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Q9Z0K8

- VNN1_MOUSE

UniProt

Q9Z0K8 - VNN1_MOUSE

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Protein
Pantetheinase
Gene
Vnn1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine.2 Publications

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei81 – 811Proton acceptor By similarity
Active sitei180 – 1801Proton donor By similarity
Active sitei213 – 2131Nucleophile By similarity

GO - Molecular functioni

  1. GPI anchor binding Source: BHF-UCL
  2. pantetheine hydrolase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

  1. acute inflammatory response Source: BHF-UCL
  2. chronic inflammatory response Source: BHF-UCL
  3. inflammatory response Source: BHF-UCL
  4. innate immune response Source: BHF-UCL
  5. negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress Source: BHF-UCL
  6. pantothenate metabolic process Source: Ensembl
  7. positive regulation of T cell differentiation in thymus Source: BHF-UCL
  8. single organismal cell-cell adhesion Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Pantetheinase (EC:3.5.1.92)
Alternative name(s):
Pantetheine hydrolase
Vascular non-inflammatory molecule 1
Short name:
Vanin-1
Gene namesi
Name:Vnn1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:108395. Vnn1.

Subcellular locationi

Cell membrane; Lipid-anchorGPI-anchor Reviewed prediction

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. integral component of membrane Source: BHF-UCL
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 Publication
Add
BLAST
Chaini24 – 488465Pantetheinase
PRO_0000019714Add
BLAST
Propeptidei489 – 51224Removed in mature form Reviewed prediction
PRO_0000019715Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi132 – 1321N-linked (GlcNAc...) Reviewed prediction
Glycosylationi148 – 1481N-linked (GlcNAc...) Reviewed prediction
Glycosylationi316 – 3161N-linked (GlcNAc...) Reviewed prediction
Glycosylationi354 – 3541N-linked (GlcNAc...) Reviewed prediction
Lipidationi488 – 4881GPI-anchor amidated asparagine Reviewed prediction

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

MaxQBiQ9Z0K8.
PaxDbiQ9Z0K8.
PRIDEiQ9Z0K8.

PTM databases

PhosphoSiteiQ9Z0K8.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiQ9Z0K8.
BgeeiQ9Z0K8.
CleanExiMM_VNN1.
GenevestigatoriQ9Z0K8.

Structurei

3D structure databases

ProteinModelPortaliQ9Z0K8.
SMRiQ9Z0K8. Positions 56-243.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 330304CN hydrolase
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0388.
GeneTreeiENSGT00390000013823.
HOGENOMiHOG000007627.
HOVERGENiHBG003996.
InParanoidiQ3TJI0.
KOiK08069.
OMAiRYYLQIC.
OrthoDBiEOG7HF1J0.
TreeFamiTF323645.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
InterProiIPR012101. Biotinidase_euk.
IPR003010. C-N_Hydrolase.
[Graphical view]
PANTHERiPTHR10609. PTHR10609. 1 hit.
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
PIRSFiPIRSF011861. Biotinidase. 1 hit.
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Z0K8-1 [UniParc]FASTAAdd to Basket

« Hide

MGMSWWLACA AAFSALCVLK ASSLDTFLAA VYEHAVILPK DTLLPVSHSE    50
ALALMNQNLD LLEGAIVSAA KQGAHIIVTP EDGIYGVRFT RDTIYPYLEE 100
IPDPQVNWIP CDNPKRFGST PVQERLSCLA KNNSIYVVAN MGDKKPCNTS 150
DSHCPPDGRF QYNTDVVFDS QGKLVARYHK QNIFMGEDQF NVPMEPEFVT 200
FDTPFGKFGV FTCFDILFHD PAVTLVTEFQ VDTILFPTAW MDVLPHLAAI 250
EFHSAWAMGM GVNFLAANLH NPSRRMTGSG IYAPDSPRVF HYDRKTQEGK 300
LLFAQLKSHP IHSPVNWTSY ASSVESTPTK TQEFQSIVFF DEFTFVELKG 350
IKGNYTVCQN DLCCHLSYQM SEKRADEVYA FGAFDGLHTV EGQYYLQICI 400
LLKCKTTNLR TCGSSVDTAF TRFEMFSLSG TFGTRYVFPE VLLSEVKLAP 450
GEFQVSSDGR LVSLKPTSGP VLTIGLFGRL YGKDWASNAS SDFIAHSLII 500
MLIVTPIIHY LC 512
Length:512
Mass (Da):57,091
Last modified:July 27, 2011 - v3
Checksum:iD55E192765A8282C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31M → T in CAA10567. 1 Publication
Sequence conflicti3 – 31M → T in AAH19203. 1 Publication
Sequence conflicti49 – 491S → G in CAA10567. 1 Publication
Sequence conflicti71 – 722KQ → NE in BAB22347. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS35868.1.
RefSeqiNP_035834.2. NM_011704.3.
UniGeneiMm.27154.

Genome annotation databases

EnsembliENSMUST00000041416; ENSMUSP00000040599; ENSMUSG00000037440.
GeneIDi22361.
KEGGimmu:22361.
UCSCiuc007eqc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS35868.1.
RefSeqi NP_035834.2. NM_011704.3.
UniGenei Mm.27154.

3D structure databases

ProteinModelPortali Q9Z0K8.
SMRi Q9Z0K8. Positions 56-243.
ModBasei Search...

PTM databases

PhosphoSitei Q9Z0K8.

Proteomic databases

MaxQBi Q9Z0K8.
PaxDbi Q9Z0K8.
PRIDEi Q9Z0K8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000041416 ; ENSMUSP00000040599 ; ENSMUSG00000037440 .
GeneIDi 22361.
KEGGi mmu:22361.
UCSCi uc007eqc.2. mouse.

Organism-specific databases

CTDi 8876.
MGIi MGI:108395. Vnn1.

Phylogenomic databases

eggNOGi COG0388.
GeneTreei ENSGT00390000013823.
HOGENOMi HOG000007627.
HOVERGENi HBG003996.
InParanoidi Q3TJI0.
KOi K08069.
OMAi RYYLQIC.
OrthoDBi EOG7HF1J0.
TreeFami TF323645.

Miscellaneous databases

NextBioi 302669.
PROi Q9Z0K8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Z0K8.
Bgeei Q9Z0K8.
CleanExi MM_VNN1.
Genevestigatori Q9Z0K8.

Family and domain databases

Gene3Di 3.60.110.10. 1 hit.
InterProi IPR012101. Biotinidase_euk.
IPR003010. C-N_Hydrolase.
[Graphical view ]
PANTHERi PTHR10609. PTHR10609. 1 hit.
Pfami PF00795. CN_hydrolase. 1 hit.
[Graphical view ]
PIRSFi PIRSF011861. Biotinidase. 1 hit.
SUPFAMi SSF56317. SSF56317. 1 hit.
PROSITEi PS50263. CN_HYDROLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiVNN1_MOUSE
AccessioniPrimary (citable) accession number: Q9Z0K8
Secondary accession number(s): Q3TJI0, Q8VCT1, Q9DCH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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