Shingu K., Ito S.
FEBS Lett. 459:433-437(1999) [PubMed: 10526179] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Stomach.
[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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Stomach.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[4]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 201-209, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB027125 mRNA. Translation: BAA86850.1.
AK008949 mRNA. Translation: BAB25986.1.
BC021937 mRNA. Translation: AAH21937.1.
IPIIPI00310658.
RefSeqNP_038806.2.
UniGeneMm.27447

3D structure databases

HSSPHSSP built from PDB template 1J96 based on UniProtKB P52895.
ModBaseSearch...

Genome annotation databases

EnsemblENSMUSG00000021213. Mus musculus. [Contig view]
GeneID27384.
KEGGmmu:27384.

Organism-specific databases

MGIMGI:1351662. Akr1c13.

Phylogenomic databases

HOVERGENQ8VC28.
OMAQ8VC28. MHYPVPM.

Gene expression databases

ArrayExpressQ8VC28.
BgeeQ8VC28.
CleanExMM_AKR1C13.
GermOnlineENSMUSG00000021213. Mus musculus.

Family and domain databases

InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHERPTHR11732. Aldo/ket_red. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
ProDomPD000288. Aldo/ket_red. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio305324.
SOURCESearch...

Entry information

Entry nameAK1CD_MOUSE
AccessionPrimary (citable) accession number: Q8VC28
Secondary accession number(s): Q9D7R9, Q9R0M9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: January 17, 2003
Last modified: June 16, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents