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Q9Z0K8 (VNN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pantetheinase

EC=3.5.1.92
Alternative name(s):
Pantetheine hydrolase
Vascular non-inflammatory molecule 1
Short name=Vanin-1
Gene names
Name:Vnn1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length512 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.5 Ref.6

Catalytic activity

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

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor Potential.

Tissue specificity

Ubiquitous.

Post-translational modification

N-glycosylated. Ref.1

Sequence similarities

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

Contains 1 CN hydrolase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.1
Chain24 – 488465Pantetheinase
PRO_0000019714
Propeptide489 – 51224Removed in mature form Potential
PRO_0000019715

Regions

Domain27 – 330304CN hydrolase

Amino acid modifications

Lipidation4881GPI-anchor amidated asparagine Potential
Glycosylation1321N-linked (GlcNAc...) Potential
Glycosylation1481N-linked (GlcNAc...) Potential
Glycosylation3161N-linked (GlcNAc...) Potential
Glycosylation3541N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict31M → T in CAA10567. Ref.1
Sequence conflict31M → T in AAH19203. Ref.4
Sequence conflict491S → G in CAA10567. Ref.1
Sequence conflict71 – 722KQ → NE in BAB22347. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Z0K8 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: D55E192765A8282C

FASTA51257,091
        10         20         30         40         50         60 
MGMSWWLACA AAFSALCVLK ASSLDTFLAA VYEHAVILPK DTLLPVSHSE ALALMNQNLD 

        70         80         90        100        110        120 
LLEGAIVSAA KQGAHIIVTP EDGIYGVRFT RDTIYPYLEE IPDPQVNWIP CDNPKRFGST 

       130        140        150        160        170        180 
PVQERLSCLA KNNSIYVVAN MGDKKPCNTS DSHCPPDGRF QYNTDVVFDS QGKLVARYHK 

       190        200        210        220        230        240 
QNIFMGEDQF NVPMEPEFVT FDTPFGKFGV FTCFDILFHD PAVTLVTEFQ VDTILFPTAW 

       250        260        270        280        290        300 
MDVLPHLAAI EFHSAWAMGM GVNFLAANLH NPSRRMTGSG IYAPDSPRVF HYDRKTQEGK 

       310        320        330        340        350        360 
LLFAQLKSHP IHSPVNWTSY ASSVESTPTK TQEFQSIVFF DEFTFVELKG IKGNYTVCQN 

       370        380        390        400        410        420 
DLCCHLSYQM SEKRADEVYA FGAFDGLHTV EGQYYLQICI LLKCKTTNLR TCGSSVDTAF 

       430        440        450        460        470        480 
TRFEMFSLSG TFGTRYVFPE VLLSEVKLAP GEFQVSSDGR LVSLKPTSGP VLTIGLFGRL 

       490        500        510 
YGKDWASNAS SDFIAHSLII MLIVTPIIHY LC 

« Hide

References

« Hide 'large scale' references
[1]"Vanin-1, a novel GPI-linked perivascular molecule involved in thymus homing."
Aurrand-Lions M., Galland F., Bazin H., Zakharyev V.M., Imhof B.A., Naquet P.
Immunity 5:391-405(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-47, GLYCOSYLATION.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Kidney and Placenta.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., 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].
Tissue: Kidney.
[5]"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.
[6]"Pantetheinase activity of membrane-bound Vanin-1: lack of free cysteamine in tissues of Vanin-1 deficient mice."
Pitari G., Malergue F., Martin F., Philippe J.-M., Massucci M.T., Chabret C., Maras B., Dupre S., Naquet P., Galland F.
FEBS Lett. 483:149-154(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ132098 mRNA. Translation: CAA10567.1.
AK002773 mRNA. Translation: BAB22347.1.
AK145984 mRNA. Translation: BAE26806.1.
AK167427 mRNA. Translation: BAE39515.1.
CH466540 Genomic DNA. Translation: EDL04771.1.
BC019203 mRNA. Translation: AAH19203.1.
RefSeqNP_035834.2. NM_011704.3.
UniGeneMm.27154.

3D structure databases

ProteinModelPortalQ9Z0K8.
SMRQ9Z0K8. Positions 26-310.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9Z0K8.

Proteomic databases

PaxDbQ9Z0K8.
PRIDEQ9Z0K8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041416; ENSMUSP00000040599; ENSMUSG00000037440.
GeneID22361.
KEGGmmu:22361.
UCSCuc007eqc.2. mouse.

Organism-specific databases

CTD8876.
MGIMGI:108395. Vnn1.

Phylogenomic databases

eggNOGCOG0388.
GeneTreeENSGT00390000013823.
HOGENOMHOG000007627.
HOVERGENHBG003996.
InParanoidQ3TJI0.
KOK08069.
OMARYYLQIC.
OrthoDBEOG7HF1J0.
TreeFamTF323645.

Gene expression databases

ArrayExpressQ9Z0K8.
BgeeQ9Z0K8.
CleanExMM_VNN1.
GenevestigatorQ9Z0K8.

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

NextBio302669.
PROQ9Z0K8.
SOURCESearch...

Entry information

Entry nameVNN1_MOUSE
AccessionPrimary (citable) accession number: Q9Z0K8
Secondary accession number(s): Q3TJI0, Q8VCT1, Q9DCH8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot