ID   VNN1_PIG                Reviewed;         513 AA.
AC   Q9BDJ5;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Pantetheinase;
DE            EC=3.5.1.92 {ECO:0000269|PubMed:10567687};
DE   AltName: Full=Pantetheine hydrolase;
DE   AltName: Full=Vascular non-inflammatory molecule 1;
DE            Short=Vanin-1;
DE   Flags: Precursor;
GN   Name=VNN1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Paradis V., Silversides D.W.;
RT   "Sus scrofa vanin-1 cDNA, partial sequences.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY, FUNCTION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10567687; DOI=10.1016/s0014-5793(99)01439-8;
RA   Maras B., Barra D., Dupre S., Pitari G.;
RT   "Is pantetheinase the actual identity of mouse and human vanin-1
RT   proteins?";
RL   FEBS Lett. 461:149-152(1999).
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:0000269|PubMed:10567687}.
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:0000269|PubMed:10567687};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O95497}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Detected in kidney (at protein level).
CC       {ECO:0000269|PubMed:10567687}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       BTD/VNN family. {ECO:0000305}.
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DR   EMBL; AF350911; AAK29437.2; -; mRNA.
DR   RefSeq; NP_999298.1; NM_214133.1.
DR   AlphaFoldDB; Q9BDJ5; -.
DR   SMR; Q9BDJ5; -.
DR   STRING; 9823.ENSSSCP00000004514; -.
DR   PaxDb; Q9BDJ5; -.
DR   PRIDE; Q9BDJ5; -.
DR   GeneID; 397246; -.
DR   KEGG; ssc:397246; -.
DR   CTD; 8876; -.
DR   eggNOG; KOG0806; Eukaryota.
DR   InParanoid; Q9BDJ5; -.
DR   OrthoDB; 1276751at2759; -.
DR   BRENDA; 3.5.1.92; 6170.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; 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; Direct protein sequencing; Glycoprotein; GPI-anchor;
KW   Hydrolase; Lipoprotein; Membrane; Reference proteome; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..487
FT                   /note="Pantetheinase"
FT                   /id="PRO_0000019716"
FT   PROPEP          488..513
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000019717"
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           487
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        353
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   513 AA;  57156 MW;  7473C080716FA311 CRC64;
     MITSPLLAYV AILFFCVLKA SSLDTFIAAV YEHAAILPDA PLTPVSHEEA LMLMNRNLDL
     LEGAVTSAAK QGAHIIVTPE DGVYGFFFSR ESIYSYLEDI PDPHVNWIPC TNPSRFGHTP
     VQKRLSCLAR DNSIYIVANI GDKKPCNASD PDCPHDGRYQ YNTDVVFDSE GRLVARYHKQ
     NLFLGEDQFD APKEPEIVTF DTTFGRFGIF TCFGILFHDP AVTLVKDFQV DTILFPTAWM
     NVLPHLTAIE FHSAWAMGMR VNFLAANIHF PLRKMTGSGI YAPDSPRAFH YDMKTKEGKL
     LLSQLDSHPH RPAVNWTSYA SGLPTPLVGN QEFKSTVFFD EFTFLELKGV AGNYTVCQKD
     LCCQLSYRML EKREDEVYAL GAFDGLHTVE GSYYLQICTL LKCKTMDLHS CGDSVETAST
     RFEMFSLSGT FGTQYVFPEV LLSDIQLAPG EFQVSSDGRL FSLKPPSGPV LTVTLFGRLY
     ERDSASGASA DLVAQGLRVM LGVIITIMYS LSW