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RecName: Full=Pantetheine hydrolase VNN2; AltName: Full=Glycosylphosphatidyl inositol-anchored protein GPI-80; AltName: Full=Protein FOAP-4; AltName: Full=Vascular non-inflammatory molecule 2; Short=Vanin-2; Flags: Precursor

UniProtKB/Swiss-Prot: O95498.3

Identical Proteins FASTA Graphics 

LOCUS       VNN2_HUMAN               520 aa            linear   PRI 27-NOV-2024
DEFINITION  RecName: Full=Pantetheine hydrolase VNN2; AltName:
            Full=Glycosylphosphatidyl inositol-anchored protein GPI-80;
            AltName: Full=Protein FOAP-4; AltName: Full=Vascular
            non-inflammatory molecule 2; Short=Vanin-2; Flags: Precursor.
ACCESSION   O95498
VERSION     O95498.3
DBSOURCE    UniProtKB: locus VNN2_HUMAN, accession O95498;
            class: standard.
            extra
            accessions:A0AUZ3,A6NDY1,A8K4E3,A8K7W0,B2DFZ0,B2DFZ1,B2DFZ2,B2DFZ3,
            F6XL73,Q2XUN1,Q9UJF3,Q9UMW2
            created: Apr 27, 2001.
            sequence updated: Mar 20, 2007.
            annotation updated: Nov 27, 2024.
            xrefs: AJ132100.1, CAA10569.1, D89974.1, BAA82525.1, AB435062.1,
            BAG30934.1, AB435063.1, BAG30935.1, AB435064.1, BAG30936.1,
            AB435065.1, BAG30937.1, AB026705.1, BAB61019.1, AK290908.1,
            BAF83597.1, AK292125.1, BAF84814.1, DQ249347.1, ABB72673.1,
            AL032821.2, CH471051.2, EAW48016.1, BC126145.1, AAI26146.1,
            BC126147.1, AAI26148.1, NP_001229279.1, NP_004656.2, NP_511043.1,
            XP_006715656.1, XP_016866896.1
            xrefs (non-sequence databases): CCDS:CCDS5161.1, CCDS:CCDS5162.1,
            CCDS:CCDS56451.1, AlphaFoldDB:O95498, SMR:O95498, BioGRID:114394,
            IntAct:O95498, STRING:9606.ENSP00000322276, GlyConnect:2089,
            GlyCosmos:O95498, GlyGen:O95498, iPTMnet:O95498,
            PhosphoSitePlus:O95498, SwissPalm:O95498, BioMuta:VNN2,
            jPOST:O95498, MassIVE:O95498, PaxDb:9606-ENSP00000322276,
            PeptideAtlas:O95498, ProteomicsDB:28159, ProteomicsDB:50925,
            ProteomicsDB:50926, ProteomicsDB:50927, ProteomicsDB:50928,
            ProteomicsDB:50929, Antibodypedia:32943, DNASU:8875,
            Ensembl:ENST00000326499.11, Ensembl:ENSP00000322276.6,
            Ensembl:ENSG00000112303.14, Ensembl:ENST00000525270.5,
            Ensembl:ENSP00000436822.1, Ensembl:ENST00000525289.5,
            Ensembl:ENSP00000436935.1, Ensembl:ENST00000525674.5,
            Ensembl:ENSP00000436863.1, Ensembl:ENST00000532053.5,
            Ensembl:ENSP00000434077.1, GeneID:8875, KEGG:hsa:8875,
            MANE-Select:ENST00000326499.11, UCSC:uc003qdt.4, AGR:HGNC:12706,
            CTD:8875, DisGeNET:8875, GeneCards:VNN2, HGNC:12706,
            HPA:ENSG00000112303, MIM 603571, neXtProt:NX_O95498,
            OpenTargets:ENSG00000112303, PharmGKB:PA37322,
            VEuPathDB:HostDB:ENSG00000112303, eggNOG:KOG0806,
            GeneTree:ENSGT00390000013823, HOGENOM:CLU_033209_2_0_1,
            InParanoid:O95498, OMA:PCNSHDS, OrthoDB:4006627at2759,
            PhylomeDB:O95498, TreeFam:TF323645, BRENDA:3.5.1.92,
            PathwayCommons:O95498, Reactome:R-HSA-163125,
            Reactome:R-HSA-199220, SignaLink:O95498, BioGRID-ORCS:8875,
            GeneWiki:VNN2, GenomeRNAi:8875, Pharos:O95498, PRO:PR:O95498,
            Proteomes:UP000005640, RNAct:O95498, Bgee:ENSG00000112303,
            ExpressionAtlas:O95498, GO:0005576, GO:0005886, GO:0098552,
            GO:0017159, GO:0015939, CDD:cd07567, FunFam:3.60.110.10:FF:000001,
            Gene3D:3.60.110.10, InterPro:IPR012101, InterPro:IPR040154,
            InterPro:IPR003010, InterPro:IPR036526, InterPro:IPR043957,
            PANTHER:PTHR10609, PANTHER:PTHR10609:SF15, Pfam:PF00795,
            Pfam:PF19018, PIRSF:PIRSF011861, SUPFAM:SSF56317, PROSITE:PS50263
KEYWORDS    Alternative splicing; Cell membrane; Glycoprotein; GPI-anchor;
            Hydrolase; Lipoprotein; Membrane; Proteomics identification;
            Reference proteome; Signal.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 520)
  AUTHORS   Galland,F., Malergue,F., Bazin,H., Mattei,M.G., Aurrand-Lions,M.,
            Theillet,C. and Naquet,P.
  TITLE     Two human genes related to murine vanin-1 are located on the long
            arm of human chromosome 6
  JOURNAL   Genomics 53 (2), 203-213 (1998)
   PUBMED   9790769
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-404.;
            TISSUE=Kidney
REFERENCE   2  (residues 1 to 520)
  AUTHORS   Suzuki,K., Watanabe,T., Sakurai,S., Ohtake,K., Kinoshita,T.,
            Araki,A., Fujita,T., Takei,H., Takeda,Y., Sato,Y., Yamashita,T.,
            Araki,Y. and Sendo,F.
  TITLE     A novel glycosylphosphatidyl inositol-anchored protein on human
            leukocytes: a possible role for regulation of neutrophil adherence
            and migration
  JOURNAL   J Immunol 162 (7), 4277-4284 (1999)
   PUBMED   10201959
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-404.;
            TISSUE=Peripheral blood
REFERENCE   3  (residues 1 to 520)
  AUTHORS   Nitto,T., Inoue,T. and Node,K.
  TITLE     Alternative spliced variants in the pantetheinase family of genes
            expressed in human neutrophils
  JOURNAL   Gene 426 (1-2), 57-64 (2008)
   PUBMED   18805469
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), AND VARIANT
            MET-404.;
            TISSUE=Neutrophil
REFERENCE   4  (residues 1 to 520)
  AUTHORS   Takayama,K., Fujii,Y., Tsuritani,K., Yajima,Y., Amemiya,T.,
            Ukai,Y., Naito,K. and Kawaguchi,A.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-APR-1999) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-404.;
            TISSUE=Blood
REFERENCE   5  (residues 1 to 520)
  AUTHORS   Ota,T., Suzuki,Y., Nishikawa,T., Otsuki,T., Sugiyama,T., Irie,R.,
            Wakamatsu,A., Hayashi,K., Sato,H., Nagai,K., Kimura,K., Makita,H.,
            Sekine,M., Obayashi,M., Nishi,T., Shibahara,T., Tanaka,T.,
            Ishii,S., Yamamoto,J., Saito,K., Kawai,Y., Isono,Y., Nakamura,Y.,
            Nagahari,K., Murakami,K., Yasuda,T., Iwayanagi,T., Wagatsuma,M.,
            Shiratori,A., Sudo,H., Hosoiri,T., Kaku,Y., Kodaira,H., Kondo,H.,
            Sugawara,M., Takahashi,M., Kanda,K., Yokoi,T., Furuya,T.,
            Kikkawa,E., Omura,Y., Abe,K., Kamihara,K., Katsuta,N., Sato,K.,
            Tanikawa,M., Yamazaki,M., Ninomiya,K., Ishibashi,T., Yamashita,H.,
            Murakawa,K., Fujimori,K., Tanai,H., Kimata,M., Watanabe,M.,
            Hiraoka,S., Chiba,Y., Ishida,S., Ono,Y., Takiguchi,S., Watanabe,S.,
            Yosida,M., Hotuta,T., Kusano,J., Kanehori,K., Takahashi-Fujii,A.,
            Hara,H., Tanase,T.O., Nomura,Y., Togiya,S., Komai,F., Hara,R.,
            Takeuchi,K., Arita,M., Imose,N., Musashino,K., Yuuki,H., Oshima,A.,
            Sasaki,N., Aotsuka,S., Yoshikawa,Y., Matsunawa,H., Ichihara,T.,
            Shiohata,N., Sano,S., Moriya,S., Momiyama,H., Satoh,N., Takami,S.,
            Terashima,Y., Suzuki,O., Nakagawa,S., Senoh,A., Mizoguchi,H.,
            Goto,Y., Shimizu,F., Wakebe,H., Hishigaki,H., Watanabe,T.,
            Sugiyama,A., Takemoto,M., Kawakami,B., Yamazaki,M., Watanabe,K.,
            Kumagai,A., Itakura,S., Fukuzumi,Y., Fujimori,Y., Komiyama,M.,
            Tashiro,H., Tanigami,A., Fujiwara,T., Ono,T., Yamada,K., Fujii,Y.,
            Ozaki,K., Hirao,M., Ohmori,Y., Kawabata,A., Hikiji,T., Kobatake,N.,
            Inagaki,H., Ikema,Y., Okamoto,S., Okitani,R., Kawakami,T.,
            Noguchi,S., Itoh,T., Shigeta,K., Senba,T., Matsumura,K.,
            Nakajima,Y., Mizuno,T., Morinaga,M., Sasaki,M., Togashi,T.,
            Oyama,M., Hata,H., Watanabe,M., Komatsu,T., Mizushima-Sugano,J.,
            Satoh,T., Shirai,Y., Takahashi,Y., Nakagawa,K., Okumura,K.,
            Nagase,T., Nomura,N., Kikuchi,H., Masuho,Y., Yamashita,R.,
            Nakai,K., Yada,T., Nakamura,Y., Ohara,O., Isogai,T. and Sugano,S.
  TITLE     Complete sequencing and characterization of 21,243 full-length
            human cDNAs
  JOURNAL   Nat Genet 36 (1), 40-45 (2004)
   PUBMED   14702039
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6), AND
            VARIANT MET-404.;
            TISSUE=Synovium
REFERENCE   6  (residues 1 to 520)
  CONSRTM   NIEHS SNPs program
  TITLE     Direct Submission
  JOURNAL   Submitted (??-OCT-2005) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-17; GLU-112;
            ILE-241; SER-349 AND MET-404.
REFERENCE   7  (residues 1 to 520)
  AUTHORS   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., Clamp,M.E., Bethel,G., Milne,S., Ainscough,R.,
            Almeida,J.P., Ambrose,K.D., Andrews,T.D., Ashwell,R.I.,
            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., 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.,
            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.,
            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., 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., Hubbard,T., Sulston,J.E.,
            Dunham,I., Rogers,J. and Beck,S.
  TITLE     The DNA sequence and analysis of human chromosome 6
  JOURNAL   Nature 425 (6960), 805-811 (2003)
   PUBMED   14574404
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   8  (residues 1 to 520)
  AUTHORS   Mural,R.J., Istrail,S., Sutton,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. and Venter,J.C.
  TITLE     Direct Submission
  JOURNAL   Submitted (??-SEP-2005) to the EMBL/GenBank/DDBJ databases
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
REFERENCE   9  (residues 1 to 520)
  AUTHORS   Gerhard,D.S., Wagner,L., Feingold,E.A., Shenmen,C.M., Grouse,L.H.,
            Schuler,G., Klein,S.L., Old,S., Rasooly,R., Good,P., Guyer,M.,
            Peck,A.M., Derge,J.G., Lipman,D., Collins,F.S., Jang,W., Sherry,S.,
            Feolo,M., Misquitta,L., Lee,E., Rotmistrovsky,K., Greenhut,S.F.,
            Schaefer,C.F., Buetow,K., Bonner,T.I., Haussler,D., Kent,J.,
            Kiekhaus,M., Furey,T., Brent,M., Prange,C., Schreiber,K.,
            Shapiro,N., Bhat,N.K., Hopkins,R.F., Hsie,F., Driscoll,T.,
            Soares,M.B., Casavant,T.L., Scheetz,T.E., Brown-stein,M.J.,
            Usdin,T.B., Toshiyuki,S., Carninci,P., Piao,Y., Dudekula,D.B.,
            Ko,M.S., Kawakami,K., Suzuki,Y., Sugano,S., Gruber,C.E.,
            Smith,M.R., Simmons,B., Moore,T., Waterman,R., Johnson,S.L.,
            Ruan,Y., Wei,C.L., Mathavan,S., Gunaratne,P.H., Wu,J., Garcia,A.M.,
            Hulyk,S.W., Fuh,E., Yuan,Y., Sneed,A., Kowis,C., Hodgson,A.,
            Muzny,D.M., McPherson,J., Gibbs,R.A., Fahey,J., Helton,E.,
            Ketteman,M., Madan,A., Rodrigues,S., Sanchez,A., Whiting,M.,
            Madari,A., Young,A.C., Wetherby,K.D., Granite,S.J., Kwong,P.N.,
            Brinkley,C.P., Pearson,R.L., Bouffard,G.G., Blakesly,R.W.,
            Green,E.D., Dickson,M.C., Rodriguez,A.C., Grimwood,J., Schmutz,J.,
            Myers,R.M., Butterfield,Y.S., Griffith,M., Griffith,O.L.,
            Krzywinski,M.I., Liao,N., Morin,R., Palmquist,D., Petrescu,A.S.,
            Skalska,U., Smailus,D.E., Stott,J.M., Schnerch,A., Schein,J.E.,
            Jones,S.J., Holt,R.A., Baross,A., Marra,M.A., Clifton,S.,
            Makowski,K.A., Bosak,S. and Malek,J.
  CONSRTM   MGC Project Team
  TITLE     The status, quality, and expansion of the NIH full-length cDNA
            project: the Mammalian Gene Collection (MGC)
  JOURNAL   Genome Res 14 (10B), 2121-2127 (2004)
   PUBMED   15489334
  REMARK    NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
            MET-404.
            Erratum:[Genome Res. 2006 Jun;16(6):804. Morrin, Ryan [corrected to
            Morin, Ryan]]
REFERENCE   10 (residues 1 to 520)
  AUTHORS   Martin,F., Malergue,F., Pitari,G., Philippe,J.M., Philips,S.,
            Chabret,C., Granjeaud,S., Mattei,M.G., Mungall,A.J., Naquet,P. and
            Galland,F.
  TITLE     Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and
            encode isoforms of pantetheinase ectoenzymes
  JOURNAL   Immunogenetics 53 (4), 296-306 (2001)
   PUBMED   11491533
  REMARK    FUNCTION, AND CATALYTIC ACTIVITY.
REFERENCE   11 (residues 1 to 520)
  AUTHORS   Liu,T., Qian,W.J., Gritsenko,M.A., Camp,D.G. II, Monroe,M.E.,
            Moore,R.J. and Smith,R.D.
  TITLE     Human plasma N-glycoproteome analysis by immunoaffinity
            subtraction, hydrazide chemistry, and mass spectrometry
  JOURNAL   J Proteome Res 4 (6), 2070-2080 (2005)
   PUBMED   16335952
  REMARK    GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411.;
            TISSUE=Plasma
REFERENCE   12 (residues 1 to 520)
  AUTHORS   Jansen,P.A., Kamsteeg,M., Rodijk-Olthuis,D., van
            Vlijmen-Willems,I.M., de Jongh,G.J., Bergers,M., Tjabringa,G.S.,
            Zeeuwen,P.L. and Schalkwijk,J.
  TITLE     Expression of the vanin gene family in normal and inflamed human
            skin: induction by proinflammatory cytokines
  JOURNAL   J Invest Dermatol 129 (9), 2167-2174 (2009)
   PUBMED   19322213
  REMARK    TISSUE SPECIFICITY.
COMMENT     On Mar 23, 2007 this sequence version replaced gi:13431962.
            [FUNCTION] Amidohydrolase that hydrolyzes specifically one of the
            carboamide linkages in D-pantetheine thus recycling pantothenic
            acid (vitamin B5) and releasing cysteamine (PubMed:11491533).
            Involved in the thymus homing of bone marrow cells. May regulate
            beta-2 integrin-mediated cell adhesion, migration and motility of
            neutrophil. {ECO:0000269|PubMed:11491533}.
            [CATALYTIC ACTIVITY] Reaction=(R)-pantetheine + H2O = cysteamine +
            (R)-pantothenate; Xref=Rhea:RHEA:13445, ChEBI:CHEBI:15377,
            ChEBI:CHEBI:16753, ChEBI:CHEBI:29032, ChEBI:CHEBI:58029;
            EC=3.5.1.92; Evidence={ECO:0000269|PubMed:11491533};
            PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13446;
            Evidence={ECO:0000305|PubMed:11491533}.
            [INTERACTION] O95498; Q92993: KAT5; NbExp=3; IntAct=EBI-21494555,
            EBI-399080; O95498; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-21494555,
            EBI-11742507; O95498; P17252: PRKCA; NbExp=3; IntAct=EBI-21494555,
            EBI-1383528; O95498; Q15047-2: SETDB1; NbExp=3;
            IntAct=EBI-21494555, EBI-9090795; O95498; P61981: YWHAG; NbExp=3;
            IntAct=EBI-21494555, EBI-359832.
            [SUBCELLULAR LOCATION] Cell membrane {ECO:0000305}; Lipid-anchor,
            GPI-anchor {ECO:0000305}.
            [ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
            isoforms=6; Name=1; IsoId=O95498-1; Sequence=Displayed; Name=2;
            Synonyms=GPI-80 variant protein 3; IsoId=O95498-2;
            Sequence=VSP_038557; Name=3; Synonyms=GPI-80 variant protein 2;
            IsoId=O95498-3; Sequence=VSP_038558, VSP_038559; Name=4;
            Synonyms=GPI-80 variant protein 1; IsoId=O95498-4;
            Sequence=VSP_038556, VSP_038560; Name=5; Synonyms=GPI-80 variant
            protein 4; IsoId=O95498-5; Sequence=VSP_038554, VSP_038555; Name=6;
            IsoId=O95498-6; Sequence=VSP_044912.
            [TISSUE SPECIFICITY] Widely expressed with higher expression in
            spleen and blood. {ECO:0000269|PubMed:19322213}.
            [MISCELLANEOUS] [Isoform 3]: May be produced at very low levels due
            to a premature stop codon in the mRNA, leading to nonsense-mediated
            mRNA decay. {ECO:0000305}.
            [MISCELLANEOUS] [Isoform 4]: May be produced at very low levels due
            to a premature stop codon in the mRNA, leading to nonsense-mediated
            mRNA decay. {ECO:0000305}.
            [MISCELLANEOUS] [Isoform 5]: May be produced at very low levels due
            to a premature stop codon in the mRNA, leading to nonsense-mediated
            mRNA decay. {ECO:0000305}.
            [SIMILARITY] Belongs to the carbon-nitrogen hydrolase superfamily.
            BTD/VNN family. {ECO:0000305}.
FEATURES             Location/Qualifiers
     source          1..520
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
     gene            1..520
                     /gene="VNN2"
     Protein         1..520
                     /product="Pantetheine hydrolase VNN2"
                     /EC_number="3.5.1.92"
                     /note="Glycosylphosphatidyl inositol-anchored protein
                     GPI-80; Protein FOAP-4; Vascular non-inflammatory molecule
                     2; Vanin-2"
                     /UniProtKB_evidence="Evidence at protein level"
     Region          1..53
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 6).
                     /evidence=ECO:0000303|PubMed:14702039. /id=VSP_044912."
     Region          1..22
                     /region_name="Signal"
                     /note="/evidence=ECO:0000255."
     Region          17
                     /region_name="Variant"
                     /note="T -> N (in dbSNP:rs33950336).
                     /evidence=ECO:0000269|Ref.6. /id=VAR_025177."
     Region          23..493
                     /region_name="Mature chain"
                     /note="Pantetheine hydrolase VNN2. /id=PRO_0000019718."
     Region          26..329
                     /region_name="biotinidase_like"
                     /note="biotinidase and vanins (class 4 nitrilases);
                     cd07567"
                     /db_xref="CDD:143591"
     Region          30
                     /region_name="Variant"
                     /note="V -> A (in dbSNP:rs2294760). /id=VAR_031261."
     Region          31..306
                     /region_name="Domain"
                     /note="CN hydrolase.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00054."
     Site            39
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            order(80,179,183,185,211..212,214..215,237)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:143591"
     Site            order(80,179,211)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:143591"
     Site            80
                     /site_type="active"
                     /note="Proton acceptor.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00054."
     Region          112
                     /region_name="Variant"
                     /note="D -> E (in dbSNP:rs35993077).
                     /evidence=ECO:0000269|Ref.6. /id=VAR_025178."
     Region          116..119
                     /region_name="Splicing variant"
                     /note="FGHT -> SAQC (in isoform 5).
                     /evidence=ECO:0000303|PubMed:18805469. /id=VSP_038554."
     Region          120..520
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 5).
                     /evidence=ECO:0000303|PubMed:18805469. /id=VSP_038555."
     Site            179
                     /site_type="active"
                     /note="Proton donor.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00054."
     Region          180..400
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 2).
                     /evidence=ECO:0000303|PubMed:18805469. /id=VSP_038557."
     Site            order(180..184,191..193,212,214..218,221..222,243..244,
                     246..248,250..251,275..276,325..329)
                     /site_type="other"
                     /note="putative dimer interface [polypeptide binding]"
                     /db_xref="CDD:143591"
     Region          180..195
                     /region_name="Splicing variant"
                     /note="YHLYSEPQFNVPEKPE -> EVVFMHQMVPKCIIMT (in isoform
                     4). /evidence=ECO:0000303|PubMed:18805469.
                     /id=VSP_038556."
     Region          180..192
                     /region_name="Splicing variant"
                     /note="YHLYSEPQFNVPE -> ETLQSVKRSFAVI (in isoform 3).
                     /evidence=ECO:0000303|PubMed:18805469. /id=VSP_038558."
     Region          193..520
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 3).
                     /evidence=ECO:0000303|PubMed:18805469. /id=VSP_038559."
     Region          196..520
                     /region_name="Splicing variant"
                     /note="Missing (in isoform 4).
                     /evidence=ECO:0000303|PubMed:18805469. /id=VSP_038560."
     Site            211
                     /site_type="active"
                     /note="Nucleophile.
                     /evidence=ECO:0000255|PROSITE-ProRule:PRU00054."
     Region          218
                     /region_name="Conflict"
                     /note="D -> Y (in Ref. 1; CAA10569).
                     /evidence=ECO:0000305."
     Region          241
                     /region_name="Variant"
                     /note="V -> I (in dbSNP:rs33920182).
                     /evidence=ECO:0000269|Ref.6. /id=VAR_025179."
     Site            273
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          344..487
                     /region_name="Vanin_C"
                     /note="Vanin C-terminal domain; pfam19018"
                     /db_xref="CDD:465946"
     Site            347
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          349
                     /region_name="Variant"
                     /note="T -> S (in dbSNP:rs36092168).
                     /evidence=ECO:0000269|Ref.6. /id=VAR_025180."
     Site            357
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Region          404
                     /region_name="Variant"
                     /note="L -> M (in dbSNP:rs4895944).
                     /evidence=ECO:0000269|PubMed:10201959,
                     ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
                     ECO:0000269|PubMed:18805469, ECO:0000269|PubMed:9790769,
                     ECO:0000269|Ref.4, ECO:0000269|Ref.6. /id=VAR_023530."
     Site            411
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000269|PubMed:16335952."
     Site            468
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255."
     Site            493
                     /site_type="lipid-binding"
                     /note="GPI-anchor amidated cysteine.
                     /evidence=ECO:0000255."
     Region          494..520
                     /region_name="Propeptide"
                     /note="Removed in mature form. /evidence=ECO:0000255.
                     /id=PRO_0000019719."
ORIGIN      
        1 mvtssfpisv avfalitlqv gtqdsfiaav yehavilpnk tetpvsqeda lnlmnenidi
       61 letaikqaae qgariivtpe dalygwkftr etvfpyledi pdpqvnwipc qdphrfghtp
      121 vqarlsclak dnsiyvlanl gdkkpcnsrd stcppngyfq yntnvvynte gklvaryhky
      181 hlysepqfnv pekpelvtfn tafgrfgift cfdiffydpg vtlvkdfhvd tilfptawmn
      241 vlplltaief hsawamgmgv nllvanthhv slnmtgsgiy apngpkvyhy dmktelgkll
      301 lsevdshpls slayptavnw nayattikpf pvqkntfrgf isrdgfnfte lfenagnltv
      361 cqkelcchls yrmlqkeene vyvlgaftgl hgrrrreywq vctllkcktt nlttcgrpve
      421 tastrfemfs lsgtfgteyv fpevllteih lspgkfevlk dgrlvnkngs sgpiltvslf
      481 grwytkdsly sscgtsnsai tyllifillm iialqnivml
//
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