Q64FG0 (RETST_MACFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
All-trans-retinol 13,14-reductase
EC=1.3.99.23

Alternative name(s):
All-trans-13,14-dihydroretinol saturase
Short name=RetSat
PPAR-alpha-regulated and starvation-induced gene protein

Gene names

Name:	RETSAT
Synonyms:	PPSIG

Organism

Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)

Taxonomic identifier

9541 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca

Protein attributes

Sequence length	610 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Retinol saturase carrying out the saturation of the 13-14 double bond of all-trans-retinol to produce all-trans-13,14-dihydroretinol. Has activity toward all-trans-retinol as substrate. Does not use all-trans-retinoic acid nor 9-cis, 11-cis or 13-cis-retinol isomers as substrates. May play a role in the metabolism of vitamin A By similarity.
Catalytic activity	All-trans-13,14-dihydroretinol + acceptor = all-trans-retinol + reduced acceptor.
Cofactor	NAD, NADP, or FAD By similarity.
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein By similarity.
Sequence similarities	Belongs to the carotenoid/retinoid oxidoreductase family. CrtISO subfamily.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal
Ligand	FAD Flavoprotein NAD NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	retinol metabolic process Inferred from sequence or structural similarity Ref.1. Source: HGNC
Cellular component	endoplasmic reticulum membrane Inferred from sequence or structural similarity Ref.1. Source: HGNC nuclear outer membrane Inferred from sequence or structural similarity Ref.1. Source: HGNC
Molecular function	all-trans-retinol 13,14-reductase activity Inferred from sequence or structural similarity Ref.1. Source: HGNC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Chain	19 – 610	592	All-trans-retinol 13,14-reductase		PRO_0000225666
Regions
	Nucleotide binding	70 – 98	29	FAD or NAD or NADP Potential

Sequences

	Sequence		Length	Mass (Da)
	Q64FG0 [UniParc]. Last modified October 25, 2004. Version 1. Checksum: FD74D22F28129FB1	FASTA	610	66,918
	10 20 30 40 50 60 MWLPLVLFLA VLLLAVVCKV YLGLFSGKSP NPFSEDVKRP PAPLVTDKEA RKKVLKQAFS 70 80 90 100 110 120 ASRVPEKLDV VVIGSGFGGL AAAAILAKAG KRVLVLEQHT KAGGACHTFG ENGLEFDTGI 130 140 150 160 170 180 HYIGRMEEGS IGRFILDQIT EGQLDWVPMS SPFDIMVLEG PNGRKEYPMY SGEKAYIQGL 190 200 210 220 230 240 KEKFPQEEAI IDKYIKLVKV VSNGVAHAIL LKFLPLPVIQ LLDRCGLLTR FSPFLHASTQ 250 260 270 280 290 300 SLAEVLQQLG ASSELQAVLS YIFPTYGVTP RHSAFSMHAL LVNHYLKGAF YPRGGSSEIA 310 320 330 340 350 360 FHTIPVIQRA GGAVLTRATV QSVLLDSAGK ACGVSVKKGH ELVNIYCPVV VSNAGLFNTY 370 380 390 400 410 420 EHLLPGNARC LPGVKQQLGM VRPGLGMMSV FICLQGTKED LHLPSTNYYV YHDTDMDQAM 430 440 450 460 470 480 ERYVSMPREK AAEHIPLLFI AFPSAKDPTW EDRFPGRSSM IMLIPSAYEW FEEWQAELKG 490 500 510 520 530 540 KRGSDYETYK NSFVEASMSV AMKLFPQLEG KVESVTAGSP LTNQFYLAAP RGACYGADHD 550 560 570 580 590 600 LGRLHPRVMA SLRAQSPIPN LYLTGQDIFT CGLVGALQGA LLCSSAILKR NLYSDLKDLG 610 SRIQAQKKKN

References

[1]	"Identification of all-trans-retinol: all-trans-13,14-dihydroretinol saturase." Moise A.R., Kuksa V., Imanishi Y., Palczewski K. J. Biol. Chem. 279:50230-50242(2004) [PubMed: 15358783] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY707524 mRNA. Translation: AAU34019.1.
3D structure databases
ProteinModelPortal	Q64FG0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG079484.
Family and domain databases
InterPro	IPR003953. FAD_bind2_N. [Graphical view]
Pfam	PF00890. FAD_binding_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RETST_MACFA

Accession

Primary (citable) accession number: Q64FG0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	October 25, 2004
Last modified:	September 21, 2011
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program