Reviewed, UniProtKB/Swiss-Prot Q28399 (ALDH1_ELEED)

Names and origin

Protein names

Recommended name:
    Aldehyde dehydrogenase, cytosolic 1
    EC=1.2.1.3
Alternative name(s):
    ALDH class 1
    ETA-crystallin

Gene names

Name:

ALDH1

Organism

Elephantulus edwardii (Cape long-eared elephant shrew)

Taxonomic identifier

28737 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Afrotheria › Macroscelidea › Macroscelididae › Elephantulus

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Major component of the eye of elephant shrews, which in contrast to other mammals, possesses both a lens- and a non-lens class-1 aldehyde dehydrogenase 1. This eye-specific form is a structural protein of the lens and, in other part of the eye, serves as the major form of ALDH1. Can convert/oxidize retinaldehyde to retinoic acid.
Catalytic activity	An aldehyde + NAD(+) + H(2)O = an acid + NADH.
Pathway	Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.
Subunit structure	Homotetramer.
Subcellular location	CytoplasmBy similarity.
Tissue specificity	Eye specific, with very high expression in the lens.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aldehyde dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 501

501

Aldehyde dehydrogenase, cytosolic 1

PRO_0000056427

Regions

Nucleotide binding

246 – 251

6

NAD

Sites

Active site

269

1

Proton acceptor

Active site

303

1

Nucleophile

Site

170

1

Transition state stabilizer

Secondary structure

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501

Helix Strand Turn

Details...

Beta strand

22 – 25

4

Beta strand

28 – 30

3

Beta strand

37 – 41

5

Turn

43 – 45

3

Beta strand

48 – 53

6

Helix

57 – 71

15

Helix

76 – 79

4

Helix

82 – 98

17

Helix

100 – 111

12

Helix

115 – 120

6

Helix

122 – 136

15

Helix

137 – 139

3

Beta strand

142 – 145

4

Beta strand

148 – 159

12

Beta strand

162 – 166

5

Helix

172 – 185

14

Beta strand

189 – 193

5

Helix

200 – 212

13

Beta strand

218 – 221

4

Turn

226 – 228

3

Helix

229 – 234

6

Beta strand

241 – 246

6

Helix

248 – 260

13

Beta strand

265 – 269

5

Beta strand

274 – 278

5

Helix

284 – 296

13

Helix

297 – 300

4

Beta strand

306 – 312

7

Helix

313 – 326

14

Helix

348 – 364

17

Beta strand

367 – 370

4

Beta strand

373 – 379

7

Beta strand

385 – 390

6

Helix

395 – 398

4

Beta strand

403 – 411

9

Helix

414 – 422

9

Beta strand

423 – 425

3

Beta strand

428 – 433

6

Helix

437 – 446

10

Beta strand

449 – 455

7

Helix

470 – 472

3

Beta strand

473 – 475

3

Helix

479 – 483

5

Helix

484 – 486

3

Beta strand

487 – 495

9

Sequences

	Sequence		Length	Mass (Da)
	Q28399-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 9E3D5BBE083ACAD7	FASTA	501	54,538
	10 20 30 40 50 60 MSSSGMPDLP APLTNIKIQH TKLFINNEWH ESVSGKTFPV FNPATEEKIC EVEEADKEDV 70 80 90 100 110 120 DKAVKAAREA FQMGSPWRTM DASERGQLIY KLADLIERDR LLLATLESIN AGKVFASAYL 130 140 150 160 170 180 MDLDYCIKAL RYCAGWADKI QGRTIPVDGE FFSYTRHEPI GVCGLIFPWN APMILLACKI 190 200 210 220 230 240 GPALCCGNTV IVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDVD 250 260 270 280 290 300 KVAFTGSTEV GKMIQEAAAK SNLKRVTLEL GAKNPCIVFA DADLDSAVEF AHQGVFTNQG 310 320 330 340 350 360 QSCIAASKLF VEEAIYDEFV QRSVERAKKY VFGNPLTPGV NHGPQINKAQ HNKIMELIES 370 380 390 400 410 420 GKKEGAKLEC GGGPWGNKGY FIQPTVFSNV TDDMRIAKEE IFGPVQQIMK FKSLDEVIKR 430 440 450 460 470 480 ANNTYYGLVA GVFTKDLDKA VTVSSALQAG TVWVNCYLAA SAQSPAGGFK MSGHGREMGE 490 500 YGIHEYTEVK TVTMKISEKN S

References

[1]	"A retinaldehyde dehydrogenase as a structural protein in a mammalian eye lens. Gene recruitment of eta-crystallin." Graham C., Hodin J., Wistow G. J. Biol. Chem. 271:15623-15628(1996) [PubMed: 8663049] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lens.
[2]	"Crystal structure of eta-crystallin: adaptation of a class 1 aldehyde dehydrogenase for a new role in the eye lens." Bateman O.A., Purkiss A.G., van Montfort R., Slingsby C., Graham C., Wistow G. Biochemistry 42:4349-4356(2003) [PubMed: 12693930] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH NAD, FUNCTION, HOMOTETRAMERIZATION.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U02483 mRNA. Translation: AAB60268.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1O9J	X-ray	2.40	A/B/C/D	1-501	[»]
1PEJ	model	-	A	1-501	[»]

ModBase

Search...

Phylogenomic databases

HOVERGEN

Q28399.

Family and domain databases

InterPro

IPR016160. Ald_DHase_CS.
IPR016162. Ald_DHase_N.
IPR015590. Aldehyde_DHase.
[Graphical view]

Gene3D

G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.

PANTHER

PTHR11699. Aldehyde_dehyd. 1 hit.

Pfam

PF00171. Aldedh. 1 hit.
[Graphical view]

PROSITE

PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. False negative.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ALDH1_ELEED

Accession

Primary (citable) accession number: Q28399

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	November 4, 2008
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)