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Q8BH00 (AL8A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldehyde dehydrogenase family 8 member A1
EC=1.2.1.-
Alternative name(s):
Retinal dehydrogenase 4
Gene names
Name:Aldh8a1
Synonyms:Raldh4
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts 9-cis-retinal to 9-cis-retinoic acid. Has lower activity towards 13-cis-retinal. Has much lower activity towards all-trans-retinal. Has a preference for NAD, but shows considerable activity with NADP (in vitro) By similarity. Ref.1

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

Detected in hepatocytes and in proximal and distal convoluted tubules in kidney cortex (at protein level). Highly expressed in adult liver and in kidney cortex. First detected in embryonic liver after 15 days of development. Ref.1

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

Activity was measured with total soluble protein.

KM=2.3 µM for 9-cis-retinal Ref.1

Vmax=3.4 nmol/min/mg enzyme

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological process9-cis-retinoic acid biosynthetic process

Inferred from direct assay. Source: MGI

retinal metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionretinal dehydrogenase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 487487Aldehyde dehydrogenase family 8 member A1
PRO_0000312955

Regions

Nucleotide binding231 – 2366NAD By similarity

Sites

Active site2531Proton acceptor By similarity
Active site2871Nucleophile By similarity
Site1551Transition state stabilizer By similarity

Amino acid modifications

Modified residue831Phosphoserine By similarity

Natural variations

Natural variant1451V → G in strain: FVB/N. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8BH00 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 5E205A495BD61ED7

FASTA48753,664
        10         20         30         40         50         60 
MAGKRELLML ENFIGGKFLP CNSYIDSYDP STGEVYCKVP NSGKEEIEAA VEAAREAFPA 

        70         80         90        100        110        120 
WSSRSPQERS LVLNRLADVL EQSLEELAQA ESKDQGKTLT LARTMDIPRS VLNFRFFASS 

       130        140        150        160        170        180 
NLHHVSECTQ MSHLGCMHYT VRTPVGIAGL ISPWNLPLYL LTWKIAPAIA AGNTVIAKPS 

       190        200        210        220        230        240 
EMTSVTAWMF CKLLDKAGVP PGVINIVFGT GPRVGEALVS HPEVPLISFT GSQPTAERIT 

       250        260        270        280        290        300 
QLSAPHCKKL SLELGGKNPA IIFEDANLEE CIPATVRSSF ANQGEICLCT SRIFVQRSIY 

       310        320        330        340        350        360 
SEFLKRFVEA TRKWKVGVPS DPSANMGALI SKAHLEKVRS YVLKAQTEGA RILCGEGVDQ 

       370        380        390        400        410        420 
LSLPLRNQAG YFMLPTVITD IKDESRCMTE EIFGPVTCVV PFDSEEEVIT RANSVRYGLA 

       430        440        450        460        470        480 
ATVWSKDVGR IHRVAKKLQS GLVWTNCWLI RELNLPFGGM KSSGIGREGA KDSYDFFTEI 


KTITIKY

« Hide

References

« Hide 'large scale' references
[1]"Mouse retinal dehydrogenase 4 (RALDH4), molecular cloning, cellular expression, and activity in 9-cis-retinoic acid biosynthesis in intact cells."
Lin M., Zhang M., Abraham M., Smith S.M., Napoli J.L.
J. Biol. Chem. 278:9856-9861(2003) [PubMed: 12519776] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Embryo.
[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: Liver tumor and Spleen.
[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], VARIANT GLY-145.
Strain: FVB/N.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF510322 mRNA. Translation: AAO64246.1.
AK050298 mRNA. Translation: BAC34173.1.
AK143752 mRNA. Translation: BAE25524.1.
BC013511 mRNA. Translation: AAH13511.1.
BC038493 mRNA. Translation: AAH38493.1.
IPIIPI00267407.
RefSeqNP_848828.1. NM_178713.4.
UniGeneMm.90181.

3D structure databases

HSSPHSSP built from PDB template 2D4E based on UniProtKB Q5SJP9.
ProteinModelPortalQ8BH00.
SMRQ8BH00. Positions 10-487.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8BH00.

PTM databases

PhosphoSiteQ8BH00.

Proteomic databases

PRIDEQ8BH00.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042699; ENSMUSP00000038878; ENSMUSG00000037542.
GeneID237320.
KEGGmmu:237320.
UCSCuc007eoq.1. mouse.

Organism-specific databases

CTD64577.
MGIMGI:2653900. Aldh8a1.

Phylogenomic databases

eggNOGroNOG04187.
GeneTreeENSGT00560000077032.
HOGENOMHBG752218.
HOVERGENHBG000097.
InParanoidQ8BH00.
OMAITENRSG.
OrthoDBEOG45HRX8.
PhylomeDBQ8BH00.

Gene expression databases

ArrayExpressQ8BH00.
BgeeQ8BH00.
CleanExMM_ALDH8A1.
GenevestigatorQ8BH00.

Family and domain databases

InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio383298.
SOURCESearch...

Entry information

Entry nameAL8A1_MOUSE
AccessionPrimary (citable) accession number: Q8BH00
Secondary accession number(s): Q91WS6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2003
Last modified: September 21, 2011
This is version 73 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

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