VNN1_BOVIN
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 25-MAY-2022, entry version 97.
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 iPTMnet; Q58CQ9; -.
DR PaxDb; Q58CQ9; -.
DR PRIDE; Q58CQ9; -.
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 OrthoDB; 1276751at2759; -.
DR TreeFam; TF323645; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; -; 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; PTHR10609; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF19018; Vanin_C; 1.
DR PIRSF; PIRSF011861; Biotinidase; 1.
DR SUPFAM; SSF56317; SSF56317; 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
