ID   VNN1_CANLF              Reviewed;         514 AA.
AC   Q9TSX8;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Pantetheinase;
DE            EC=3.5.1.92 {ECO:0000250|UniProtKB:O95497};
DE   AltName: Full=Pantetheine hydrolase;
DE   AltName: Full=Tiff66;
DE   AltName: Full=Vascular non-inflammatory molecule 1;
DE            Short=Vanin-1;
DE   Flags: Precursor;
GN   Name=VNN1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RA   Prehn S., Hartmann E., Fridrichson T., Henske A., Boehm S., Otto A.,
RA   Ziesche W., Kurzchalia T.;
RT   "Isolation and identification of canine TIFF66.";
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
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; U39663; AAF21452.1; -; mRNA.
DR   RefSeq; NP_001003372.1; NM_001003372.1.
DR   AlphaFoldDB; Q9TSX8; -.
DR   SMR; Q9TSX8; -.
DR   STRING; 9615.ENSCAFP00000000268; -.
DR   PaxDb; Q9TSX8; -.
DR   Ensembl; ENSCAFT00845008456; ENSCAFP00845006661; ENSCAFG00845004723.
DR   Ensembl; ENSCAFT00845008537; ENSCAFP00845006737; ENSCAFG00845004762.
DR   GeneID; 442973; -.
DR   KEGG; cfa:442973; -.
DR   CTD; 8876; -.
DR   VEuPathDB; HostDB:ENSCAFG00845004723; -.
DR   VEuPathDB; HostDB:ENSCAFG00845004762; -.
DR   eggNOG; KOG0806; Eukaryota.
DR   GeneTree; ENSGT00390000013823; -.
DR   InParanoid; Q9TSX8; -.
DR   OrthoDB; 1276751at2759; -.
DR   Proteomes; UP000002254; Chromosome 1.
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   2: Evidence at transcript 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_0000019710"
FT   PROPEP          493..514
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000019711"
FT   DOMAIN          40..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        316
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        354
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   514 AA;  57432 MW;  7A7BD64C1A1C62CE CRC64;
     MITSRLLVYV AVLVLCVIKV SSRDTFIAAV YEHAVKLPNA TLVPVSHEEA LAVMNQNLDL
     LEAAITSAAN QGAHIIVTPE DGIYGWNFSR ETIYPYLEDI PDPGVNWIPC NNPKRFGYTP
     VQERLSCLAK DNSIYVVANI GDKKPCNASD SQCPLDGRYQ YNTDVVFDSQ GKLVARYHKH
     NLFMGENQFN VPKKPEIVTF DTIFGRFGVF TCFDILFYDP AVTLVKDFHV DTIVFPTAWM
     NVLPHLSAIQ FHSAWAMGMG VNFLASNIHH PSKRMTGSGI YAPDSPRAFH YDMKTKEGKL
     LLSQLDSYTH HPIVVNWTSY ASGIKAFPTE NQEFTGTAFF DEFTFLELTR VTGNYTVCQK
     KLCCHLSYKM SEKRTDEVYA LGAFDGLHVV EGRYYLQICT LLKCKTAHVH TCGGAVETAS
     TRFDMFSLSG TFGTQYVFPE VLLSETQLAP GEFQVSSDGR LFSMKPLSGP LLTVTLFGRI
     YEKDQTLKAS SDPRSQVPGV MLLVIIPIVC SLSW