ID A0A140T891_BOVIN Unreviewed; 515 AA. AC A0A140T891; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 29-MAY-2024, sequence version 2. DT 02-OCT-2024, entry version 42. DE RecName: Full=Pantetheinase {ECO:0000256|ARBA:ARBA00039352}; DE EC=3.5.1.92 {ECO:0000256|ARBA:ARBA00039042}; DE AltName: Full=Pantetheine hydrolase {ECO:0000256|ARBA:ARBA00043080}; DE AltName: Full=Vascular non-inflammatory molecule 1 {ECO:0000256|ARBA:ARBA00041612}; GN Name=VNN1 {ECO:0000313|VGNC:VGNC:36807}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000020086.6, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000020086.6, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000020086.6, RC ECO:0000313|Proteomes:UP000009136}; RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A., RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C., RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.; RT "ARS-UCD1.2."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSBTAP00000020086.6} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000020086.6}; RG Ensembl; RL Submitted (JUN-2024) to UniProtKB. CC -!- FUNCTION: Amidohydrolase that hydrolyzes specifically one of the CC carboamide linkages in D-pantetheine thus recycling pantothenic acid CC (vitamin B5) and releasing cysteamine. {ECO:0000256|ARBA:ARBA00037598}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-pantetheine + H2O = (R)-pantothenate + cysteamine; CC Xref=Rhea:RHEA:13445, ChEBI:CHEBI:15377, ChEBI:CHEBI:16753, CC ChEBI:CHEBI:29032, ChEBI:CHEBI:58029; EC=3.5.1.92; CC Evidence={ECO:0000256|ARBA:ARBA00036605}; CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; CC Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}. Membrane CC {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor CC {ECO:0000256|ARBA:ARBA00004589}. CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. CC BTD/VNN family. {ECO:0000256|ARBA:ARBA00008225}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; A0A140T891; -. DR Ensembl; ENSBTAT00000020086.7; ENSBTAP00000020086.6; ENSBTAG00000015094.7. DR KEGG; bta:526704; -. DR CTD; 8876; -. DR VEuPathDB; HostDB:ENSBTAG00000015094; -. DR VGNC; VGNC:36807; VNN1. DR GeneTree; ENSGT00390000013823; -. DR InParanoid; A0A140T891; -. DR OMA; NWIPCID; -. DR Reactome; R-BTA-163125; Post-translational modification: synthesis of GPI-anchored proteins. DR Reactome; R-BTA-199220; Vitamin B5 (pantothenate) metabolism. DR Reactome; R-BTA-6798695; Neutrophil degranulation. DR Proteomes; UP000009136; Chromosome 9. DR Bgee; ENSBTAG00000015094; Expressed in olfactory segment of nasal mucosa and 98 other cell types or tissues. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0017159; F:pantetheine hydrolase activity; IBA:GO_Central. DR GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl. DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl. DR GO; GO:0002544; P:chronic inflammatory response; IEA:Ensembl. DR GO; GO:0015938; P:coenzyme A catabolic process; IEA:Ensembl. DR GO; GO:0045087; P:innate immune response; IEA:Ensembl. DR GO; GO:0015939; P:pantothenate metabolic process; IBA:GO_Central. DR GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl. DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IEA:Ensembl. DR CDD; cd07567; biotinidase_like; 1. DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1. DR InterPro; IPR012101; Biotinidase-like_euk. DR InterPro; IPR040154; Biotinidase/VNN. DR InterPro; IPR003010; C-N_Hydrolase. DR InterPro; IPR036526; C-N_Hydrolase_sf. DR InterPro; IPR043957; Vanin_C. DR PANTHER; PTHR10609; BIOTINIDASE-RELATED; 1. DR PANTHER; PTHR10609:SF16; PANTETHEINASE; 1. DR Pfam; PF00795; CN_hydrolase; 1. DR Pfam; PF19018; Vanin_C; 1. DR PIRSF; PIRSF011861; Biotinidase; 1. DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 1. DR PROSITE; PS50263; CN_HYDROLASE; 1. PE 3: Inferred from homology; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288}; KW Membrane {ECO:0000256|ARBA:ARBA00022622}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..22 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 23..515 FT /note="Pantetheinase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5041987784" FT DOMAIN 31..307 FT /note="CN hydrolase" FT /evidence="ECO:0000259|PROSITE:PS50263" FT ACT_SITE 80 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR011861-1" FT ACT_SITE 179 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR011861-1" FT ACT_SITE 212 FT /note="Nucleophile" FT /evidence="ECO:0000256|PIRSR:PIRSR011861-1" SQ SEQUENCE 515 AA; 57612 MW; 266C8B3BA8F71573 CRC64; MIMSQLLNYV AVLFFCVSRA SSLDTFIAAV YEHAVILPNA TLVPVSPEEA LAVMNRNLDL LEGAVTSASK QGAHIIVTPE DGIYGFNFTR ESIYPYLEDI PDPQVNWIPC NNPDRFGHTP VQQRLSCLAK DNSIYIVANI GDKKSCNASD PQCPPDGRYQ YNTDVVFDTK GKLVARYHKQ NLFLNEDQFN APKEPEVVTF NTTFGKFGIF TCFDILFHDP AVTLVRDSRV DTILFPTAWM NVLPHLSAIE FHSAWAMGMR VNFLASNLHY PLKKMTGSGI YAPDSPRAFH YDMKTEEGKL LLAQLDSHPH PTPVVNWTSY ASGVEAHSVG NQEFTGIIFF DEFTFLELKE IGGNYTVCQR DLCCHLSYKM SEKRSDEVYA LGAFDGLHTV EGSYYLQICT LLKCKTTDLH TCGDSVETAS TRFEMFSLSG TFGTQYVFPE VLLSEIQLAP GEFQVSNDGR LFSLKPTSGP VLTVTLFGRL YEKDSAPNTL SDLTTQALRG DYKVDVYQIW LHNGL //