Reviewed, UniProtKB/Swiss-Prot Q6NUM9 (RETST_HUMAN)

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

Gene names

Name:	RETSAT
ORF Names:	UNQ439/PRO872

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal
Ligand	FAD Flavoprotein NAD NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from sequence or structural similarity. Source: HGNC retinol metabolic process Inferred from sequence or structural similarity. Source: HGNC
Cellular component	endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: HGNC extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear outer membrane Inferred from sequence or structural similarity. Source: HGNC
Molecular function	all-trans-retinol 13,14-reductase activity Inferred from sequence or structural similarity. Source: HGNC electron carrier activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q6NUM9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q6NUM9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     457-481: RSTMIMLIPTAYEWFEEWQAELKGK → GECDCRIPTHQPVLSGCSPRCLLRG
     482-610: Missing.

Note: No experimental confirmation available.

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_0000225665
Regions
	Nucleotide binding	70 – 98	29	FAD or NAD or NADP Potential
Natural variations
	Alternative sequence	457 – 481	25	RSTMI…ELKGK → GECDCRIPTHQPVLSGCSPR CLLRG in isoform 2.		VSP_017410
	Alternative sequence	482 – 610	129	Missing in isoform 2.		VSP_017411
	Natural variant	533	1	A → V: dbSNP rs4832169.		VAR_025473
	Natural variant	536	1	G → R: dbSNP rs4832168.		VAR_059243
	Natural variant	559	1	P → T: dbSNP rs13384912.		VAR_059244
Experimental info
	Sequence conflict	140	1	T → S in AAH68517. Ref.4
	Sequence conflict	298	1	E → Q in AAH11418. Ref.4
	Sequence conflict	353	1	N → S in BAC11505. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: 06AE8EBC16BBA2EC	FASTA	610	66,820
	10 20 30 40 50 60 MWLPLVLLLA VLLLAVLCKV YLGLFSGSSP NPFSEDVKRP PAPLVTDKEA RKKVLKQAFS 70 80 90 100 110 120 ANQVPEKLDV VVIGSGFGGL AAAAILAKAG KRVLVLEQHT KAGGCCHTFG KNGLEFDTGI 130 140 150 160 170 180 HYIGRMEEGS IGRFILDQIT EGQLDWAPLS SPFDIMVLEG PNGRKEYPMY SGEKAYIQGL 190 200 210 220 230 240 KEKFPQEEAI IDKYIKLVKV VSSGAPHAIL LKFLPLPVVQ LLDRCGLLTR FSPFLQASTQ 250 260 270 280 290 300 SLAEVLQQLG ASSELQAVLS YIFPTYGVTP NHSAFSMHAL LVNHYMKGGF YPRGGSSEIA 310 320 330 340 350 360 FHTIPVIQRA GGAVLTKATV QSVLLDSAGK ACGVSVKKGH ELVNIYCPIV VSNAGLFNTY 370 380 390 400 410 420 EHLLPGNARC LPGVKQQLGT VRPGLGMTSV FICLRGTKED LHLPSTNYYV YYDTDMDQAM 430 440 450 460 470 480 ERYVSMPREE AAEHIPLLFF AFPSAKDPTW EDRFPGRSTM IMLIPTAYEW FEEWQAELKG 490 500 510 520 530 540 KRGSDYETFK NSFVEASMSV VLKLFPQLEG KVESVTAGSP LTNQFYLAAP RGACYGADHD 550 560 570 580 590 600 LGRLHPCVMA SLRAQSPIPN LYLTGQDIFT CGLVGALQGA LLCSSAILKR NLYSDLKNLD 610 SRIRAQKKKN
	Isoform 2. Checksum: 6266754EA5A201E4	FASTA	481	52,439
	10 20 30 40 50 60 MWLPLVLLLA VLLLAVLCKV YLGLFSGSSP NPFSEDVKRP PAPLVTDKEA RKKVLKQAFS 70 80 90 100 110 120 ANQVPEKLDV VVIGSGFGGL AAAAILAKAG KRVLVLEQHT KAGGCCHTFG KNGLEFDTGI 130 140 150 160 170 180 HYIGRMEEGS IGRFILDQIT EGQLDWAPLS SPFDIMVLEG PNGRKEYPMY SGEKAYIQGL 190 200 210 220 230 240 KEKFPQEEAI IDKYIKLVKV VSSGAPHAIL LKFLPLPVVQ LLDRCGLLTR FSPFLQASTQ 250 260 270 280 290 300 SLAEVLQQLG ASSELQAVLS YIFPTYGVTP NHSAFSMHAL LVNHYMKGGF YPRGGSSEIA 310 320 330 340 350 360 FHTIPVIQRA GGAVLTKATV QSVLLDSAGK ACGVSVKKGH ELVNIYCPIV VSNAGLFNTY 370 380 390 400 410 420 EHLLPGNARC LPGVKQQLGT VRPGLGMTSV FICLRGTKED LHLPSTNYYV YYDTDMDQAM 430 440 450 460 470 480 ERYVSMPREE AAEHIPLLFF AFPSAKDPTW EDRFPGGECD CRIPTHQPVL SGCSPRCLLR G

References

[1]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]	"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries." Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y. , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T. DNA Res. 12:117-126(2005) [PubMed: 16303743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Thyroid.
[3]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-610 (ISOFORM 2). Tissue: Colon and Testis.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 195-610 (ISOFORM 1). Tissue: Hepatoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY358568 mRNA. Translation: AAQ88931.1. AK075261 mRNA. Translation: BAC11505.1. AC062037 Genomic DNA. Translation: AAY24126.1. AC093162 Genomic DNA. Translation: AAY24096.1. BC068517 mRNA. Translation: AAH68517.1. BC011418 mRNA. Translation: AAH11418.1. Different initiation. AK000303 mRNA. Translation: BAA91069.1. Different initiation.
IPI	IPI00296157. IPI00335161.
RefSeq	NP_060220.3.
UniGene	Hs.440401
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q6NUM9.
Genome annotation databases
Ensembl	ENST00000263854; ENSP00000263854; ENSG00000042445; Homo sapiens. [Genome view] ENST00000295802; ENSP00000295802; ENSG00000042445; Homo sapiens. [Genome view] ENST00000409984; ENSP00000387196; ENSG00000042445; Homo sapiens. [Genome view] ENST00000429806; ENSP00000388202; ENSG00000042445; Homo sapiens. [Genome view] ENST00000449375; ENSP00000412166; ENSG00000042445; Homo sapiens. [Genome view] ENST00000457495; ENSP00000405040; ENSG00000042445; Homo sapiens. [Genome view]
GeneID	54884.
KEGG	hsa:54884.
NMPDR	fig|9606.3.peg.18139.
UCSC	uc002spd.1. human.
Organism-specific databases
CTD	54884.
GeneCards	GC02M085422.
HGNC	HGNC:25991. RETSAT.
HPA	HPA007961.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q6NUM9.
OMA	GIHYIGR.
Enzyme and pathway databases
BRENDA	1.3.99.23. 247.
Gene expression databases
ArrayExpress	Q6NUM9.
Bgee	Q6NUM9.
CleanEx	HS_RETSAT.
Genevestigator	Q6NUM9.
GermOnline	ENSG00000042445. Homo sapiens.
Family and domain databases
InterPro	IPR003953. FAD_bind2_N. [Graphical view]
Pfam	PF00890. FAD_binding_2. 1 hit. [Graphical view]
ProDom	PD139017. Phytn_dehydro. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...
Other Resources
DrugBank	DB00162. Vitamin A.
NextBio	57859.

Entry information

Entry name

RETST_HUMAN

Accession

Primary (citable) accession number: Q6NUM9
Secondary accession number(s): A6NIK3 , Q53R95, Q53SA9, Q6UX05, Q8N2H5, Q96FA4, Q9NXE5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	March 7, 2006
Last modified:	November 3, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.