Q13630 (FCL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
GDP-L-fucose synthase
EC=1.1.1.271

Alternative name(s):
GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase
Protein FX
Red cell NADP(H)-binding protein
Short-chain dehydrogenase/reductase family 4E member 1

Gene names

Name:	TSTA3
Synonyms:	SDR4E1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Two step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction. Ref.1
Catalytic activity	GDP-L-fucose + NADP+ = GDP-4-dehydro-6-deoxy-D-mannose + NADPH.
Pathway	Nucleotide-sugar biosynthesis; GDP-L-fucose biosynthesis via de novo pathway; GDP-L-fucose from GDP-alpha-D-mannose: step 2/2.
Subunit structure	Homodimer. Ref.1
Sequence similarities	Belongs to the fucose synthase family.

Ontologies

Keywords
Ligand	NADP
Molecular function	Isomerase Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	'de novo' GDP-L-fucose biosynthetic process Inferred from direct assay. Source: UniProtKB GDP-mannose metabolic process Inferred from direct assay. Source: UniProtKB leukocyte cell-cell adhesion Non-traceable author statement. Source: UniProtKB
Cellular component	cytoplasm Inferred by curator. Source: UniProtKB
Molecular function	GDP-4-dehydro-D-rhamnose reductase activity Traceable author statement. Source: UniProtKB GDP-L-fucose synthase activity Inferred from direct assay. Source: UniProtKB coenzyme binding Inferred from electronic annotation. Source: InterPro electron carrier activity Traceable author statement Ref.1. Source: UniProtKB isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW nucleotide 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 – 321	321	GDP-L-fucose synthase		PRO_0000174350
Regions
	Nucleotide binding	9 – 39	31	NADP Potential
Amino acid modifications
	Modified residue	147	1	N6-acetyllysine Ref.6
Experimental info
	Sequence conflict	5	1	Q → E AA sequence Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q13630 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 94BB1FF61658007C	FASTA	321	35,893
	10 20 30 40 50 60 MGEPQGSMRI LVTGGSGLVG KAIQKVVADG AGLPGEDWVF VSSKDADLTD TAQTRALFEK 70 80 90 100 110 120 VQPTHVIHLA AMVGGLFRNI KYNLDFWRKN VHMNDNVLHS AFEVGARKVV SCLSTCIFPD 130 140 150 160 170 180 KTTYPIDETM IHNGPPHNSN FGYSYAKRMI DVQNRAYFQQ YGCTFTAVIP TNVFGPHDNF 190 200 210 220 230 240 NIEDGHVLPG LIHKVHLAKS SGSALTVWGT GNPRRQFIYS LDLAQLFIWV LREYNEVEPI 250 260 270 280 290 300 ILSVGEEDEV SIKEAAEAVV EAMDFHGEVT FDTTKSDGQF KKTASNSKLR TYLPDFRFTP 310 320 FKQAVKETCA WFTDNYEQAR K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Synthesis of GDP-L-fucose by the human FX protein." Tonetti M., Sturla L., Bisso A., Benatti U., De Flora A. J. Biol. Chem. 271:27274-27279(1996) [PubMed: 8910301] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT. Tissue: Placenta.
[2]	"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]. Tissue: Placenta.
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]. Tissue: Lung and Skin.
[5]	"Primary structure of human erythrocyte nicotinamide adenine dinucleotide phosphate (NADP[H])-binding protein FX: identification with the mouse tum-transplantation antigen P35B." Camardella L., Carratore V., Ciardiello A., Damonte G., Benatti U., De Flora A. Blood 85:264-267(1995) [PubMed: 7803801] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE. Tissue: Erythrocyte.
[6]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147, MASS SPECTROMETRY.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases
EMBL GenBank DDBJ	U58766 mRNA. Translation: AAC50786.1. AK313560 mRNA. Translation: BAG36334.1. CH471162 Genomic DNA. Translation: EAW82218.1. CH471162 Genomic DNA. Translation: EAW82220.1. CH471162 Genomic DNA. Translation: EAW82222.1. BC001941 mRNA. Translation: AAH01941.1. BC093061 mRNA. Translation: AAH93061.1.
IPI	IPI00014361.
RefSeq	NP_003304.1. NM_003313.3.
UniGene	Hs.404119.
3D structure databases
ProteinModelPortal	Q13630.
SMR	Q13630. Positions 8-319.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13630. 2 interactions.
STRING	Q13630.
PTM databases
PhosphoSite	Q13630.
Polymorphism databases
DMDM	13124123.
2D gel databases
REPRODUCTION-2DPAGE	IPI00014361.
Proteomic databases
PeptideAtlas	Q13630.
PRIDE	Q13630.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000360125; ENSP00000353243; ENSG00000104522. ENST00000425753; ENSP00000398803; ENSG00000104522.
GeneID	7264.
KEGG	hsa:7264.
UCSC	uc003yyz.1. human.
Organism-specific databases
CTD	7264.
GeneCards	GC08M144694.
H-InvDB	HIX0007843.
HGNC	HGNC:12390. TSTA3.
HPA	HPA023361.
MIM	137020. gene.
neXtProt	NX_Q13630.
PharmGKB	PA37056.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG09094.
GeneTree	ENSGT00390000004681.
HOGENOM	HBG381459.
HOVERGEN	HBG000059.
InParanoid	Q13630.
OMA	KTASNEK.
OrthoDB	EOG4VT5XR.
PhylomeDB	Q13630.
Gene expression databases
ArrayExpress	Q13630.
Bgee	Q13630.
CleanEx	HS_TSTA3.
Genevestigator	Q13630.
GermOnline	ENSG00000104522. Homo sapiens.
Family and domain databases
InterPro	IPR001509. Epimerase_deHydtase. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K02377.
Pfam	PF01370. Epimerase. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00157. NADH.
NextBio	28399.
SOURCE	Search...

Entry information

Entry name

FCL_HUMAN

Accession

Primary (citable) accession number: Q13630
Secondary accession number(s): B2R8Y7 , D3DWK5, Q567Q9, Q9UDG7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.