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Protein

Pantetheinase

Gene

VNN1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei80 – 801Proton acceptorPROSITE-ProRule annotation
Active sitei179 – 1791Proton donorPROSITE-ProRule annotation
Active sitei212 – 2121NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 492470PantetheinasePRO_0000239702Add
BLAST
Propeptidei493 – 51018Removed in mature formSequence AnalysisPRO_0000239703Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi39 – 391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi87 – 871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis
Lipidationi492 – 4921GPI-anchor amidated aspartateSequence Analysis
Glycosylationi504 – 5041O-linked (GalNAc...)1 Publication

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PRIDEiQ58CQ9.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000020086.

Structurei

3D structure databases

ProteinModelPortaliQ58CQ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 336311CN hydrolasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CN hydrolase domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0388.
HOGENOMiHOG000007627.
HOVERGENiHBG003996.
InParanoidiQ58CQ9.
KOiK08069.
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.

Q58CQ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIMSQLLNYV AVLFFCVSRA SSLDTFIAAV YEHAVILPNA TLVPVSPEEA
60 70 80 90 100
LAVMNRNLDL LEGAVTSASK QGAHIIVTPE DGIYGFNFTR ESIYPYLEDI
110 120 130 140 150
PDPQVNWIPC NNPDRFGHTP VQQRLSCLAK DNSIYIVANI GDKKSCNASD
160 170 180 190 200
PQCPPDGRYQ YNTDVVFDSK GKLVARYHKQ NLFLNEDQFN APKEPEVVTF
210 220 230 240 250
NTTFGKFGIF TCFDILFHDP AVTLVRDSHV DTILFPTAWM NVLPHLSAIE
260 270 280 290 300
FHSAWAMGMR VNFLASNLHY PLKKMTGSGI YAPDSPRAFH YDMKTEEGKL
310 320 330 340 350
LLAQLDSHPH PTPVVNWTSY ASGVEAHSVG NQEFTGIIFF DEFTFLELKE
360 370 380 390 400
IGGNYTVCQR DLCCHLSYKM SEKRSDEVYA LGAFDGLHTV EGSYYLQICT
410 420 430 440 450
LLKCKTTDLH TCGDSVETAS TRFEMFSLSG TFGTQYVFPE VLLSEIQLAP
460 470 480 490 500
GEFQVSNDGR LFSLKPTSGP VLTVTLFGRL YEKDSAPNTL SDLTTQALRL
510
NPKTDAWKSK
Length:510
Mass (Da):56,947
Last modified:April 26, 2005 - v1
Checksum:iF38CF8E2D14ADD03
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti169 – 1691S → T in AAI49326 (Ref. 2) Curated
Sequence conflicti229 – 2291H → R in AAI49326 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021888 mRNA. Translation: AAX46735.1.
BC149325 mRNA. Translation: AAI49326.1.
RefSeqiNP_001019727.2. NM_001024556.2.
UniGeneiBt.28243.

Genome annotation databases

GeneIDi526704.
KEGGibta:526704.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021888 mRNA. Translation: AAX46735.1.
BC149325 mRNA. Translation: AAI49326.1.
RefSeqiNP_001019727.2. NM_001024556.2.
UniGeneiBt.28243.

3D structure databases

ProteinModelPortaliQ58CQ9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000020086.

Proteomic databases

PRIDEiQ58CQ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi526704.
KEGGibta:526704.

Organism-specific databases

CTDi8876.

Phylogenomic databases

eggNOGiCOG0388.
HOGENOMiHOG000007627.
HOVERGENiHBG003996.
InParanoidiQ58CQ9.
KOiK08069.
OrthoDBiEOG7HF1J0.
TreeFamiTF323645.

Miscellaneous databases

NextBioi20874430.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal medulla.
  3. "Affinity enrichment and characterization of mucin core-1 type glycopeptides from bovine serum."
    Darula Z., Medzihradszky K.F.
    Mol. Cell. Proteomics 8:2515-2526(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-504, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiVNN1_BOVIN
AccessioniPrimary (citable) accession number: Q58CQ9
Secondary accession number(s): A6QPH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: April 26, 2005
Last modified: June 24, 2015
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.