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O95497 (VNN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pantetheinase

EC=3.5.1.92
Alternative name(s):
Pantetheine hydrolase
Tiff66
Vascular non-inflammatory molecule 1
Short name=Vanin-1
Gene names
Name:VNN1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine. Ref.7 Ref.8

Catalytic activity

(R)-pantetheine + H2O = (R)-pantothenate + 2-aminoethanethiol.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor Potential.

Tissue specificity

Widely expressed with higher expression in spleen, kidney and blood. Overexpressed in lesional psoriatic skin. Ref.11

Induction

By Th17/Th1 type cytokines, but not by Th2-type. Ref.11

Sequence similarities

Belongs to the carbon-nitrogen hydrolase superfamily. BTD/VNN family.

Contains 1 CN hydrolase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHydrolase
   PTMGlycoprotein
GPI-anchor
Lipoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacute inflammatory response

Inferred from sequence or structural similarity PubMed 14966568. Source: BHF-UCL

cellular component movement

Traceable author statement Ref.1. Source: ProtInc

chronic inflammatory response

Inferred from sequence or structural similarity PubMed 14966568. Source: BHF-UCL

inflammatory response

Inferred from sequence or structural similarity PubMed 15282320. Source: BHF-UCL

innate immune response

Inferred from sequence or structural similarity PubMed 14966568. Source: BHF-UCL

negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from sequence or structural similarity PubMed 15282320. Source: BHF-UCL

pantothenate metabolic process

Inferred from direct assay Ref.8. Source: BHF-UCL

positive regulation of T cell differentiation in thymus

Inferred from sequence or structural similarity Ref.8. Source: BHF-UCL

response to oxidative stress

Traceable author statement PubMed 17145956. Source: BHF-UCL

single organismal cell-cell adhesion

Inferred from sequence or structural similarity Ref.8. Source: BHF-UCL

   Cellular_componentanchored component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

integral component of membrane

Traceable author statement PubMed 17145956. Source: BHF-UCL

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGPI anchor binding

Traceable author statement PubMed 17145956. Source: BHF-UCL

pantetheine hydrolase activity

Inferred from direct assay Ref.8. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 491470Pantetheinase
PRO_0000019712
Propeptide492 – 51322Removed in mature form Potential
PRO_0000019713

Regions

Domain25 – 328304CN hydrolase

Sites

Active site791Proton acceptor By similarity
Active site1781Proton donor By similarity
Active site2111Nucleophile By similarity

Amino acid modifications

Lipidation4911GPI-anchor amidated glycine Potential
Glycosylation381N-linked (GlcNAc...) Ref.9
Glycosylation1301N-linked (GlcNAc...) Ref.10
Glycosylation2001N-linked (GlcNAc...) Potential
Glycosylation2831N-linked (GlcNAc...) Ref.10
Glycosylation3151N-linked (GlcNAc...) Ref.10
Glycosylation3531N-linked (GlcNAc...) Ref.9 Ref.10 Ref.12

Natural variations

Natural variant261T → I. Ref.1 Ref.2 Ref.3 Ref.4
Corresponds to variant rs2294757 [ dbSNP | Ensembl ].
VAR_023529
Natural variant631A → T. Ref.4
VAR_023967
Natural variant1311N → S. Ref.4 Ref.6
Corresponds to variant rs2272996 [ dbSNP | Ensembl ].
VAR_023968
Natural variant1361V → L. Ref.4
Corresponds to variant rs45610032 [ dbSNP | Ensembl ].
VAR_023969
Natural variant1461D → N. Ref.4
Corresponds to variant rs45624336 [ dbSNP | Ensembl ].
VAR_023970
Natural variant2961E → D. Ref.4
Corresponds to variant rs45523444 [ dbSNP | Ensembl ].
VAR_023971
Natural variant3251A → E. Ref.4
Corresponds to variant rs34535050 [ dbSNP | Ensembl ].
VAR_023972
Natural variant3361T → A. Ref.4
Corresponds to variant rs45562238 [ dbSNP | Ensembl ].
VAR_023973
Natural variant3731I → T. Ref.4
Corresponds to variant rs35938565 [ dbSNP | Ensembl ].
VAR_023974

Experimental info

Sequence conflict1011D → N in AAH96268. Ref.6
Sequence conflict1131N → I in AAY88742. Ref.4
Sequence conflict4231E → D in AAF21453. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O95497 [UniParc].

Last modified September 27, 2005. Version 2.
Checksum: 018D2417C12E403F

FASTA51357,012
        10         20         30         40         50         60 
MTTQLPAYVA ILLFYVSRAS CQDTFTAAVY EHAAILPNAT LTPVSREEAL ALMNRNLDIL 

        70         80         90        100        110        120 
EGAITSAADQ GAHIIVTPED AIYGWNFNRD SLYPYLEDIP DPEVNWIPCN NRNRFGQTPV 

       130        140        150        160        170        180 
QERLSCLAKN NSIYVVANIG DKKPCDTSDP QCPPDGRYQY NTDVVFDSQG KLVARYHKQN 

       190        200        210        220        230        240 
LFMGENQFNV PKEPEIVTFN TTFGSFGIFT CFDILFHDPA VTLVKDFHVD TIVFPTAWMN 

       250        260        270        280        290        300 
VLPHLSAVEF HSAWAMGMRV NFLASNIHYP SKKMTGSGIY APNSSRAFHY DMKTEEGKLL 

       310        320        330        340        350        360 
LSQLDSHPSH SAVVNWTSYA SSIEALSSGN KEFKGTVFFD EFTFVKLTGV AGNYTVCQKD 

       370        380        390        400        410        420 
LCCHLSYKMS ENIPNEVYAL GAFDGLHTVE GRYYLQICTL LKCKTTNLNT CGDSAETAST 

       430        440        450        460        470        480 
RFEMFSLSGT FGTQYVFPEV LLSENQLAPG EFQVSTDGRL FSLKPTSGPV LTVTLFGRLY 

       490        500        510 
EKDWASNASS GLTAQARIIM LIVIAPIVCS LSW 

« Hide

References

« Hide 'large scale' references
[1]"Two human genes related to murine vanin-1 are located on the long arm of human chromosome 6."
Galland F., Malergue F., Bazin H., Mattei M.-G., Aurrand-Lions M., Theillet C., Naquet P.
Genomics 53:203-213(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-26.
Tissue: Liver.
[2]"Human Tiff66."
Prehn S., Friedrichson T., Henske A., Boehm S., Hartmann E., Kurzchalia T.V.
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ILE-26.
[3]"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], VARIANT ILE-26.
Tissue: Umbilical cord blood.
[4]NIEHS SNPs program
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-26; THR-63; SER-131; LEU-136; ASN-146; ASP-296; GLU-325; ALA-336 AND THR-373.
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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], VARIANT SER-131.
[7]"Is pantetheinase the actual identity of mouse and human vanin-1 proteins?"
Maras B., Barra D., Dupre S., Pitari G.
FEBS Lett. 461:149-152(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode isoforms of pantetheinase ectoenzymes."
Martin F., Malergue F., Pitari G., Philippe J.M., Philips S., Chabret C., Granjeaud S., Mattei M.G., Mungall A.J., Naquet P., Galland F.
Immunogenetics 53:296-306(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"A proteomic analysis of human bile."
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.
Mol. Cell. Proteomics 3:715-728(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-38 AND ASN-353.
Tissue: Bile.
[10]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130; ASN-283; ASN-315 AND ASN-353.
Tissue: Plasma.
[11]"Expression of the vanin gene family in normal and inflamed human skin: induction by proinflammatory cytokines."
Jansen P.A.M., Kamsteeg M., Rodijk-Olthuis D., van Vlijmen-Willems I.M.J.J., de Jongh G.J., Bergers M., Tjabringa G.S., Zeeuwen P.L.J.M., Schalkwijk J.
J. Invest. Dermatol. 129:2167-2174(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION BY CYTOKINES.
[12]"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-353.
Tissue: Liver.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ132099 mRNA. Translation: CAA10568.1.
U39664 mRNA. Translation: AAF21453.1.
AK290425 mRNA. Translation: BAF83114.1.
DQ100297 Genomic DNA. Translation: AAY88742.1.
AL032821 Genomic DNA. Translation: CAB40075.1.
BC096265 mRNA. Translation: AAH96265.1.
BC096266 mRNA. Translation: AAH96266.1.
BC096267 mRNA. Translation: AAH96267.1.
BC096268 mRNA. Translation: AAH96268.1.
CCDSCCDS5159.1.
RefSeqNP_004657.2. NM_004666.2.
UniGeneHs.12114.
Hs.720659.

3D structure databases

ProteinModelPortalO95497.
SMRO95497. Positions 54-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000356905.

PTM databases

PhosphoSiteO95497.

Proteomic databases

PaxDbO95497.
PeptideAtlasO95497.
PRIDEO95497.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367928; ENSP00000356905; ENSG00000112299.
GeneID8876.
KEGGhsa:8876.
UCSCuc003qdo.3. human.

Organism-specific databases

CTD8876.
GeneCardsGC06M133001.
H-InvDBHIX0022602.
HGNCHGNC:12705. VNN1.
MIM603570. gene.
neXtProtNX_O95497.
PharmGKBPA37321.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0388.
HOVERGENHBG003996.
InParanoidO95497.
KOK08069.
OMARYYLQIC.
OrthoDBEOG7HF1J0.
PhylomeDBO95497.
TreeFamTF323645.

Gene expression databases

BgeeO95497.
CleanExHS_VNN1.
GenevestigatorO95497.

Family and domain databases

Gene3D3.60.110.10. 1 hit.
InterProIPR012101. Biotinidase_euk.
IPR003010. C-N_Hydrolase.
[Graphical view]
PANTHERPTHR10609. PTHR10609. 1 hit.
PfamPF00795. CN_hydrolase. 1 hit.
[Graphical view]
PIRSFPIRSF011861. Biotinidase. 1 hit.
SUPFAMSSF56317. SSF56317. 1 hit.
PROSITEPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiVNN1.
GenomeRNAi8876.
NextBio33325.
PROO95497.
SOURCESearch...

Entry information

Entry nameVNN1_HUMAN
AccessionPrimary (citable) accession number: O95497
Secondary accession number(s): A8K310 expand/collapse secondary AC list , Q4JFW6, Q4VAS7, Q4VAS8, Q4VAS9, Q9UF16, Q9UJF4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: September 27, 2005
Last modified: July 9, 2014
This is version 124 of the entry and version 2 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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 6

Human chromosome 6: entries, gene names and cross-references to MIM