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Vascular non-inflammatory molecule 3 (Vanin-3) (EC 3.5.1.92)

 VNN3_HUMAN              Reviewed;         501 AA.
Q9NY84; B2DFY0; B2DFY1; B2DFY3; B2DFY5; B2DFY6; B2DFY7; B2DFY8;
Q3SX90; Q9BQY2;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
07-FEB-2006, sequence version 2.
25-OCT-2017, entry version 143.
RecName: Full=Vascular non-inflammatory molecule 3;
Short=Vanin-3;
EC=3.5.1.92;
Flags: Precursor;
Name=VNN3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-222, FUNCTION, AND
TISSUE SPECIFICITY.
PubMed=11491533; DOI=10.1007/s002510100327;
Martin F., Malergue F., Pitari G., Philippe J.M., Philips S.,
Chabret C., Granjeaud S., Mattei M.G., Mungall A.J., Naquet P.,
Galland F.;
"Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode
isoforms of pantetheinase ectoenzymes.";
Immunogenetics 53:296-306(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7 AND 8).
TISSUE=Neutrophil;
PubMed=18805469; DOI=10.1016/j.gene.2008.08.019;
Nitto T., Inoue T., Node K.;
"Alternative spliced variants in the pantetheinase family of genes
expressed in human neutrophils.";
Gene 426:57-64(2008).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-33; ALA-89; LYS-91
AND ALA-222.
NIEHS SNPs program;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 95-489 (ISOFORM 1), AND VARIANT ALA-222.
TISSUE=Liver;
PubMed=10501839; DOI=10.1007/s002510050580;
Granjeaud S., Naquet P., Galland F.;
"An ESTs description of the new vanin gene family conserved from fly
to human.";
Immunogenetics 49:964-972(1999).
[8]
TISSUE SPECIFICITY, AND INDUCTION BY CYTOKINES.
PubMed=19322213; DOI=10.1038/jid.2009.67;
Jansen P.A.M., Kamsteeg M., Rodijk-Olthuis D.,
van Vlijmen-Willems I.M.J.J., de Jongh G.J., Bergers M.,
Tjabringa G.S., Zeeuwen P.L.J.M., Schalkwijk J.;
"Expression of the vanin gene family in normal and inflamed human
skin: induction by proinflammatory cytokines.";
J. Invest. Dermatol. 129:2167-2174(2009).
-!- FUNCTION: Amidohydrolase that hydrolyzes specifically one of the
carboamide linkages in D-pantetheine thus recycling pantothenic
acid (vitamin B5) and releasing cysteamine.
{ECO:0000269|PubMed:11491533}.
-!- CATALYTIC ACTIVITY: (R)-pantetheine + H(2)O = (R)-pantothenate +
2-aminoethanethiol.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor,
GPI-anchor {ECO:0000305}. Note=According to PubMed:11491533,
secreted. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1;
IsoId=Q9NY84-1; Sequence=Displayed;
Name=2; Synonyms=PAGEL-gamma;
IsoId=Q9NY84-2; Sequence=VSP_017138, VSP_017139;
Note=Expressed in neutrophils, this isoform displays a
frameshift at Glu-227 due to one missing nucleotide compared to
isoform 1, this missing nucleotide could be a variation as it is
also present on genomic sequence.;
Name=3; Synonyms=PAGEL-alpha;
IsoId=Q9NY84-3; Sequence=VSP_029578, VSP_029579;
Name=4; Synonyms=PAGEL-beta;
IsoId=Q9NY84-4; Sequence=VSP_038563, VSP_038567;
Name=5; Synonyms=PAGEL-delta;
IsoId=Q9NY84-5; Sequence=VSP_038568, VSP_038569;
Name=6; Synonyms=PAGEL-epsilon;
IsoId=Q9NY84-6; Sequence=VSP_038562, VSP_038566;
Name=7; Synonyms=PAGEL-zeta;
IsoId=Q9NY84-7; Sequence=VSP_038564, VSP_038565;
Name=8; Synonyms=PAGEL-eta;
IsoId=Q9NY84-8; Sequence=VSP_038561, VSP_038564, VSP_038565;
-!- TISSUE SPECIFICITY: Widely expressed with higher expression in
liver and blood. Expressed in differentiated keratinocytes in
epidermis and in epithelial cells in dermis. Overexpressed in
lesional psoriatic skin. {ECO:0000269|PubMed:11491533,
ECO:0000269|PubMed:19322213}.
-!- INDUCTION: By Th17/Th1 type cytokines, but not by Th2-type.
{ECO:0000269|PubMed:19322213}.
-!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
BTD/VNN family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/vnn3/";
-----------------------------------------------------------------------
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EMBL; AJ238982; CAB76824.1; -; mRNA.
EMBL; AB435052; BAG30924.1; -; mRNA.
EMBL; AB435053; BAG30925.1; -; mRNA.
EMBL; AB435054; BAG30926.1; -; mRNA.
EMBL; AB435055; BAG30927.1; -; mRNA.
EMBL; AB435056; BAG30928.1; -; mRNA.
EMBL; AB435057; BAG30929.1; -; mRNA.
EMBL; AB435058; BAG30930.1; -; mRNA.
EMBL; AB435059; BAG30931.1; -; mRNA.
EMBL; AB435060; BAG30932.1; -; mRNA.
EMBL; AB435061; BAG30933.1; -; mRNA.
EMBL; DQ220706; ABA60895.1; -; Genomic_DNA.
EMBL; AL032821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471051; EAW48017.1; -; Genomic_DNA.
EMBL; BC104416; AAI04417.1; -; mRNA.
EMBL; BC104417; AAI04418.1; -; mRNA.
RefSeq; NP_001278632.1; NM_001291703.1.
UniGene; Hs.183656; -.
ProteinModelPortal; Q9NY84; -.
SMR; Q9NY84; -.
BioGrid; 120630; 1.
STRING; 9606.ENSP00000440594; -.
PhosphoSitePlus; Q9NY84; -.
DMDM; 88952267; -.
PaxDb; Q9NY84; -.
PeptideAtlas; Q9NY84; -.
PRIDE; Q9NY84; -.
Ensembl; ENST00000275223; ENSP00000443073; ENSG00000093134. [Q9NY84-3]
Ensembl; ENST00000367927; ENSP00000438024; ENSG00000093134. [Q9NY84-2]
Ensembl; ENST00000392393; ENSP00000441182; ENSG00000093134. [Q9NY84-4]
Ensembl; ENST00000414302; ENSP00000444505; ENSG00000093134. [Q9NY84-6]
Ensembl; ENST00000417437; ENSP00000463583; ENSG00000093134. [Q9NY84-8]
Ensembl; ENST00000423615; ENSP00000443901; ENSG00000093134. [Q9NY84-7]
Ensembl; ENST00000425515; ENSP00000439449; ENSG00000093134. [Q9NY84-3]
Ensembl; ENST00000427187; ENSP00000444491; ENSG00000093134. [Q9NY84-5]
Ensembl; ENST00000509351; ENSP00000464241; ENSG00000093134. [Q9NY84-7]
Ensembl; ENST00000519686; ENSP00000438175; ENSG00000093134. [Q9NY84-3]
GeneID; 55350; -.
KEGG; hsa:55350; -.
UCSC; uc011ecl.3; human. [Q9NY84-1]
CTD; 55350; -.
DisGeNET; 55350; -.
EuPathDB; HostDB:ENSG00000093134.13; -.
GeneCards; VNN3; -.
H-InvDB; HIX0032812; -.
HGNC; HGNC:16431; VNN3.
HPA; HPA010818; -.
MIM; 606592; gene.
neXtProt; NX_Q9NY84; -.
OpenTargets; ENSG00000093134; -.
eggNOG; KOG0806; Eukaryota.
eggNOG; COG0388; LUCA.
GeneTree; ENSGT00390000013823; -.
HOVERGEN; HBG103088; -.
InParanoid; Q9NY84; -.
OMA; CLCKSAG; -.
PhylomeDB; Q9NY84; -.
BRENDA; 3.5.1.92; 2681.
Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
GenomeRNAi; 55350; -.
PRO; PR:Q9NY84; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000093134; -.
CleanEx; HS_VNN3; -.
ExpressionAtlas; Q9NY84; baseline and differential.
Genevisible; Q9NY84; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0017159; F:pantetheine hydrolase activity; IBA:GO_Central.
GO; GO:0006501; P:C-terminal protein lipidation; TAS:Reactome.
GO; GO:0015939; P:pantothenate metabolic process; IBA:GO_Central.
CDD; cd07567; biotinidase_like; 1.
Gene3D; 3.60.110.10; -; 1.
InterPro; IPR012101; Biotinidase-like_euk.
InterPro; IPR003010; C-N_Hydrolase.
InterPro; IPR036526; C-N_Hydrolase_sf.
Pfam; PF00795; CN_hydrolase; 1.
PIRSF; PIRSF011861; Biotinidase; 1.
SUPFAM; SSF56317; SSF56317; 1.
PROSITE; PS50263; CN_HYDROLASE; 1.
2: Evidence at transcript level;
Alternative splicing; Cell membrane; Complete proteome; Glycoprotein;
GPI-anchor; Hydrolase; Lipoprotein; Membrane; Polymorphism;
Reference proteome; Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 470 Vascular non-inflammatory molecule 3.
/FTId=PRO_0000019720.
PROPEP 471 501 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000019721.
DOMAIN 31 307 CN hydrolase. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
ACT_SITE 80 80 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
ACT_SITE 179 179 Proton donor. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
ACT_SITE 212 212 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU00054}.
LIPID 470 470 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 147 147 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 270 270 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 358 358 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 70 70 K -> KQVLPFYTCKGDLQFGQRVFGIHDKLFCPTCFE
(in isoform 8).
{ECO:0000303|PubMed:18805469}.
/FTId=VSP_038561.
VAR_SEQ 115 133 RFGNTPVQQRLSCLAKDNS -> STIFLHLKFSLISPRIQN
L (in isoform 6).
{ECO:0000303|PubMed:18805469}.
/FTId=VSP_038562.
VAR_SEQ 116 147 FGNTPVQQRLSCLAKDNSIYVVANIGDKKPCN -> KSKKM
NEPVSKELCYHCHSECNQYGQWKLYRT (in isoform
4). {ECO:0000303|PubMed:18805469}.
/FTId=VSP_038563.
VAR_SEQ 116 129 FGNTPVQQRLSCLA -> EWNLRPRSSQGVPL (in
isoform 7 and isoform 8).
{ECO:0000303|PubMed:18805469}.
/FTId=VSP_038564.
VAR_SEQ 116 117 FG -> NH (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:18805469}.
/FTId=VSP_029578.
VAR_SEQ 118 501 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:18805469}.
/FTId=VSP_029579.
VAR_SEQ 130 501 Missing (in isoform 7 and isoform 8).
{ECO:0000303|PubMed:18805469}.
/FTId=VSP_038565.
VAR_SEQ 134 501 Missing (in isoform 6).
{ECO:0000303|PubMed:18805469}.
/FTId=VSP_038566.
VAR_SEQ 148 501 Missing (in isoform 4).
{ECO:0000303|PubMed:18805469}.
/FTId=VSP_038567.
VAR_SEQ 180 207 YNLFAPEIQFDFPKDSELVTFDTPFGKF -> GVESTPQKQ
SRCTTMTWKQRVVSCCYQN (in isoform 5).
{ECO:0000303|PubMed:18805469}.
/FTId=VSP_038568.
VAR_SEQ 208 501 Missing (in isoform 5).
{ECO:0000303|PubMed:18805469}.
/FTId=VSP_038569.
VAR_SEQ 228 274 VSIDSILYPTAWYNTLPLLSAVPFHSAWAKAMGVNLLAANT
HNTSMH -> FQLTAFSTPQHGTTRCPSSRLFPSIQHGPRP
WESIYLLQIPTTPACT (in isoform 2).
{ECO:0000303|PubMed:18805469}.
/FTId=VSP_017138.
VAR_SEQ 275 501 Missing (in isoform 2).
{ECO:0000303|PubMed:18805469}.
/FTId=VSP_017139.
VARIANT 33 33 H -> R (in dbSNP:rs764264).
{ECO:0000269|Ref.3}.
/FTId=VAR_025265.
VARIANT 89 89 T -> A (in dbSNP:rs36012859).
{ECO:0000269|Ref.3}.
/FTId=VAR_025266.
VARIANT 91 91 E -> K (in dbSNP:rs12174042).
{ECO:0000269|Ref.3}.
/FTId=VAR_025267.
VARIANT 222 222 V -> A (in dbSNP:rs6569834).
{ECO:0000269|PubMed:10501839,
ECO:0000269|PubMed:11491533,
ECO:0000269|Ref.3}.
/FTId=VAR_025268.
SEQUENCE 501 AA; 56118 MW; 9305A7B2AB68F687 CRC64;
MIISHFPKCV AVFALLALSV GALDTFIAAV YEHAVILPNR TETPVSKEEA LLLMNKNIDV
LEKAVKLAAK QGAHIIVTPE DGIYGWIFTR ESIYPYLEDI PDPGVNWIPC RDPWRFGNTP
VQQRLSCLAK DNSIYVVANI GDKKPCNASD SQCPPDGRYQ YNTDVVFDSQ GKLLARYHKY
NLFAPEIQFD FPKDSELVTF DTPFGKFGIF TCFDIFSHDP AVVVVDEVSI DSILYPTAWY
NTLPLLSAVP FHSAWAKAMG VNLLAANTHN TSMHMTGSGI YAPEAVKVYH YDMETESGQL
LLSELKSRPR REPTYPAAVD WHAYASSVKP FSSEQSDFLG MIYFDEFTFT KLKRNTGNYT
ACQKDLCCHL TYKMSEKRTD EIYALGAFDG LHTVEGQYYL QICALLKCQT TDLETCGEPV
GSAFTKFEDF SLSGTFGTRY VFPQIILSGS QLAPERHYEI SRDGRLRSRS GAPLPVLVMA
LYGRVFEKDP PRLGQGSGKF Q


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