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Q8IW45 (NNRD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent (S)-NAD(P)H-hydrate dehydratase

EC=4.2.1.93
Alternative name(s):
ATP-dependent NAD(P)HX dehydratase
Carbohydrate kinase domain-containing protein
Gene names
Name:CARKD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration By similarity. HAMAP-Rule MF_03157

Catalytic activity

ATP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = ADP + phosphate + NADH. HAMAP-Rule MF_03157

ATP + (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = ADP + phosphate + NADPH.

Cofactor

Magnesium By similarity. HAMAP-Rule MF_03157

Subcellular location

Mitochondrion By similarity HAMAP-Rule MF_03157.

Sequence similarities

Belongs to the NnrD/CARKD family.

Contains 1 YjeF C-terminal domain.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransit peptide
   LigandATP-binding
NAD
NADP
Nucleotide-binding
   Molecular functionLyase
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnicotinamide nucleotide metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent NAD(P)H-hydrate dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IW45-1)

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: Q8IW45-2)

The sequence of this isoform differs from the canonical sequence as follows:
     299-347: SSPLLVAAFG...GAAFSKLFET → GISDLKLTIW...RGGGRLQQAL
Isoform 3 (identifier: Q8IW45-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-221: Missing.
Isoform 4 (identifier: Q8IW45-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-129: MVTRAGAGTA...SPELIVHPVL → MLPDGPGSSLWGNPGLQTS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 347ATP-dependent (S)-NAD(P)H-hydrate dehydratase HAMAP-Rule MF_03157PRO_0000337021

Regions

Domain53 – 344292YjeF C-terminal
Nucleotide binding246 – 2505ATP By similarity
Nucleotide binding265 – 27410ATP By similarity
Region206 – 2127NAD(P)HX By similarity

Sites

Binding site1531NAD(P)HX; via amide nitrogen By similarity
Binding site2751NAD(P)HX By similarity

Amino acid modifications

Modified residue851Phosphotyrosine By similarity
Glycosylation2401N-linked (GlcNAc...) Ref.5
Glycosylation2971N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 221221Missing in isoform 3.
VSP_033829
Alternative sequence1 – 129129MVTRA…VHPVL → MLPDGPGSSLWGNPGLQTS in isoform 4.
VSP_042012
Alternative sequence299 – 34749SSPLL…KLFET → GISDLKLTIWGPEIETGVKT RAQGSCGPRTTTPTSPHLLL SPSPQVQPSPGGRVWRLLSH QAVQPPSLPEARSLHHHLRH DRRGGGRLQQAL in isoform 2.
VSP_033830
Natural variant1401K → E.
Corresponds to variant rs3742191 [ dbSNP | Ensembl ].
VAR_043564
Natural variant1491V → I.
Corresponds to variant rs3742192 [ dbSNP | Ensembl ].
VAR_043565
Natural variant1521P → T.
Corresponds to variant rs1044112 [ dbSNP | Ensembl ].
VAR_043566

Experimental info

Sequence conflict2061N → D in BAA91797. Ref.1
Sequence conflict2531S → P in BAB14863. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 70D42B97D6E8A41B

FASTA34736,576
        10         20         30         40         50         60 
MVTRAGAGTA VAGAVVVALL SAALALYGPP LDAVLERAFS LRKAHSIKDM ENTLQLVRNI 

        70         80         90        100        110        120 
IPPLSSTKHK GQDGRIGVVG GCQEYTGAPY FAAISALKVG ADLSHVFCAS AAAPVIKAYS 

       130        140        150        160        170        180 
PELIVHPVLD SPNAVHEVEK WLPRLHALVV GPGLGRDDAL LRNVQGILEV SKARDIPVVI 

       190        200        210        220        230        240 
DADGLWLVAQ QPALIHGYRK AVLTPNHVEF SRLYDAVLRG PMDSDDSHGS VLRLSQALGN 

       250        260        270        280        290        300 
VTVVQKGERD ILSNGQQVLV CSQEGSSRRC GGQGDLLSGS LGVLVHWALL AGPQKTNGSS 

       310        320        330        340 
PLLVAAFGAC SLTRQCNHQA FQKHGRSTTT SDMIAEVGAA FSKLFET 

« Hide

Isoform 2 [UniParc].

Checksum: 8A32124EA07160CE
Show »

FASTA39041,360
Isoform 3 [UniParc].

Checksum: 031B1043E9E8AEC9
Show »

FASTA12613,188
Isoform 4 [UniParc].

Checksum: 2AED83A9CD769A97
Show »

FASTA23725,200

References

[1]"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. expand/collapse author list , 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] (ISOFORMS 2; 3 AND 4).
Tissue: Testis.
[2]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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. expand/collapse author list , 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 (JUL-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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[5]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-240.
Tissue: Liver.
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK001631 mRNA. Translation: BAA91797.1.
AK024260 mRNA. Translation: BAB14863.1.
AK302117 mRNA. Translation: BAG63496.1.
AL139385 Genomic DNA. Translation: CAI17008.1.
CH471085 Genomic DNA. Translation: EAX09121.1.
CH471085 Genomic DNA. Translation: EAX09125.1.
BC041028 mRNA. Translation: AAH41028.1.
CCDSCCDS55903.1. [Q8IW45-4]
CCDS9513.1. [Q8IW45-2]
RefSeqNP_001229810.1. NM_001242881.1. [Q8IW45-1]
NP_001229811.1. NM_001242882.1.
NP_001229812.1. NM_001242883.1. [Q8IW45-4]
NP_060680.2. NM_018210.3. [Q8IW45-2]
UniGeneHs.408324.

3D structure databases

ProteinModelPortalQ8IW45.
SMRQ8IW45. Positions 56-279.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120857. 1 interaction.
IntActQ8IW45. 1 interaction.
STRING9606.ENSP00000311984.

PTM databases

PhosphoSiteQ8IW45.

Polymorphism databases

DMDM74728128.

Proteomic databases

MaxQBQ8IW45.
PaxDbQ8IW45.
PRIDEQ8IW45.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309957; ENSP00000311984; ENSG00000213995. [Q8IW45-2]
ENST00000424185; ENSP00000413191; ENSG00000213995. [Q8IW45-4]
GeneID55739.
KEGGhsa:55739.
UCSCuc001vrb.3. human. [Q8IW45-1]
uc001vrc.3. human. [Q8IW45-2]
uc010tjk.2. human. [Q8IW45-4]
uc021rmn.1. human. [Q8IW45-3]

Organism-specific databases

CTD55739.
GeneCardsGC13P111267.
H-InvDBHIX0011456.
HIX0011457.
HIX0171873.
HGNCHGNC:25576. CARKD.
HPAHPA010551.
neXtProtNX_Q8IW45.
PharmGKBPA164717652.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0063.
HOGENOMHOG000163126.
HOVERGENHBG103700.
KOK17757.
OMASHQAVQP.
OrthoDBEOG76X60M.
PhylomeDBQ8IW45.
TreeFamTF300116.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000153481-MONOMER.

Gene expression databases

ArrayExpressQ8IW45.
BgeeQ8IW45.
CleanExHS_CARKD.
GenevestigatorQ8IW45.

Family and domain databases

Gene3D3.40.1190.20. 1 hit.
HAMAPMF_01965. NADHX_dehydratase.
InterProIPR029056. Ribokinase-like.
IPR000631. YjeF_C.
[Graphical view]
PfamPF01256. Carb_kinase. 1 hit.
[Graphical view]
SUPFAMSSF53613. SSF53613. 1 hit.
TIGRFAMsTIGR00196. yjeF_cterm. 1 hit.
PROSITEPS51383. YJEF_C_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCARKD. human.
GeneWikiCARKD.
GenomeRNAi55739.
NextBio60690.
PROQ8IW45.

Entry information

Entry nameNNRD_HUMAN
AccessionPrimary (citable) accession number: Q8IW45
Secondary accession number(s): B4DXT4 expand/collapse secondary AC list , Q5T9X3, Q9H7W1, Q9NVF5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM