ID PPGB_HUMAN Reviewed; 480 AA. AC P10619; B2R798; Q561W6; Q5JZH1; Q96KJ2; Q9BR08; Q9BW68; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2002, sequence version 2. DT 09-DEC-2015, entry version 194. DE RecName: Full=Lysosomal protective protein; DE EC=3.4.16.5; DE AltName: Full=Carboxypeptidase C; DE AltName: Full=Carboxypeptidase L; DE AltName: Full=Cathepsin A; DE AltName: Full=Protective protein cathepsin A; DE Short=PPCA; DE AltName: Full=Protective protein for beta-galactosidase; DE Contains: DE RecName: Full=Lysosomal protective protein 32 kDa chain; DE Contains: DE RecName: Full=Lysosomal protective protein 20 kDa chain; DE Flags: Precursor; GN Name=CTSA; Synonyms=PPGB; 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 PARTIAL PROTEIN SEQUENCE. RX PubMed=3136930; DOI=10.1016/S0092-8674(88)90999-3; RA Galjart N.J., Gillemans N., Harris A., van de Horst G.T.J., RA Verheijen F.W., Galjaard H., D'Azzo A.; RT "Expression of cDNA encoding the human 'protective protein' associated RT with lysosomal beta-galactosidase and neuraminidase: homology to yeast RT proteases."; RL Cell 54:755-764(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta, and Skin; 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 [5] RP PROTEIN SEQUENCE OF 29-53 AND 327-351. RC TISSUE=Platelet; RX PubMed=1694176; RA Jackman H.L., Tan F., Tamei H., Beurling-Harbury C., Li X.-Y., RA Skidgel R.A., Erdoes E.G.; RT "A peptidase in human platelets that deamidates tachykinins. Probable RT identity with the lysosomal 'protective protein'."; RL J. Biol. Chem. 265:11265-11272(1990). RN [6] RP PROTEIN SEQUENCE OF 29-37. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., RA Thomas G.R., Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass RT spectrometric identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [7] RP FUNCTION, AND MUTAGENESIS. RX PubMed=1907282; RA Galjart N.J., Morreau H., Willemsen R., Gillemans N., Bonten E.J., RA D'Azzo A.; RT "Human lysosomal protective protein has cathepsin A-like activity RT distinct from its protective function."; RL J. Biol. Chem. 266:14754-14762(1991). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145. RC TISSUE=Platelet; RX PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200; RA Lewandrowski U., Moebius J., Walter U., Sickmann A.; RT "Elucidation of N-glycosylation sites on human platelet proteins: a RT glycoproteomic approach."; RL Mol. Cell. Proteomics 5:226-233(2006). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145 AND ASN-333. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-28, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX PubMed=8591035; DOI=10.1016/S0969-2126(01)00260-X; RA Rudenko G., Bonten E., D'Azzo A., Hol W.G.J.; RT "Three-dimensional structure of the human 'protective protein': RT structure of the precursor form suggests a complex activation RT mechanism."; RL Structure 3:1249-1259(1995). RN [13] RP VARIANT GSL VAL-440. RX PubMed=1756715; RA Zhou X.Y., Galjart N.J., Willemsen R., Gillemans N., Galjaard H., RA D'Azzo A.; RT "A mutation in a mild form of galactosialidosis impairs dimerization RT of the protective protein and renders it unstable."; RL EMBO J. 10:4041-4048(1991). RN [14] RP VARIANTS GSL ARG-49; ARG-65; LEU-90; ASN-249 AND CYS-395. RX PubMed=8514852; DOI=10.1172/JCI116472; RA Shimmoto M., Fukuhara Y., Itoh K., Oshima A., Sakuraba H., Suzuki Y.; RT "Protective protein gene mutations in galactosialidosis."; RL J. Clin. Invest. 91:2393-2398(1993). RN [15] RP VARIANTS GSL TYR-51; MET-132; PRO-236; ASN-249; THR-406; SER-439 AND RP VAL-440. RX PubMed=8968752; DOI=10.1093/hmg/5.12.1977; RA Zhou X.Y., van der Spoel A., Rottier R., Hale G., Willemsen R., RA Berry G.T., Strisciuglio P., Morrone A., Zammarchi E., Andria G., RA d'Azzo A.; RT "Molecular and biochemical analysis of protective protein/cathepsin A RT mutations: correlation with clinical severity in galactosialidosis."; RL Hum. Mol. Genet. 5:1977-1987(1996). RN [16] RP VARIANT GSL GLU-453. RX PubMed=10944848; DOI=10.1007/s100380070027; RA Takiguchi K., Itoh K., Shimmoto M., Ozand P.T., Doi H., Sakuraba H.; RT "Structural and functional study of K453E mutant protective RT protein/cathepsin A causing the late infantile form of RT galactosialidosis."; RL J. Hum. Genet. 45:200-206(2000). CC -!- FUNCTION: Protective protein appears to be essential for both the CC activity of beta-galactosidase and neuraminidase, it associates CC with these enzymes and exerts a protective function necessary for CC their stability and activity. This protein is also a CC carboxypeptidase and can deamidate tachykinins. CC {ECO:0000269|PubMed:1907282}. CC -!- CATALYTIC ACTIVITY: Release of a C-terminal amino acid with broad CC specificity. {ECO:0000255|PROSITE-ProRule:PRU10074, CC ECO:0000255|PROSITE-ProRule:PRU10075}. CC -!- SUBUNIT: Heterodimer of a 32 kDa chain and a 20 kDa chain; CC disulfide-linked. CC -!- SUBCELLULAR LOCATION: Lysosome. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P10619-1; Sequence=Displayed; CC Name=2; CC IsoId=P10619-2; Sequence=VSP_054832; CC Note=Gene prediction based on EST data.; CC -!- DISEASE: Galactosialidosis (GSL) [MIM:256540]: A lysosomal storage CC disease associated with a combined deficiency of beta- CC galactosidase and neuraminidase, secondary to a defect in CC cathepsin A. All patients have clinical manifestations typical of CC a lysosomal disorder, such as coarse facies, cherry red spots, CC vertebral changes, foam cells in the bone marrow, and vacuolated CC lymphocytes. Three phenotypic subtypes are recognized. The early CC infantile form is associated with fetal hydrops, edema, ascites, CC visceromegaly, skeletal dysplasia, and early death. The late CC infantile type is characterized by hepatosplenomegaly, growth CC retardation, cardiac involvement, and a normal or mildly affected CC mental state. The juvenile/adult form is characterized by CC myoclonus, ataxia, angiokeratoma, mental retardation, neurologic CC deterioration, absence of visceromegaly, and long survival. CC {ECO:0000269|PubMed:10944848, ECO:0000269|PubMed:1756715, CC ECO:0000269|PubMed:8514852, ECO:0000269|PubMed:8968752}. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAI20248.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; M22960; AAA36476.1; -; mRNA. DR EMBL; AK312898; BAG35745.1; -; mRNA. DR EMBL; AL008726; CAA15501.1; -; Genomic_DNA. DR EMBL; AL008726; CAI20248.1; ALT_INIT; Genomic_DNA. DR EMBL; BC000597; AAH00597.1; -; mRNA. DR EMBL; BC093009; AAH93009.1; -; mRNA. DR CCDS; CCDS46609.1; -. [P10619-1] DR PIR; A31589; A31589. DR RefSeq; NP_000299.2; NM_000308.2. DR RefSeq; NP_001121167.1; NM_001127695.1. [P10619-1] DR RefSeq; NP_001161066.1; NM_001167594.1. DR UniGene; Hs.609336; -. DR PDB; 1IVY; X-ray; 2.20 A; A/B=29-480. DR PDB; 3BP4; X-ray; 1.85 A; C=2-10. DR PDB; 3BP7; X-ray; 1.80 A; C=2-10. DR PDB; 3BXN; X-ray; 1.86 A; C=2-10. DR PDB; 4AZ0; X-ray; 2.17 A; A=29-326, B=327-480. DR PDB; 4AZ3; X-ray; 2.04 A; A=29-326, B=327-480. DR PDB; 4CI9; X-ray; 1.58 A; A=29-480. DR PDB; 4CIA; X-ray; 1.98 A; A=29-480. DR PDB; 4CIB; X-ray; 1.89 A; A=29-480. DR PDB; 4MWS; X-ray; 2.80 A; A/B=29-480. DR PDB; 4MWT; X-ray; 3.85 A; A/B=29-480. DR PDBsum; 1IVY; -. DR PDBsum; 3BP4; -. DR PDBsum; 3BP7; -. DR PDBsum; 3BXN; -. DR PDBsum; 4AZ0; -. DR PDBsum; 4AZ3; -. DR PDBsum; 4CI9; -. DR PDBsum; 4CIA; -. DR PDBsum; 4CIB; -. DR PDBsum; 4MWS; -. DR PDBsum; 4MWT; -. DR ProteinModelPortal; P10619; -. DR SMR; P10619; 29-480. DR BioGrid; 111472; 31. DR IntAct; P10619; 10. DR MINT; MINT-3007366; -. DR STRING; 9606.ENSP00000361562; -. DR BindingDB; P10619; -. DR ChEMBL; CHEMBL6115; -. DR GuidetoPHARMACOLOGY; 1581; -. DR ESTHER; human-CTSA; Carboxypeptidase_S10. DR MEROPS; S10.002; -. DR PhosphoSite; P10619; -. DR BioMuta; CTSA; -. DR DMDM; 20178316; -. DR OGP; P10619; -. DR MaxQB; P10619; -. DR PaxDb; P10619; -. DR PRIDE; P10619; -. DR DNASU; 5476; -. DR Ensembl; ENST00000191018; ENSP00000191018; ENSG00000064601. [P10619-1] DR Ensembl; ENST00000372459; ENSP00000361537; ENSG00000064601. [P10619-1] DR GeneID; 5476; -. DR KEGG; hsa:5476; -. DR UCSC; uc002xqh.3; human. [P10619-1] DR CTD; 5476; -. DR GeneCards; CTSA; -. DR HGNC; HGNC:9251; CTSA. DR HPA; CAB024930; -. DR HPA; HPA031068; -. DR MalaCards; CTSA; -. DR MIM; 256540; phenotype. DR MIM; 613111; gene. DR neXtProt; NX_P10619; -. DR Orphanet; 351; Galactosialidosis. DR PharmGKB; PA33572; -. DR eggNOG; KOG1282; Eukaryota. DR eggNOG; COG2939; LUCA. DR GeneTree; ENSGT00790000123075; -. DR HOVERGEN; HBG053652; -. DR InParanoid; P10619; -. DR KO; K13289; -. DR OrthoDB; EOG7KQ21H; -. DR PhylomeDB; P10619; -. DR TreeFam; TF323769; -. DR BRENDA; 3.4.16.5; 2681. DR Reactome; R-HSA-1660662; Glycosphingolipid metabolism. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-4085001; Sialic acid metabolism. DR SABIO-RK; P10619; -. DR SignaLink; P10619; -. DR ChiTaRS; CTSA; human. DR EvolutionaryTrace; P10619; -. DR GeneWiki; Cathepsin_A; -. DR GenomeRNAi; 5476; -. DR NextBio; 21202; -. DR PRO; PR:P10619; -. DR Proteomes; UP000005640; Chromosome 20. DR Bgee; P10619; -. DR CleanEx; HS_CTSA; -. DR ExpressionAtlas; P10619; baseline and differential. DR Genevisible; P10619; HS. DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome. DR GO; GO:0005764; C:lysosome; NAS:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0004180; F:carboxypeptidase activity; TAS:ProtInc. DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc. DR GO; GO:0004185; F:serine-type carboxypeptidase activity; IMP:ParkinsonsUK-UCL. DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome. DR GO; GO:0061684; P:chaperone-mediated autophagy; IGI:ParkinsonsUK-UCL. DR GO; GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; TAS:Reactome. DR GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome. DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc. DR GO; GO:0043085; P:positive regulation of catalytic activity; TAS:GOC. DR GO; GO:0043687; P:post-translational protein modification; TAS:Reactome. DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome. DR GO; GO:0006508; P:proteolysis; IDA:ParkinsonsUK-UCL. DR GO; GO:1904714; P:regulation of chaperone-mediated autophagy; TAS:ParkinsonsUK-UCL. DR GO; GO:0031647; P:regulation of protein stability; IMP:ParkinsonsUK-UCL. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0006665; P:sphingolipid metabolic process; TAS:Reactome. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR001563; Peptidase_S10. DR InterPro; IPR018202; Peptidase_S10_AS. DR PANTHER; PTHR11802; PTHR11802; 2. DR Pfam; PF00450; Peptidase_S10; 1. DR PRINTS; PR00724; CRBOXYPTASEC. DR SUPFAM; SSF53474; SSF53474; 1. DR PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1. DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Carboxypeptidase; KW Complete proteome; Direct protein sequencing; Disease mutation; KW Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease; KW Reference proteome; Signal; Zymogen. FT SIGNAL 1 28 {ECO:0000244|PubMed:25944712, FT ECO:0000269|PubMed:12665801, FT ECO:0000269|PubMed:1694176}. FT CHAIN 29 480 Lysosomal protective protein. FT /FTId=PRO_0000004274. FT CHAIN 29 326 Lysosomal protective protein 32 kDa FT chain. FT /FTId=PRO_0000004275. FT CHAIN 327 480 Lysosomal protective protein 20 kDa FT chain. FT /FTId=PRO_0000004276. FT ACT_SITE 178 178 FT ACT_SITE 400 400 {ECO:0000250}. FT ACT_SITE 457 457 FT CARBOHYD 145 145 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16263699, FT ECO:0000269|PubMed:19159218}. FT CARBOHYD 333 333 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:19159218}. FT DISULFID 88 362 FT DISULFID 240 256 FT DISULFID 241 246 FT DISULFID 281 331 FT VAR_SEQ 102 118 Missing (in isoform 2). {ECO:0000305}. FT /FTId=VSP_054832. FT VARIANT 49 49 Q -> R (in GSL). FT {ECO:0000269|PubMed:8514852}. FT /FTId=VAR_001385. FT VARIANT 51 51 S -> Y (in GSL). FT {ECO:0000269|PubMed:8968752}. FT /FTId=VAR_063018. FT VARIANT 65 65 W -> R (in GSL; dbSNP:rs28934603). FT {ECO:0000269|PubMed:8514852}. FT /FTId=VAR_001386. FT VARIANT 90 90 S -> L (in GSL). FT {ECO:0000269|PubMed:8514852}. FT /FTId=VAR_001387. FT VARIANT 132 132 V -> M (in GSL). FT {ECO:0000269|PubMed:8968752}. FT /FTId=VAR_063019. FT VARIANT 236 236 L -> P (in GSL). FT {ECO:0000269|PubMed:8968752}. FT /FTId=VAR_063020. FT VARIANT 249 249 Y -> N (in GSL; small amount of FT activity). {ECO:0000269|PubMed:8514852, FT ECO:0000269|PubMed:8968752}. FT /FTId=VAR_001388. FT VARIANT 395 395 Y -> C (in GSL; loss of activity). FT {ECO:0000269|PubMed:8514852}. FT /FTId=VAR_001389. FT VARIANT 406 406 M -> T (in GSL). FT {ECO:0000269|PubMed:8968752}. FT /FTId=VAR_063021. FT VARIANT 439 439 G -> S (in GSL). FT {ECO:0000269|PubMed:8968752}. FT /FTId=VAR_063022. FT VARIANT 440 440 F -> V (in GSL). FT {ECO:0000269|PubMed:1756715, FT ECO:0000269|PubMed:8968752}. FT /FTId=VAR_001390. FT VARIANT 453 453 K -> E (in GSL). FT {ECO:0000269|PubMed:10944848}. FT /FTId=VAR_063023. FT MUTAGEN 178 178 S->A: Inactivates the enzyme. FT {ECO:0000269|PubMed:1907282}. FT MUTAGEN 457 457 H->Q: Inactivates the enzyme. FT {ECO:0000269|PubMed:1907282}. FT CONFLICT 19 19 Missing (in Ref. 4; AAH00597). FT {ECO:0000305}. FT CONFLICT 56 56 G -> S (in Ref. 1; AAA36476). FT {ECO:0000305}. FT HELIX 31 33 {ECO:0000244|PDB:4CI9}. FT STRAND 41 43 {ECO:0000244|PDB:4CIA}. FT STRAND 49 55 {ECO:0000244|PDB:4CI9}. FT STRAND 60 67 {ECO:0000244|PDB:4CI9}. FT TURN 73 75 {ECO:0000244|PDB:4CI9}. FT STRAND 78 82 {ECO:0000244|PDB:4CI9}. FT TURN 85 87 {ECO:0000244|PDB:4CI9}. FT HELIX 91 96 {ECO:0000244|PDB:4CI9}. FT STRAND 99 103 {ECO:0000244|PDB:4CI9}. FT STRAND 110 112 {ECO:0000244|PDB:4CI9}. FT HELIX 117 119 {ECO:0000244|PDB:4CI9}. FT STRAND 120 126 {ECO:0000244|PDB:4CI9}. FT STRAND 136 139 {ECO:0000244|PDB:1IVY}. FT HELIX 146 163 {ECO:0000244|PDB:4CI9}. FT HELIX 165 167 {ECO:0000244|PDB:4CI9}. FT STRAND 168 170 {ECO:0000244|PDB:4MWS}. FT STRAND 172 177 {ECO:0000244|PDB:4CI9}. FT HELIX 180 192 {ECO:0000244|PDB:4CI9}. FT STRAND 199 206 {ECO:0000244|PDB:4CI9}. FT HELIX 211 224 {ECO:0000244|PDB:4CI9}. FT HELIX 230 240 {ECO:0000244|PDB:4CI9}. FT HELIX 254 268 {ECO:0000244|PDB:4CI9}. FT STRAND 269 271 {ECO:0000244|PDB:4CI9}. FT STRAND 286 292 {ECO:0000244|PDB:1IVY}. FT STRAND 295 298 {ECO:0000244|PDB:1IVY}. FT HELIX 315 317 {ECO:0000244|PDB:1IVY}. FT HELIX 318 321 {ECO:0000244|PDB:1IVY}. FT STRAND 324 327 {ECO:0000244|PDB:1IVY}. FT HELIX 335 341 {ECO:0000244|PDB:4CI9}. FT HELIX 344 349 {ECO:0000244|PDB:4CI9}. FT HELIX 364 369 {ECO:0000244|PDB:4CI9}. FT STRAND 375 377 {ECO:0000244|PDB:4CI9}. FT HELIX 378 386 {ECO:0000244|PDB:4CI9}. FT STRAND 391 397 {ECO:0000244|PDB:4CI9}. FT STRAND 401 403 {ECO:0000244|PDB:4CI9}. FT HELIX 405 414 {ECO:0000244|PDB:4CI9}. FT STRAND 424 429 {ECO:0000244|PDB:4CI9}. FT HELIX 431 433 {ECO:0000244|PDB:4CI9}. FT STRAND 435 444 {ECO:0000244|PDB:4CI9}. FT STRAND 447 452 {ECO:0000244|PDB:4CI9}. FT HELIX 459 462 {ECO:0000244|PDB:4CI9}. FT HELIX 464 475 {ECO:0000244|PDB:4CI9}. SQ SEQUENCE 480 AA; 54466 MW; 46B737DEE775C508 CRC64; MIRAAPPPLF LLLLLLLLLV SWASRGEAAP DQDEIQRLPG LAKQPSFRQY SGYLKGSGSK HLHYWFVESQ KDPENSPVVL WLNGGPGCSS LDGLLTEHGP FLVQPDGVTL EYNPYSWNLI ANVLYLESPA GVGFSYSDDK FYATNDTEVA QSNFEALQDF FRLFPEYKNN KLFLTGESYA GIYIPTLAVL VMQDPSMNLQ GLAVGNGLSS YEQNDNSLVY FAYYHGLLGN RLWSSLQTHC CSQNKCNFYD NKDLECVTNL QEVARIVGNS GLNIYNLYAP CAGGVPSHFR YEKDTVVVQD LGNIFTRLPL KRMWHQALLR SGDKVRMDPP CTNTTAASTY LNNPYVRKAL NIPEQLPQWD MCNFLVNLQY RRLYRSMNSQ YLKLLSSQKY QILLYNGDVD MACNFMGDEW FVDSLNQKME VQRRPWLVKY GDSGEQIAGF VKEFSHIAFL TIKGAGHMVP TDKPLAAFTM FSRFLNKQPY //