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Database: UniProt
Entry: VNN3_MOUSE
LinkDB: VNN3_MOUSE
Original site: VNN3_MOUSE 
ID   VNN3_MOUSE              Reviewed;         500 AA.
AC   Q9QZ25; E9QMT9;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   24-JAN-2024, entry version 146.
DE   RecName: Full=Vascular non-inflammatory molecule 3;
DE            Short=Vanin-3;
DE   Flags: Precursor;
GN   Name=Vnn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=10501839; DOI=10.1007/s002510050580;
RA   Granjeaud S., Naquet P., Galland F.;
RT   "An ESTs description of the new vanin gene family conserved from fly to
RT   human.";
RL   Immunogenetics 49:964-972(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=11491533; DOI=10.1007/s002510100327;
RA   Martin F., Malergue F., Pitari G., Philippe J.M., Philips S., Chabret C.,
RA   Granjeaud S., Mattei M.G., Mungall A.J., Naquet P., Galland F.;
RT   "Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode
RT   isoforms of pantetheinase ectoenzymes.";
RL   Immunogenetics 53:296-306(2001).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}. Note=According to PubMed:11491533, secreted.
CC       {ECO:0000269|PubMed:11491533}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous with higher expression in liver.
CC       {ECO:0000269|PubMed:11491533}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC       BTD/VNN family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB59323.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ132103; CAB59323.1; ALT_INIT; mRNA.
DR   EMBL; AC153973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS23734.1; -.
DR   RefSeq; NP_036109.3; NM_011979.2.
DR   AlphaFoldDB; Q9QZ25; -.
DR   SMR; Q9QZ25; -.
DR   STRING; 10090.ENSMUSP00000020190; -.
DR   GlyCosmos; Q9QZ25; 5 sites, No reported glycans.
DR   GlyGen; Q9QZ25; 5 sites.
DR   iPTMnet; Q9QZ25; -.
DR   PhosphoSitePlus; Q9QZ25; -.
DR   CPTAC; non-CPTAC-4002; -.
DR   MaxQB; Q9QZ25; -.
DR   PaxDb; 10090-ENSMUSP00000020190; -.
DR   ProteomicsDB; 297576; -.
DR   Antibodypedia; 2278; 87 antibodies from 22 providers.
DR   DNASU; 26464; -.
DR   Ensembl; ENSMUST00000020190.8; ENSMUSP00000020190.8; ENSMUSG00000020010.8.
DR   GeneID; 26464; -.
DR   KEGG; mmu:26464; -.
DR   UCSC; uc007eqb.2; mouse.
DR   AGR; MGI:1347055; -.
DR   CTD; 26464; -.
DR   MGI; MGI:1347055; Vnn3.
DR   VEuPathDB; HostDB:ENSMUSG00000020010; -.
DR   eggNOG; KOG0806; Eukaryota.
DR   GeneTree; ENSGT00390000013823; -.
DR   HOGENOM; CLU_033209_2_0_1; -.
DR   InParanoid; Q9QZ25; -.
DR   OMA; ERHYEIS; -.
DR   OrthoDB; 4006627at2759; -.
DR   PhylomeDB; Q9QZ25; -.
DR   TreeFam; TF323645; -.
DR   BioGRID-ORCS; 26464; 2 hits in 76 CRISPR screens.
DR   PRO; PR:Q9QZ25; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q9QZ25; Protein.
DR   Bgee; ENSMUSG00000020010; Expressed in granulocyte and 33 other cell types or tissues.
DR   Genevisible; Q9QZ25; MM.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
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; IDA:BHF-UCL.
DR   GO; GO:0015939; P:pantothenate metabolic process; IDA:BHF-UCL.
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:SF4; VASCULAR NON-INFLAMMATORY MOLECULE 3; 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   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..469
FT                   /note="Vascular non-inflammatory molecule 3"
FT                   /id="PRO_0000019722"
FT   PROPEP          470..500
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000019723"
FT   DOMAIN          31..307
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   LIPID           469
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        39
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        270
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        319
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        393
FT                   /note="V -> G (in Ref. 1; CAB59323)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   500 AA;  56305 MW;  46F29333292C5AED CRC64;
     MASLHFPQWA VSFVFFAQAV GSMDTFIAAV YEHAVILPNK TESPVSTEEA LLLINKNIDI
     LESAIKLAAR QGAHIIVTPE DGIYGWIFTR ETIYPYLEDI PDPEVNWIPC RDPRRFGYTP
     VQERLSCLAK ENSIYIMANI GDKKPCNATD PHCPPDGRYQ YNTNVVFDSK GRLTARYHKY
     NLFEPEIQFD FPKDSELVTF DTPFGKFGIF TCFDIFSYDP AVVVVKDTQV DSVLLPTAWY
     NTLPLLSAVP FHSVWARAMG VNVLAANTHN TSMHMTGSGI YSPEAVRVYH YDMETESGQL
     LLSELRSRPR QHATPAEVNW SAYARTVKPF SSGQADFPGK IYFDEFSFTK LTGSAGNYTV
     CQKDLCCHLT YKMSESRMDE VYVLGAFDGL HTVEGQYYLQ ICTLLKCQTT NSRTCGEPVG
     SAFTKFEEFS LSGTFRTKYV FPQIVLSGSQ LALERYYEVS RDGRLRSRGG APLPILVMAL
     YGRVFERDPP RLGQGPGKLQ
//
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