ID VNN2_HUMAN Reviewed; 520 AA. AC O95498; A0AUZ3; A6NDY1; A8K4E3; A8K7W0; B2DFZ0; B2DFZ1; B2DFZ2; AC B2DFZ3; F6XL73; Q2XUN1; Q9UJF3; Q9UMW2; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 3. DT 13-FEB-2019, entry version 162. DE RecName: Full=Vascular non-inflammatory molecule 2; DE Short=Vanin-2; DE EC=3.5.1.92; DE AltName: Full=Glycosylphosphatidyl inositol-anchored protein GPI-80; DE AltName: Full=Protein FOAP-4; DE Flags: Precursor; GN Name=VNN2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT of 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., RA 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 RP 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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; RP ILE-241; 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., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA 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., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RP 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP FUNCTION. RX PubMed=11491533; DOI=10.1007/s002510100327; RA Martin F., Malergue F., Pitari G., Philippe J.M., Philips S., RA Chabret C., Granjeaud S., Mattei M.G., Mungall A.J., Naquet P., RA 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., RA Moore R.J., 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., RA Tjabringa G.S., Zeeuwen P.L.J.M., Schalkwijk J.; RT "Expression of the vanin gene family in normal and inflamed human RT skin: 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 CC acid (vitamin B5) and releasing cysteamine. Involved in the thymus CC homing of bone marrow cells. May regulate beta-2 integrin-mediated CC 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, CC GPI-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 Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC Name=4; Synonyms=GPI-80 variant protein 1; CC IsoId=O95498-4; Sequence=VSP_038556, VSP_038560; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC Name=5; Synonyms=GPI-80 variant protein 4; CC IsoId=O95498-5; Sequence=VSP_038554, VSP_038555; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC Name=6; CC IsoId=O95498-6; Sequence=VSP_044912; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in CC spleen and blood. {ECO:0000269|PubMed:19322213}. 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/"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- 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. DR RefSeq; NP_004656.2; NM_004665.4. DR RefSeq; NP_511043.1; NM_078488.2. DR RefSeq; XP_006715656.1; XM_006715593.3. [O95498-6] DR RefSeq; XP_016866896.1; XM_017011407.1. DR UniGene; Hs.293130; -. DR ProteinModelPortal; O95498; -. DR SMR; O95498; -. DR BioGrid; 114394; 45. DR IntAct; O95498; 1. DR STRING; 9606.ENSP00000322276; -. DR iPTMnet; O95498; -. DR PhosphoSitePlus; O95498; -. DR SwissPalm; O95498; -. DR BioMuta; VNN2; -. DR jPOST; O95498; -. DR PaxDb; O95498; -. DR PeptideAtlas; O95498; -. DR PRIDE; O95498; -. DR ProteomicsDB; 50925; -. DR ProteomicsDB; 50926; -. [O95498-2] DR ProteomicsDB; 50927; -. [O95498-3] DR ProteomicsDB; 50928; -. [O95498-4] DR ProteomicsDB; 50929; -. [O95498-5] DR DNASU; 8875; -. DR Ensembl; ENST00000326499; ENSP00000322276; ENSG00000112303. [O95498-1] DR Ensembl; ENST00000525270; ENSP00000436822; ENSG00000112303. [O95498-6] DR Ensembl; ENST00000525289; ENSP00000436935; ENSG00000112303. [O95498-2] DR Ensembl; ENST00000525674; ENSP00000436863; ENSG00000112303. [O95498-4] DR Ensembl; ENST00000532053; ENSP00000434077; ENSG00000112303. [O95498-3] DR GeneID; 8875; -. DR KEGG; hsa:8875; -. DR UCSC; uc003qdt.4; human. [O95498-1] DR CTD; 8875; -. DR DisGeNET; 8875; -. DR EuPathDB; HostDB:ENSG00000112303.13; -. DR GeneCards; VNN2; -. DR HGNC; HGNC:12706; VNN2. DR MIM; 603571; gene. DR neXtProt; NX_O95498; -. DR OpenTargets; ENSG00000112303; -. DR PharmGKB; PA37322; -. DR eggNOG; KOG0806; Eukaryota. DR eggNOG; COG0388; LUCA. DR GeneTree; ENSGT00390000013823; -. DR HOVERGEN; HBG003996; -. DR InParanoid; O95498; -. DR KO; K08069; -. DR OMA; EYWQVCT; -. DR OrthoDB; 1276751at2759; -. DR PhylomeDB; O95498; -. DR TreeFam; TF323645; -. DR BRENDA; 3.5.1.92; 2681. DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins. DR Reactome; R-HSA-199220; Vitamin B5 (pantothenate) metabolism. DR GeneWiki; VNN2; -. DR GenomeRNAi; 8875; -. DR PRO; PR:O95498; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000112303; Expressed in 127 organ(s), highest expression level in blood. 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 PANTHER; PTHR10609; PTHR10609; 1. DR Pfam; PF00795; CN_hydrolase; 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; Complete proteome; Glycoprotein; KW GPI-anchor; Hydrolase; Lipoprotein; Membrane; Polymorphism; KW Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 493 Vascular non-inflammatory molecule 2. FT /FTId=PRO_0000019718. FT PROPEP 494 520 Removed in mature form. {ECO:0000255}. FT /FTId=PRO_0000019719. FT DOMAIN 31 306 CN hydrolase. {ECO:0000255|PROSITE- FT ProRule:PRU00054}. FT COMPBIAS 393 396 Poly-Arg. FT ACT_SITE 80 80 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00054}. FT ACT_SITE 179 179 Proton donor. {ECO:0000255|PROSITE- FT ProRule:PRU00054}. FT ACT_SITE 211 211 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU00054}. FT LIPID 493 493 GPI-anchor amidated cysteine. FT {ECO:0000255}. FT CARBOHYD 39 39 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 273 273 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 347 347 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 357 357 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 411 411 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952}. FT CARBOHYD 468 468 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT VAR_SEQ 1 53 Missing (in isoform 6). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_044912. FT VAR_SEQ 116 119 FGHT -> SAQC (in isoform 5). FT {ECO:0000303|PubMed:18805469}. FT /FTId=VSP_038554. FT VAR_SEQ 120 520 Missing (in isoform 5). FT {ECO:0000303|PubMed:18805469}. FT /FTId=VSP_038555. FT VAR_SEQ 180 400 Missing (in isoform 2). FT {ECO:0000303|PubMed:18805469}. FT /FTId=VSP_038557. FT VAR_SEQ 180 195 YHLYSEPQFNVPEKPE -> EVVFMHQMVPKCIIMT (in FT isoform 4). FT {ECO:0000303|PubMed:18805469}. FT /FTId=VSP_038556. FT VAR_SEQ 180 192 YHLYSEPQFNVPE -> ETLQSVKRSFAVI (in FT isoform 3). FT {ECO:0000303|PubMed:18805469}. FT /FTId=VSP_038558. FT VAR_SEQ 193 520 Missing (in isoform 3). FT {ECO:0000303|PubMed:18805469}. FT /FTId=VSP_038559. FT VAR_SEQ 196 520 Missing (in isoform 4). FT {ECO:0000303|PubMed:18805469}. FT /FTId=VSP_038560. FT VARIANT 17 17 T -> N (in dbSNP:rs33950336). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_025177. FT VARIANT 30 30 V -> A (in dbSNP:rs2294760). FT /FTId=VAR_031261. FT VARIANT 112 112 D -> E (in dbSNP:rs35993077). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_025178. FT VARIANT 241 241 V -> I (in dbSNP:rs33920182). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_025179. FT VARIANT 349 349 T -> S (in dbSNP:rs36092168). FT {ECO:0000269|Ref.6}. FT /FTId=VAR_025180. FT VARIANT 404 404 L -> M (in dbSNP:rs4895944). FT {ECO:0000269|PubMed:10201959, FT ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:18805469, FT ECO:0000269|PubMed:9790769, FT ECO:0000269|Ref.4, ECO:0000269|Ref.6}. FT /FTId=VAR_023530. FT CONFLICT 218 218 D -> Y (in Ref. 1; CAA10569). FT {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 //