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Reviewed, UniProtKB/Swiss-Prot O95498 (VNN2_HUMAN)

Last modified November 25, 2008. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Vascular non-inflammatory molecule 2
      Short name=Vanin-2
Alternative name(s):
    Glycosylphosphatidyl inositol-anchored protein GPI-80
    Protein FOAP-4
Gene names
Name: VNN2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Probable hydrolase. Involved in the thymus homing of bone marrow cells. May regulate beta-2 integrin-mediated cell adhesion, migration and motility of neutrophil.

Subcellular location

Cell membrane; Lipid-anchor › GPI-anchorPotential.

Tissue specificity

Expressed in spleen, thymus, peripheral blood lymphocytes and kidney.

Sequence similarities

Belongs to the CN hydrolase family. BTD/VNN subfamily.

Contains 1 CN hydrolase domain.

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Ontologies

Keywords

   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHydrolase
   PTMGPI-anchor
Glycoprotein
Lipoprotein

Gene Ontology (GO)

   Biological processcell motion Ref.1

Traceable author statement. Source: ProtInc

nitrogen compound metabolic process

Inferred from electronic annotation. Source: InterPro

pantothenate metabolic process

Inferred from direct assay. Source: UniProtKB

   Cellular componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionpantetheine hydrolase activity

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 493471Vascular non-inflammatory molecule 2
PRO_0000019718
Propeptide494 – 52027Removed in mature form Potential
PRO_0000019719

Regions

Domain26 – 328303CN hydrolase
Compositional bias393 – 3964Poly-Arg

Amino acid modifications

Lipidation4931GPI-anchor amidated cysteine Potential
Glycosylation391N-linked (GlcNAc...) Potential
Glycosylation2731N-linked (GlcNAc...) Potential
Glycosylation3471N-linked (GlcNAc...) Potential
Glycosylation3571N-linked (GlcNAc...) Potential
Glycosylation4111N-linked (GlcNAc...)
Glycosylation4681N-linked (GlcNAc...) Potential

Natural variations

Natural variant171T → N
VAR_025177
Natural variant301V → A: dbSNP rs2294760.
VAR_031261
Natural variant1121D → E
VAR_025178
Natural variant2411V → I: dbSNP rs33920182.
VAR_025179
Natural variant3491T → S
VAR_025180
Natural variant4041L → M: dbSNP rs4895944.
VAR_023530

Experimental info

Sequence conflict2181D → Y in CAA10569. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
O95498-1 [UniParc].

Last modified March 20, 2007. Version 3.
Checksum: 14460E1DE5B04870

FASTA52058,503
        10         20         30         40         50         60 
MVTSSFPISV AVFALITLQV GTQDSFIAAV YEHAVILPNK TETPVSQEDA LNLMNENIDI 

        70         80         90        100        110        120 
LETAIKQAAE QGARIIVTPE DALYGWKFTR ETVFPYLEDI PDPQVNWIPC QDPHRFGHTP 

       130        140        150        160        170        180 
VQARLSCLAK DNSIYVLANL GDKKPCNSRD STCPPNGYFQ YNTNVVYNTE GKLVARYHKY 

       190        200        210        220        230        240 
HLYSEPQFNV PEKPELVTFN TAFGRFGIFT CFDIFFYDPG VTLVKDFHVD TILFPTAWMN 

       250        260        270        280        290        300 
VLPLLTAIEF HSAWAMGMGV NLLVANTHHV SLNMTGSGIY APNGPKVYHY DMKTELGKLL 

       310        320        330        340        350        360 
LSEVDSHPLS SLAYPTAVNW NAYATTIKPF PVQKNTFRGF ISRDGFNFTE LFENAGNLTV 

       370        380        390        400        410        420 
CQKELCCHLS YRMLQKEENE VYVLGAFTGL HGRRRREYWQ VCTLLKCKTT NLTTCGRPVE 

       430        440        450        460        470        480 
TASTRFEMFS LSGTFGTEYV FPEVLLTEIH LSPGKFEVLK DGRLVNKNGS SGPILTVSLF 

       490        500        510        520 
GRWYTKDSLY SSCGTSNSAI TYLLIFILLM IIALQNIVML

« Hide

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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: 9790769] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-404.
Tissue: Kidney.
[2]"A novel glycosylphosphatidyl inositol-anchored protein on human leukocytes: a possible role for regulation of neutrophil adherence and migration."
Suzuki K., Watanabe T., Sakurai S., Ohtake K., Kinoshita T., Araki A., Fujita T., Takei H., Takeda Y., Sato Y., Yamashita T., Araki Y., Sendo F.
J. Immunol. 162:4277-4284(1999) [PubMed: 10201959] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-404.
Tissue: Peripheral blood.
[3]"Homo sapiens mRNA for FOAP-4 protein, complete cds."
Takayama K., Fujii Y., Tsuritani K., Yajima Y., Amemiya T., Ukai Y., Naito K., Kawaguchi A.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT MET-404.
Tissue: Blood.
[4]"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."
Livingston R.J., Rieder M.J., Shaffer T., Bertucci C., Baier C.N., Rajkumar N., Willa H.T., Daniels M., Downing T.K., Stanaway I.B., Nguyen C.P., Gildersleeve H., Cassidy C.M., Johnson E.J., Swanson J.E., McFarland I., Yool B., Park C., Nickerson D.A.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASN-17; GLU-112; ILE-241; SER-349 AND MET-404.
[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: 14574404] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-404.
[7]"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: 16335952] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411, MASS SPECTROMETRY.
Tissue: Plasma.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AJ132100 mRNA. Translation: CAA10569.1.
D89974 mRNA. Translation: BAA82525.1.
AB026705 mRNA. Translation: BAB61019.1.
DQ249347 Genomic DNA. Translation: ABB72673.1.
AL032821 Genomic DNA. Translation: CAB40076.1.
BC126145 mRNA. Translation: AAI26146.1.
BC126147 mRNA. Translation: AAI26148.1.
RefSeqNP_004656.2.
NP_511043.1.
UniGeneHs.293130

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteO95498.

Polymorphism databases

NIEHS-SNPsSearch...

Genome annotation databases

EnsemblENSG00000112303. Homo sapiens. [Contig view]
GeneID8875.
KEGGhsa:8875.

Organism-specific databases

H-InvDBHIX0032748.
HGNCHGNC:12706. VNN2.
MIM603571. gene.
PharmGKBPA37322.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMO95498.
HOVERGENO95498.

Gene expression databases

ArrayExpressO95498.
CleanExHS_VNN2.
GermOnlineENSG00000112303. Homo sapiens.

Family and domain databases

InterProIPR012101. Biotinidase_euk.
IPR003010. Ntlse/CNhydtse.
[Graphical view]
Gene3DG3DSA:3.60.110.10. Ntlse/CNhydtse. 1 hit.
PANTHERPTHR10609. Biotinidase_euk. 1 hit.
PfamPF00795. CN_hydrolase. 1 hit.
[Graphical view]
PIRSFPIRSF011861. Biotinidase. 1 hit.
PROSITEPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio33319.
SOURCESearch...

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Entry information

Entry nameVNN2_HUMAN
AccessionPrimary (citable) accession number: O95498
Secondary accession number(s): A0AUZ3 expand/collapse secondary AC list , A6NDY1, Q2XUN1, Q9UJF3, Q9UMW2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 20, 2007
Last modified: November 25, 2008
This is version 72 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 6

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents