Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aldehyde dehydrogenase family 16 member A1

Gene

Aldh16a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde dehydrogenase family 16 member A1
Gene namesi
Name:Aldh16a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1916998. Aldh16a1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 802802Aldehyde dehydrogenase family 16 member A1PRO_0000312987Add
BLAST

Proteomic databases

EPDiQ571I9.
MaxQBiQ571I9.
PaxDbiQ571I9.
PRIDEiQ571I9.

PTM databases

iPTMnetiQ571I9.
PhosphoSiteiQ571I9.

Expressioni

Gene expression databases

BgeeiQ571I9.
CleanExiMM_ALDH16A1.

Interactioni

Subunit structurei

Interacts with SPG21.By similarity

Protein-protein interaction databases

IntActiQ571I9. 4 interactions.
MINTiMINT-4113910.
STRINGi10090.ENSMUSP00000007977.

Structurei

3D structure databases

ProteinModelPortaliQ571I9.
SMRiQ571I9. Positions 44-486, 530-790.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiKOG2450. Eukaryota.
COG1012. LUCA.
HOGENOMiHOG000112558.
HOVERGENiHBG069396.
InParanoidiQ571I9.
OrthoDBiEOG7Q2N4V.
PhylomeDBiQ571I9.
TreeFamiTF329461.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR011408. Aldehyde_DH.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 2 hits.
[Graphical view]
PIRSFiPIRSF036490. Aldedh_dupl. 1 hit.
SUPFAMiSSF53720. SSF53720. 2 hits.

Sequencei

Sequence statusi: Complete.

Q571I9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATRVQPST REIFTTLEYG PVPESHACAL AWLDTHNRLL GHHVNGMWLK
60 70 80 90 100
PEHRNPAPCQ DPITGENLAS CLQAEAEDIA AAVEAAKIAF KAWSQLPGAA
110 120 130 140 150
RGQHLTRLAK VVQKHQRLLW TLESLVTGRA VREVRDGDVP LAQQLLQYHA
160 170 180 190 200
VQAHAQGDAL ADWQPVGVIG LILPTPFSFL DMMWRVCPAL AMGCTVVALV
210 220 230 240 250
PPAFPTPLLL AQLAGELGSF PGILNVVCGP ASLGPVLASQ PGVQKVAFCG
260 270 280 290 300
AVEEGRVLRR TLAGRGAELG LALGTESLLL LTDSADVDSA VEGVVDAVWS
310 320 330 340 350
DRSLGGLRLL IQESVWDEAM RRLQARMAQI RSGRGLDGAV DMGARGAAAR
360 370 380 390 400
DLAQSFVDEA QSQGGQVFQA GDVPSSSPFF SPALVSGLPP AAPCAQAEVP
410 420 430 440 450
WPVVMASPFR TVKEALALAN GTPRGGSASV WSERLGQALE LGYGLQVGTV
460 470 480 490 500
WINAHGLRDP AVPTGGCKES GSSWHGGPDG LYEYLQPLGT PSQESFLCEN
510 520 530 540 550
INYDTFGLAA SSILPSGPET GPSPAPPYGL FVGGRFQSPG TQSSRPIQDS
560 570 580 590 600
SGKVSSYVAE GGAKDIRGAV EAAHQAAPGW GAQSPRARAG LLWALAAALE
610 620 630 640 650
RRKPVLTSQL ERHGAAPTVA KTEVELSVRR LQTWGTRVQD QGQTLQVTGL
660 670 680 690 700
RGPVLRLREP LGVLAVVCPD EWPLLAFVSL LAPALAHGNA VVLVPSGACP
710 720 730 740 750
LLALEVCQDI APLFPAGLVS VVTGDRDHLT RCLALHQDVQ ALWYFGSAQG
760 770 780 790 800
SQFVEWASAG NLKSVWVNRG FPRAWDVEVQ GAGQELSLHA ARTKALWLPM

GD
Length:802
Mass (Da):84,756
Last modified:January 15, 2008 - v2
Checksum:i4853B80CAC29B9AE
GO

Sequence cautioni

The sequence BAD90125.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271A → T in BAE26175 (PubMed:16141072).Curated
Sequence conflicti166 – 1661V → M in BAD90125 (Ref. 1) Curated
Sequence conflicti186 – 1861V → I in BAD90125 (Ref. 1) Curated
Sequence conflicti282 – 2821T → M in BAC27074 (PubMed:16141072).Curated
Sequence conflicti282 – 2821T → M in BAE30615 (PubMed:16141072).Curated
Sequence conflicti282 – 2821T → M in BAE36234 (PubMed:16141072).Curated
Sequence conflicti282 – 2821T → M in BAE41680 (PubMed:16141072).Curated
Sequence conflicti282 – 2821T → M in AAH13548 (PubMed:15489334).Curated
Sequence conflicti359 – 3591E → V in BAE31742 (PubMed:16141072).Curated
Sequence conflicti405 – 4051M → K in BAE31742 (PubMed:16141072).Curated
Sequence conflicti622 – 6221T → I in BAD90125 (Ref. 1) Curated
Sequence conflicti622 – 6221T → I in BAC27074 (PubMed:16141072).Curated
Sequence conflicti622 – 6221T → I in BAE30615 (PubMed:16141072).Curated
Sequence conflicti622 – 6221T → I in BAE31742 (PubMed:16141072).Curated
Sequence conflicti622 – 6221T → I in BAE36234 (PubMed:16141072).Curated
Sequence conflicti622 – 6221T → I in BAE41680 (PubMed:16141072).Curated
Sequence conflicti622 – 6221T → I in AAH13548 (PubMed:15489334).Curated
Sequence conflicti773 – 7731R → K in BAC27074 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK220200 mRNA. Translation: BAD90125.1. Different initiation.
AK030673 mRNA. Translation: BAC27074.1.
AK144995 mRNA. Translation: BAE26175.1.
AK151691 mRNA. Translation: BAE30615.1.
AK153129 mRNA. Translation: BAE31742.1.
AK161198 mRNA. Translation: BAE36234.1.
AK170276 mRNA. Translation: BAE41680.1.
BC013548 mRNA. Translation: AAH13548.2.
CCDSiCCDS21231.1.
RefSeqiNP_666066.1. NM_145954.1.
UniGeneiMm.82139.

Genome annotation databases

GeneIDi69748.
KEGGimmu:69748.
UCSCiuc009gtr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK220200 mRNA. Translation: BAD90125.1. Different initiation.
AK030673 mRNA. Translation: BAC27074.1.
AK144995 mRNA. Translation: BAE26175.1.
AK151691 mRNA. Translation: BAE30615.1.
AK153129 mRNA. Translation: BAE31742.1.
AK161198 mRNA. Translation: BAE36234.1.
AK170276 mRNA. Translation: BAE41680.1.
BC013548 mRNA. Translation: AAH13548.2.
CCDSiCCDS21231.1.
RefSeqiNP_666066.1. NM_145954.1.
UniGeneiMm.82139.

3D structure databases

ProteinModelPortaliQ571I9.
SMRiQ571I9. Positions 44-486, 530-790.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ571I9. 4 interactions.
MINTiMINT-4113910.
STRINGi10090.ENSMUSP00000007977.

PTM databases

iPTMnetiQ571I9.
PhosphoSiteiQ571I9.

Proteomic databases

EPDiQ571I9.
MaxQBiQ571I9.
PaxDbiQ571I9.
PRIDEiQ571I9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi69748.
KEGGimmu:69748.
UCSCiuc009gtr.1. mouse.

Organism-specific databases

CTDi126133.
MGIiMGI:1916998. Aldh16a1.

Phylogenomic databases

eggNOGiKOG2450. Eukaryota.
COG1012. LUCA.
HOGENOMiHOG000112558.
HOVERGENiHBG069396.
InParanoidiQ571I9.
OrthoDBiEOG7Q2N4V.
PhylomeDBiQ571I9.
TreeFamiTF329461.

Miscellaneous databases

ChiTaRSiAldh16a1. mouse.
PROiQ571I9.
SOURCEiSearch...

Gene expression databases

BgeeiQ571I9.
CleanExiMM_ALDH16A1.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 2 hits.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR011408. Aldehyde_DH.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamiPF00171. Aldedh. 2 hits.
[Graphical view]
PIRSFiPIRSF036490. Aldedh_dupl. 1 hit.
SUPFAMiSSF53720. SSF53720. 2 hits.
ProtoNetiSearch...

Publicationsi

  1. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Spleen.
  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 and NOD.
    Tissue: Bone marrow macrophage, Dendritic cell, Head and Mammary gland.
  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].
    Strain: FVB/N.
    Tissue: Kidney.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiA16A1_MOUSE
AccessioniPrimary (citable) accession number: Q571I9
Secondary accession number(s): Q3U6I2
, Q3UMC3, Q8C0L4, Q8VD78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: July 6, 2016
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

The active site cysteine and glutamate residues are not conserved in this protein. Its activity is therefore unsure.Curated

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.