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Q13630

- FCL_HUMAN

UniProt

Q13630 - FCL_HUMAN

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Protein
GDP-L-fucose synthase
Gene
TSTA3, SDR4E1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.1 Publication

Catalytic activityi

GDP-beta-L-fucose + NADP+ = GDP-4-dehydro-6-deoxy-alpha-D-mannose + NADPH.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei114 – 1141Important for catalytic activity By similarity
Sitei116 – 1161Important for catalytic activity By similarity
Active sitei143 – 1431Proton donor/acceptor By similarity
Binding sitei147 – 1471NADP
Sitei147 – 1471Lowers pKa of active site Tyr By similarity
Binding sitei186 – 1861NADP
Binding sitei194 – 1941Substrate
Binding sitei208 – 2081Substrate
Binding sitei215 – 2151Substrate
Binding sitei277 – 2771Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 207NADPUniRule annotation
Nucleotide bindingi170 – 1734NADPUniRule annotation

GO - Molecular functioni

  1. GDP-4-dehydro-D-rhamnose reductase activity Source: UniProtKB
  2. GDP-L-fucose synthase activity Source: UniProtKB
  3. coenzyme binding Source: InterPro
  4. electron carrier activity Source: UniProtKB
  5. isomerase activity Source: UniProtKB-KW

GO - Biological processi

  1. 'de novo' GDP-L-fucose biosynthetic process Source: UniProtKB
  2. GDP-mannose metabolic process Source: UniProtKB
  3. cytolysis Source: Ensembl
  4. leukocyte cell-cell adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Oxidoreductase

Keywords - Ligandi

NADP

Enzyme and pathway databases

UniPathwayiUPA00128; UER00191.

Names & Taxonomyi

Protein namesi
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 namesi
Name:TSTA3
Synonyms:SDR4E1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:12390. TSTA3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37056.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 321321GDP-L-fucose synthaseUniRule annotation
PRO_0000174350Add
BLAST

Proteomic databases

MaxQBiQ13630.
PaxDbiQ13630.
PeptideAtlasiQ13630.
PRIDEiQ13630.

2D gel databases

REPRODUCTION-2DPAGEIPI00014361.

PTM databases

PhosphoSiteiQ13630.

Expressioni

Gene expression databases

ArrayExpressiQ13630.
BgeeiQ13630.
CleanExiHS_TSTA3.
GenevestigatoriQ13630.

Organism-specific databases

HPAiHPA023361.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi113115. 14 interactions.
IntActiQ13630. 2 interactions.
STRINGi9606.ENSP00000353243.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 135
Turni14 – 163
Helixi18 – 236
Turni27 – 293
Beta strandi37 – 404
Beta strandi43 – 464
Helixi51 – 6010
Beta strandi64 – 685
Turni74 – 774
Beta strandi78 – 803
Helixi83 – 10321
Beta strandi107 – 1126
Helixi115 – 1173
Beta strandi118 – 1214
Beta strandi124 – 1263
Helixi128 – 1303
Beta strandi138 – 1403
Helixi141 – 16121
Beta strandi164 – 1707
Beta strandi172 – 1754
Turni182 – 1843
Helixi187 – 19913
Beta strandi201 – 2033
Beta strandi207 – 2093
Beta strandi217 – 2193
Helixi220 – 23213
Beta strandi240 – 2423
Helixi246 – 2483
Helixi252 – 26312
Beta strandi269 – 2724
Helixi287 – 2926
Helixi301 – 31414
Turni315 – 3184

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4B8WX-ray2.75A/B7-320[»]
4B8ZX-ray2.75A/B/C/D8-320[»]
4BKPX-ray2.70A/B/C/D8-321[»]
4BL5X-ray2.60A/B/C/D/E/F/G/H/I/J/K/L8-321[»]
4E5YX-ray2.37A/B/C/D1-321[»]
ProteinModelPortaliQ13630.
SMRiQ13630. Positions 4-321.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0451.
HOGENOMiHOG000168011.
HOVERGENiHBG000059.
InParanoidiQ13630.
KOiK02377.
OMAiIRETCEW.
PhylomeDBiQ13630.
TreeFamiTF314936.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00956. GDP_fucose_synth.
InterProiIPR001509. Epimerase_deHydtase.
IPR028614. GDP_fucose_synth.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q13630-1 [UniParc]FASTAAdd to Basket

« Hide

MGEPQGSMRI LVTGGSGLVG KAIQKVVADG AGLPGEDWVF VSSKDADLTD    50
TAQTRALFEK VQPTHVIHLA AMVGGLFRNI KYNLDFWRKN VHMNDNVLHS 100
AFEVGARKVV SCLSTCIFPD KTTYPIDETM IHNGPPHNSN FGYSYAKRMI 150
DVQNRAYFQQ YGCTFTAVIP TNVFGPHDNF NIEDGHVLPG LIHKVHLAKS 200
SGSALTVWGT GNPRRQFIYS LDLAQLFIWV LREYNEVEPI ILSVGEEDEV 250
SIKEAAEAVV EAMDFHGEVT FDTTKSDGQF KKTASNSKLR TYLPDFRFTP 300
FKQAVKETCA WFTDNYEQAR K 321
Length:321
Mass (Da):35,893
Last modified:November 1, 1996 - v1
Checksum:i94BB1FF61658007C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51Q → E AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS6408.1.
RefSeqiNP_003304.1. NM_003313.3.
UniGeneiHs.404119.

Genome annotation databases

EnsembliENST00000425753; ENSP00000398803; ENSG00000104522.
ENST00000529064; ENSP00000435386; ENSG00000104522.
GeneIDi7264.
KEGGihsa:7264.
UCSCiuc003yza.2. human.

Polymorphism databases

DMDMi13124123.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS6408.1.
RefSeqi NP_003304.1. NM_003313.3.
UniGenei Hs.404119.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4B8W X-ray 2.75 A/B 7-320 [» ]
4B8Z X-ray 2.75 A/B/C/D 8-320 [» ]
4BKP X-ray 2.70 A/B/C/D 8-321 [» ]
4BL5 X-ray 2.60 A/B/C/D/E/F/G/H/I/J/K/L 8-321 [» ]
4E5Y X-ray 2.37 A/B/C/D 1-321 [» ]
ProteinModelPortali Q13630.
SMRi Q13630. Positions 4-321.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113115. 14 interactions.
IntActi Q13630. 2 interactions.
STRINGi 9606.ENSP00000353243.

Chemistry

DrugBanki DB00157. NADH.

PTM databases

PhosphoSitei Q13630.

Polymorphism databases

DMDMi 13124123.

2D gel databases

REPRODUCTION-2DPAGE IPI00014361.

Proteomic databases

MaxQBi Q13630.
PaxDbi Q13630.
PeptideAtlasi Q13630.
PRIDEi Q13630.

Protocols and materials databases

DNASUi 7264.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000425753 ; ENSP00000398803 ; ENSG00000104522 .
ENST00000529064 ; ENSP00000435386 ; ENSG00000104522 .
GeneIDi 7264.
KEGGi hsa:7264.
UCSCi uc003yza.2. human.

Organism-specific databases

CTDi 7264.
GeneCardsi GC08M144694.
HGNCi HGNC:12390. TSTA3.
HPAi HPA023361.
MIMi 137020. gene.
neXtProti NX_Q13630.
PharmGKBi PA37056.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0451.
HOGENOMi HOG000168011.
HOVERGENi HBG000059.
InParanoidi Q13630.
KOi K02377.
OMAi IRETCEW.
PhylomeDBi Q13630.
TreeFami TF314936.

Enzyme and pathway databases

UniPathwayi UPA00128 ; UER00191 .

Miscellaneous databases

GeneWikii TSTA3.
GenomeRNAii 7264.
NextBioi 28399.
PROi Q13630.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13630.
Bgeei Q13630.
CleanExi HS_TSTA3.
Genevestigatori Q13630.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
HAMAPi MF_00956. GDP_fucose_synth.
InterProi IPR001509. Epimerase_deHydtase.
IPR028614. GDP_fucose_synth.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF01370. Epimerase. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  3. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Erythrocyte.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "The crystal structure of human GDP-L-fucose synthase."
    Zhou H., Sun L., Li J., Xu C., Yu F., Liu Y., Ji C., He J.
    Acta Biochim. Biophys. Sin. 45:720-725(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.
  8. "Crystal structure of human GDP-L-fucose synthase with bound NADP."
    Structural genomics consortium (SGC)
    Submitted (APR-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 8-321 IN COMPLEXES WITH GDP AND NADP.

Entry informationi

Entry nameiFCL_HUMAN
AccessioniPrimary (citable) accession number: Q13630
Secondary accession number(s): B2R8Y7
, D3DWK5, Q567Q9, Q9UDG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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