Reviewed, UniProtKB/Swiss-Prot Q28452 (QOR_LAMGU)

Names and origin

Protein names

Recommended name:
    Quinone oxidoreductase
    EC=1.6.5.5
Alternative name(s):
    NADPH:quinone reductase
    Zeta-crystallin

Gene names

Name:

CRYZ

Organism

Lama guanicoe (Guanaco)

Taxonomic identifier

9840 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Tylopoda › Camelidae › Lama

Protein attributes

Sequence length	330 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Does not have alcohol dehydrogenase activity. Binds NADP and acts through a one-electron transfer process. Orthoquinones are the best substrates. May act in the detoxification of xenobiotics By similarity.
Catalytic activity	NADPH + 2 quinone = NADP+ + 2 semiquinone.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	NADPH:quinone reductase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 330	330	Quinone oxidoreductase		PRO_0000160907

Sequences

	Sequence		Length	Mass (Da)
	Q28452-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E784E414D2BA23D6	FASTA	330	35,187
	10 20 30 40 50 60 MATGQRLMRA IRVSEFGGPE VLKLQSDVAV PIPEEHQVLI KVQACGVNPV DTYIRSGTYS 70 80 90 100 110 120 RKPRLPYTPG LDVAGLIEAV GERVSAFKKG DRVFTTSTVS GGYAEYALAA DHTVYKLPGE 130 140 150 160 170 180 LDFQKGAAIG VPYFTAYRAL LHSACAKAGE SVLVHGASGG VGLAACQIAR ACCFKVLGTA 190 200 210 220 230 240 GTEEGQRVVL QNGAHEVFNH REDINIDKIK KSVGEKGIDV IIEMLANVNL SNDLNLLSQG 250 260 270 280 290 300 GRVIIVGSKG PVEINPRDTM TKESSIKGVT LFSSTKEEFQ QFAAALQAGM EIGWLRPVIG 310 320 330 SQYPLEKVAQ AHEDLTHSSG AAGKVVLLLK

References

[1]

"Evidence for independent recruitment of zeta-crystallin/quinone reductase (CRYZ) as a crystallin in camelids and hystricomorph rodents." Gonzalez P., Rao P.V., Nunez S.B., Zigler J.S. Jr. Mol. Biol. Evol. 12:773-781(1995) [PubMed: 7476124] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lens.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L34159 mRNA. Translation: AAA99986.1.
3D structure databases
HSSP	HSSP built from PDB template 1QOR based on UniProtKB P28304.
SMR	Q28452. Positions 6-329.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q28452.
Enzyme and pathway databases
BRENDA	1.6.5.5. 292454.
Family and domain databases
InterPro	IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn. IPR013149. ADH_Zn-bd. IPR002364. Quin_OxRdtase/zeta-crystal_CS. [Graphical view]
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
PROSITE	PS01162. QOR_ZETA_CRYSTAL. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

QOR_LAMGU

Accession

Primary (citable) accession number: Q28452

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)