VNN2_HUMAN
ID VNN2_HUMAN Reviewed; 520 AA.
AC O95498; A0AUZ3; A6NDY1; A8K4E3; A8K7W0; B2DFZ0; B2DFZ1; B2DFZ2; B2DFZ3;
AC F6XL73; Q2XUN1; Q9UJF3; Q9UMW2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Pantetheine hydrolase VNN2 {ECO:0000305};
DE EC=3.5.1.92 {ECO:0000269|PubMed:11491533};
DE AltName: Full=Glycosylphosphatidyl inositol-anchored protein GPI-80;
DE AltName: Full=Protein FOAP-4;
DE AltName: Full=Vascular non-inflammatory molecule 2 {ECO:0000305};
DE Short=Vanin-2;
DE Flags: Precursor;
GN Name=VNN2 {ECO:0000312|HGNC:HGNC:12706};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-404.
RC TISSUE=Kidney;
RX PubMed=9790769; DOI=10.1006/geno.1998.5481;
RA Galland F., Malergue F., Bazin H., Mattei M.-G., Aurrand-Lions M.,
RA Theillet C., Naquet P.;
RT "Two human genes related to murine vanin-1 are located on the long arm of
RT human chromosome 6.";
RL Genomics 53:203-213(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-404.
RC TISSUE=Peripheral blood;
RX PubMed=10201959;
RA Suzuki K., Watanabe T., Sakurai S., Ohtake K., Kinoshita T., Araki A.,
RA Fujita T., Takei H., Takeda Y., Sato Y., Yamashita T., Araki Y., Sendo F.;
RT "A novel glycosylphosphatidyl inositol-anchored protein on human
RT leukocytes: a possible role for regulation of neutrophil adherence and
RT migration.";
RL J. Immunol. 162:4277-4284(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), AND VARIANT MET-404.
RC TISSUE=Neutrophil;
RX PubMed=18805469; DOI=10.1016/j.gene.2008.08.019;
RA Nitto T., Inoue T., Node K.;
RT "Alternative spliced variants in the pantetheinase family of genes
RT expressed in human neutrophils.";
RL Gene 426:57-64(2008).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MET-404.
RC TISSUE=Blood;
RA Takayama K., Fujii Y., Tsuritani K., Yajima Y., Amemiya T., Ukai Y.,
RA Naito K., Kawaguchi A.;
RT "Homo sapiens mRNA for FOAP-4 protein, complete cds.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6), AND VARIANT
RP MET-404.
RC TISSUE=Synovium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-17; GLU-112; ILE-241;
RP SER-349 AND MET-404.
RG NIEHS SNPs program;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-404.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=19322213; DOI=10.1038/jid.2009.67;
RA Jansen P.A.M., Kamsteeg M., Rodijk-Olthuis D.,
RA van Vlijmen-Willems I.M.J.J., de Jongh G.J., Bergers M., Tjabringa G.S.,
RA Zeeuwen P.L.J.M., Schalkwijk J.;
RT "Expression of the vanin gene family in normal and inflamed human skin:
RT induction by proinflammatory cytokines.";
RL J. Invest. Dermatol. 129:2167-2174(2009).
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 (PubMed:11491533). Involved in
CC the thymus homing of bone marrow cells. May regulate beta-2 integrin-
CC mediated cell adhesion, migration and motility of neutrophil.
CC {ECO:0000269|PubMed:11491533}.
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:11491533};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13446;
CC Evidence={ECO:0000305|PubMed:11491533};
CC -!- INTERACTION:
CC O95498; Q92993: KAT5; NbExp=3; IntAct=EBI-21494555, EBI-399080;
CC O95498; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-21494555, EBI-11742507;
CC O95498; P17252: PRKCA; NbExp=3; IntAct=EBI-21494555, EBI-1383528;
CC O95498; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-21494555, EBI-9090795;
CC O95498; P61981: YWHAG; NbExp=3; IntAct=EBI-21494555, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=O95498-1; Sequence=Displayed;
CC Name=2; Synonyms=GPI-80 variant protein 3;
CC IsoId=O95498-2; Sequence=VSP_038557;
CC Name=3; Synonyms=GPI-80 variant protein 2;
CC IsoId=O95498-3; Sequence=VSP_038558, VSP_038559;
CC Name=4; Synonyms=GPI-80 variant protein 1;
CC IsoId=O95498-4; Sequence=VSP_038556, VSP_038560;
CC Name=5; Synonyms=GPI-80 variant protein 4;
CC IsoId=O95498-5; Sequence=VSP_038554, VSP_038555;
CC Name=6;
CC IsoId=O95498-6; Sequence=VSP_044912;
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in spleen
CC and blood. {ECO:0000269|PubMed:19322213}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC BTD/VNN family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/vnn2/";
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DR EMBL; AJ132100; CAA10569.1; -; mRNA.
DR EMBL; D89974; BAA82525.1; -; mRNA.
DR EMBL; AB435062; BAG30934.1; -; mRNA.
DR EMBL; AB435063; BAG30935.1; -; mRNA.
DR EMBL; AB435064; BAG30936.1; -; mRNA.
DR EMBL; AB435065; BAG30937.1; -; mRNA.
DR EMBL; AB026705; BAB61019.1; -; mRNA.
DR EMBL; AK290908; BAF83597.1; -; mRNA.
DR EMBL; AK292125; BAF84814.1; -; mRNA.
DR EMBL; DQ249347; ABB72673.1; -; Genomic_DNA.
DR EMBL; AL032821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48016.1; -; Genomic_DNA.
DR EMBL; BC126145; AAI26146.1; -; mRNA.
DR EMBL; BC126147; AAI26148.1; -; mRNA.
DR CCDS; CCDS5161.1; -. [O95498-1]
DR CCDS; CCDS5162.1; -. [O95498-6]
DR CCDS; CCDS56451.1; -. [O95498-2]
DR RefSeq; NP_001229279.1; NM_001242350.2. [O95498-2]
DR RefSeq; NP_004656.2; NM_004665.4. [O95498-1]
DR RefSeq; NP_511043.1; NM_078488.2. [O95498-6]
DR RefSeq; XP_006715656.1; XM_006715593.3. [O95498-6]
DR RefSeq; XP_016866896.1; XM_017011407.1.
DR AlphaFoldDB; O95498; -.
DR SMR; O95498; -.
DR BioGRID; 114394; 52.
DR IntAct; O95498; 44.
DR STRING; 9606.ENSP00000322276; -.
DR GlyConnect; 2089; 1 N-Linked glycan (1 site).
DR GlyGen; O95498; 7 sites, 2 N-linked glycans (1 site).
DR iPTMnet; O95498; -.
DR PhosphoSitePlus; O95498; -.
DR SwissPalm; O95498; -.
DR BioMuta; VNN2; -.
DR jPOST; O95498; -.
DR MassIVE; O95498; -.
DR PaxDb; O95498; -.
DR PeptideAtlas; O95498; -.
DR PRIDE; O95498; -.
DR ProteomicsDB; 28159; -.
DR ProteomicsDB; 50925; -. [O95498-1]
DR ProteomicsDB; 50926; -. [O95498-2]
DR ProteomicsDB; 50927; -. [O95498-3]
DR ProteomicsDB; 50928; -. [O95498-4]
DR ProteomicsDB; 50929; -. [O95498-5]
DR Antibodypedia; 32943; 141 antibodies from 24 providers.
DR DNASU; 8875; -.
DR Ensembl; ENST00000326499.11; ENSP00000322276.6; ENSG00000112303.14. [O95498-1]
DR Ensembl; ENST00000525270.5; ENSP00000436822.1; ENSG00000112303.14. [O95498-6]
DR Ensembl; ENST00000525289.5; ENSP00000436935.1; ENSG00000112303.14. [O95498-2]
DR Ensembl; ENST00000525674.5; ENSP00000436863.1; ENSG00000112303.14. [O95498-4]
DR Ensembl; ENST00000532053.5; ENSP00000434077.1; ENSG00000112303.14. [O95498-3]
DR GeneID; 8875; -.
DR KEGG; hsa:8875; -.
DR MANE-Select; ENST00000326499.11; ENSP00000322276.6; NM_004665.6; NP_004656.3.
DR UCSC; uc003qdt.4; human. [O95498-1]
DR CTD; 8875; -.
DR DisGeNET; 8875; -.
DR GeneCards; VNN2; -.
DR HGNC; HGNC:12706; VNN2.
DR HPA; ENSG00000112303; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 603571; gene.
DR neXtProt; NX_O95498; -.
DR OpenTargets; ENSG00000112303; -.
DR PharmGKB; PA37322; -.
DR VEuPathDB; HostDB:ENSG00000112303; -.
DR eggNOG; KOG0806; Eukaryota.
DR GeneTree; ENSGT00390000013823; -.
DR HOGENOM; CLU_033209_2_0_1; -.
DR InParanoid; O95498; -.
DR OMA; IFFYDPA; -.
DR OrthoDB; 1276751at2759; -.
DR PhylomeDB; O95498; -.
DR TreeFam; TF323645; -.
DR BRENDA; 3.5.1.92; 2681.
DR PathwayCommons; O95498; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-HSA-199220; Vitamin B5 (pantothenate) metabolism.
DR SignaLink; O95498; -.
DR BioGRID-ORCS; 8875; 39 hits in 1069 CRISPR screens.
DR GeneWiki; VNN2; -.
DR GenomeRNAi; 8875; -.
DR Pharos; O95498; Tbio.
DR PRO; PR:O95498; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O95498; protein.
DR Bgee; ENSG00000112303; Expressed in blood and 121 other tissues.
DR ExpressionAtlas; O95498; baseline and differential.
DR Genevisible; O95498; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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; -; 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 Alternative splicing; Cell membrane; Glycoprotein; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..493
FT /note="Pantetheine hydrolase VNN2"
FT /id="PRO_0000019718"
FT PROPEP 494..520
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000019719"
FT DOMAIN 31..306
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 211
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT LIPID 493
FT /note="GPI-anchor amidated cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044912"
FT VAR_SEQ 116..119
FT /note="FGHT -> SAQC (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:18805469"
FT /id="VSP_038554"
FT VAR_SEQ 120..520
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:18805469"
FT /id="VSP_038555"
FT VAR_SEQ 180..400
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18805469"
FT /id="VSP_038557"
FT VAR_SEQ 180..195
FT /note="YHLYSEPQFNVPEKPE -> EVVFMHQMVPKCIIMT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:18805469"
FT /id="VSP_038556"
FT VAR_SEQ 180..192
FT /note="YHLYSEPQFNVPE -> ETLQSVKRSFAVI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18805469"
FT /id="VSP_038558"
FT VAR_SEQ 193..520
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:18805469"
FT /id="VSP_038559"
FT VAR_SEQ 196..520
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:18805469"
FT /id="VSP_038560"
FT VARIANT 17
FT /note="T -> N (in dbSNP:rs33950336)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_025177"
FT VARIANT 30
FT /note="V -> A (in dbSNP:rs2294760)"
FT /id="VAR_031261"
FT VARIANT 112
FT /note="D -> E (in dbSNP:rs35993077)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_025178"
FT VARIANT 241
FT /note="V -> I (in dbSNP:rs33920182)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_025179"
FT VARIANT 349
FT /note="T -> S (in dbSNP:rs36092168)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_025180"
FT VARIANT 404
FT /note="L -> M (in dbSNP:rs4895944)"
FT /evidence="ECO:0000269|PubMed:10201959,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:18805469, ECO:0000269|PubMed:9790769,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.6"
FT /id="VAR_023530"
FT CONFLICT 218
FT /note="D -> Y (in Ref. 1; CAA10569)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 58503 MW; 14460E1DE5B04870 CRC64;
MVTSSFPISV AVFALITLQV GTQDSFIAAV YEHAVILPNK TETPVSQEDA LNLMNENIDI
LETAIKQAAE QGARIIVTPE DALYGWKFTR ETVFPYLEDI PDPQVNWIPC QDPHRFGHTP
VQARLSCLAK DNSIYVLANL GDKKPCNSRD STCPPNGYFQ YNTNVVYNTE GKLVARYHKY
HLYSEPQFNV PEKPELVTFN TAFGRFGIFT CFDIFFYDPG VTLVKDFHVD TILFPTAWMN
VLPLLTAIEF HSAWAMGMGV NLLVANTHHV SLNMTGSGIY APNGPKVYHY DMKTELGKLL
LSEVDSHPLS SLAYPTAVNW NAYATTIKPF PVQKNTFRGF ISRDGFNFTE LFENAGNLTV
CQKELCCHLS YRMLQKEENE VYVLGAFTGL HGRRRREYWQ VCTLLKCKTT NLTTCGRPVE
TASTRFEMFS LSGTFGTEYV FPEVLLTEIH LSPGKFEVLK DGRLVNKNGS SGPILTVSLF
GRWYTKDSLY SSCGTSNSAI TYLLIFILLM IIALQNIVML
