ID   VNN1_BOVIN              Reviewed;         510 AA.
AC   Q58CQ9; A6QPH4;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   08-NOV-2023, entry version 101.
DE   RecName: Full=Pantetheinase;
DE            EC=3.5.1.92 {ECO:0000250|UniProtKB:O95497};
DE   AltName: Full=Pantetheine hydrolase;
DE   AltName: Full=Vascular non-inflammatory molecule 1;
DE            Short=Vanin-1;
DE   Flags: Precursor;
GN   Name=VNN1;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal medulla;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   GLYCOSYLATION AT THR-504, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=19674964; DOI=10.1074/mcp.m900211-mcp200;
RA   Darula Z., Medzihradszky K.F.;
RT   "Affinity enrichment and characterization of mucin core-1 type
RT   glycopeptides from bovine serum.";
RL   Mol. Cell. Proteomics 8:2515-2526(2009).
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:0000250|UniProtKB:O95497}.
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:0000250|UniProtKB:O95497};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O95497}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       BTD/VNN family. {ECO:0000305}.
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DR   EMBL; BT021888; AAX46735.1; -; mRNA.
DR   EMBL; BC149325; AAI49326.1; -; mRNA.
DR   RefSeq; NP_001019727.2; NM_001024556.2.
DR   AlphaFoldDB; Q58CQ9; -.
DR   SMR; Q58CQ9; -.
DR   STRING; 9913.ENSBTAP00000020086; -.
DR   GlyConnect; 772; 1 O-Linked glycan (1 site).
DR   GlyCosmos; Q58CQ9; 7 sites, 1 glycan.
DR   iPTMnet; Q58CQ9; -.
DR   PaxDb; 9913-ENSBTAP00000020086; -.
DR   GeneID; 526704; -.
DR   KEGG; bta:526704; -.
DR   CTD; 8876; -.
DR   eggNOG; KOG0806; Eukaryota.
DR   HOGENOM; CLU_033209_2_0_1; -.
DR   InParanoid; Q58CQ9; -.
DR   TreeFam; TF323645; -.
DR   Proteomes; UP000009136; Unplaced.
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; ISS:UniProtKB.
DR   GO; GO:0015939; P:pantothenate metabolic process; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW   Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..492
FT                   /note="Pantetheinase"
FT                   /id="PRO_0000239702"
FT   PROPEP          493..510
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000239703"
FT   DOMAIN          31..307
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        80
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        179
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        212
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   LIPID           492
FT                   /note="GPI-anchor amidated aspartate"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        87
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        504
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000269|PubMed:19674964"
FT   CONFLICT        169
FT                   /note="S -> T (in Ref. 2; AAI49326)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229
FT                   /note="H -> R (in Ref. 2; AAI49326)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   510 AA;  56947 MW;  F38CF8E2D14ADD03 CRC64;
     MIMSQLLNYV AVLFFCVSRA SSLDTFIAAV YEHAVILPNA TLVPVSPEEA LAVMNRNLDL
     LEGAVTSASK QGAHIIVTPE DGIYGFNFTR ESIYPYLEDI PDPQVNWIPC NNPDRFGHTP
     VQQRLSCLAK DNSIYIVANI GDKKSCNASD PQCPPDGRYQ YNTDVVFDSK GKLVARYHKQ
     NLFLNEDQFN APKEPEVVTF NTTFGKFGIF TCFDILFHDP AVTLVRDSHV 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 SDLTTQALRL NPKTDAWKSK
//