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Protein

Aldehyde dehydrogenase family 8 member A1

Gene

Aldh8a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity1 Publication

Kineticsi

Activity was measured with total soluble protein.

  1. KM=2.3 µM for 9-cis-retinal1 Publication
  1. Vmax=3.4 nmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei155 – 1551Transition state stabilizerBy similarity
Active sitei253 – 2531Proton acceptorPROSITE-ProRule annotation
Active sitei287 – 2871NucleophilePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi231 – 2366NADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.2.1.3. 3474.
ReactomeiR-MMU-5365859. RA biosynthesis pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde dehydrogenase family 8 member A1 (EC:1.2.1.-)
Alternative name(s):
Retinal dehydrogenase 4
Gene namesi
Name:Aldh8a1
Synonyms:Raldh4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:2653900. Aldh8a1.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 487487Aldehyde dehydrogenase family 8 member A1PRO_0000312955Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei362 – 3621PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BH00.
MaxQBiQ8BH00.
PaxDbiQ8BH00.
PRIDEiQ8BH00.

PTM databases

iPTMnetiQ8BH00.
PhosphoSiteiQ8BH00.
SwissPalmiQ8BH00.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ8BH00.
CleanExiMM_ALDH8A1.
ExpressionAtlasiQ8BH00. baseline and differential.
GenevisibleiQ8BH00. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8BH00. 4 interactions.
MINTiMINT-4110439.
STRINGi10090.ENSMUSP00000038878.

Structurei

3D structure databases

ProteinModelPortaliQ8BH00.
SMRiQ8BH00. Positions 9-485.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiKOG2450. Eukaryota.
COG1012. LUCA.
GeneTreeiENSGT00840000129927.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiQ8BH00.
OMAiGEALVCH.
OrthoDBiEOG7FV3Q2.
PhylomeDBiQ8BH00.
TreeFamiTF314129.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BH00-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGKRELLML ENFIGGKFLP CNSYIDSYDP STGEVYCKVP NSGKEEIEAA
60 70 80 90 100
VEAAREAFPA WSSRSPQERS LVLNRLADVL EQSLEELAQA ESKDQGKTLT
110 120 130 140 150
LARTMDIPRS VLNFRFFASS NLHHVSECTQ MSHLGCMHYT VRTPVGIAGL
160 170 180 190 200
ISPWNLPLYL LTWKIAPAIA AGNTVIAKPS EMTSVTAWMF CKLLDKAGVP
210 220 230 240 250
PGVINIVFGT GPRVGEALVS HPEVPLISFT GSQPTAERIT QLSAPHCKKL
260 270 280 290 300
SLELGGKNPA IIFEDANLEE CIPATVRSSF ANQGEICLCT SRIFVQRSIY
310 320 330 340 350
SEFLKRFVEA TRKWKVGVPS DPSANMGALI SKAHLEKVRS YVLKAQTEGA
360 370 380 390 400
RILCGEGVDQ LSLPLRNQAG YFMLPTVITD IKDESRCMTE EIFGPVTCVV
410 420 430 440 450
PFDSEEEVIT RANSVRYGLA ATVWSKDVGR IHRVAKKLQS GLVWTNCWLI
460 470 480
RELNLPFGGM KSSGIGREGA KDSYDFFTEI KTITIKY
Length:487
Mass (Da):53,664
Last modified:March 1, 2003 - v1
Checksum:i5E205A495BD61ED7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti145 – 1451V → G in strain: FVB/N. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23723.1.
RefSeqiNP_848828.1. NM_178713.4.
UniGeneiMm.90181.

Genome annotation databases

EnsembliENSMUST00000042699; ENSMUSP00000038878; ENSMUSG00000037542.
GeneIDi237320.
KEGGimmu:237320.
UCSCiuc007eoq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23723.1.
RefSeqiNP_848828.1. NM_178713.4.
UniGeneiMm.90181.

3D structure databases

ProteinModelPortaliQ8BH00.
SMRiQ8BH00. Positions 9-485.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BH00. 4 interactions.
MINTiMINT-4110439.
STRINGi10090.ENSMUSP00000038878.

PTM databases

iPTMnetiQ8BH00.
PhosphoSiteiQ8BH00.
SwissPalmiQ8BH00.

Proteomic databases

EPDiQ8BH00.
MaxQBiQ8BH00.
PaxDbiQ8BH00.
PRIDEiQ8BH00.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000042699; ENSMUSP00000038878; ENSMUSG00000037542.
GeneIDi237320.
KEGGimmu:237320.
UCSCiuc007eoq.1. mouse.

Organism-specific databases

CTDi64577.
MGIiMGI:2653900. Aldh8a1.

Phylogenomic databases

eggNOGiKOG2450. Eukaryota.
COG1012. LUCA.
GeneTreeiENSGT00840000129927.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiQ8BH00.
OMAiGEALVCH.
OrthoDBiEOG7FV3Q2.
PhylomeDBiQ8BH00.
TreeFamiTF314129.

Enzyme and pathway databases

BRENDAi1.2.1.3. 3474.
ReactomeiR-MMU-5365859. RA biosynthesis pathway.

Miscellaneous databases

NextBioi383298.
PROiQ8BH00.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BH00.
CleanExiMM_ALDH8A1.
ExpressionAtlasiQ8BH00. baseline and differential.
GenevisibleiQ8BH00. MM.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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].
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT GLY-145.
    Strain: FVB/N.
    Tissue: Kidney.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney and Liver.

Entry informationi

Entry nameiAL8A1_MOUSE
AccessioniPrimary (citable) accession number: Q8BH00
Secondary accession number(s): Q91WS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 109 of the entry and version 1 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.