Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Lysosomal protective protein (EC 3.4.16.5) (Carboxypeptidase C) (Carboxypeptidase L) (Cathepsin A) (Protective protein cathepsin A) (PPCA) (Protective protein for beta-galactosidase) [Cleaved into: Lysosomal protective protein 32 kDa chain; Lysosomal protective protein 20 kDa chain]

 PPGB_HUMAN              Reviewed;         480 AA.
P10619; B2R798; Q561W6; Q5JZH1; Q96KJ2; Q9BR08; Q9BW68;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
16-APR-2002, sequence version 2.
10-OCT-2018, entry version 219.
RecName: Full=Lysosomal protective protein;
EC=3.4.16.5;
AltName: Full=Carboxypeptidase C;
AltName: Full=Carboxypeptidase L;
AltName: Full=Cathepsin A;
AltName: Full=Protective protein cathepsin A;
Short=PPCA;
AltName: Full=Protective protein for beta-galactosidase;
Contains:
RecName: Full=Lysosomal protective protein 32 kDa chain;
Contains:
RecName: Full=Lysosomal protective protein 20 kDa chain;
Flags: Precursor;
Name=CTSA; Synonyms=PPGB;
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), AND PARTIAL PROTEIN SEQUENCE.
PubMed=3136930; DOI=10.1016/S0092-8674(88)90999-3;
Galjart N.J., Gillemans N., Harris A., van de Horst G.T.J.,
Verheijen F.W., Galjaard H., D'Azzo A.;
"Expression of cDNA encoding the human 'protective protein' associated
with lysosomal beta-galactosidase and neuraminidase: homology to yeast
proteases.";
Cell 54:755-764(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta, and Skin;
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).
[5]
PROTEIN SEQUENCE OF 29-53 AND 327-351.
TISSUE=Platelet;
PubMed=1694176;
Jackman H.L., Tan F., Tamei H., Beurling-Harbury C., Li X.-Y.,
Skidgel R.A., Erdoes E.G.;
"A peptidase in human platelets that deamidates tachykinins. Probable
identity with the lysosomal 'protective protein'.";
J. Biol. Chem. 265:11265-11272(1990).
[6]
PROTEIN SEQUENCE OF 29-37.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[7]
FUNCTION, AND MUTAGENESIS.
PubMed=1907282;
Galjart N.J., Morreau H., Willemsen R., Gillemans N., Bonten E.J.,
D'Azzo A.;
"Human lysosomal protective protein has cathepsin A-like activity
distinct from its protective function.";
J. Biol. Chem. 266:14754-14762(1991).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145 AND ASN-333.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER ALA-28, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[12]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=8591035; DOI=10.1016/S0969-2126(01)00260-X;
Rudenko G., Bonten E., D'Azzo A., Hol W.G.J.;
"Three-dimensional structure of the human 'protective protein':
structure of the precursor form suggests a complex activation
mechanism.";
Structure 3:1249-1259(1995).
[13]
VARIANT GSL VAL-440.
PubMed=1756715;
Zhou X.Y., Galjart N.J., Willemsen R., Gillemans N., Galjaard H.,
D'Azzo A.;
"A mutation in a mild form of galactosialidosis impairs dimerization
of the protective protein and renders it unstable.";
EMBO J. 10:4041-4048(1991).
[14]
VARIANTS GSL ARG-49; ARG-65; LEU-90; ASN-249 AND CYS-395.
PubMed=8514852; DOI=10.1172/JCI116472;
Shimmoto M., Fukuhara Y., Itoh K., Oshima A., Sakuraba H., Suzuki Y.;
"Protective protein gene mutations in galactosialidosis.";
J. Clin. Invest. 91:2393-2398(1993).
[15]
VARIANTS GSL TYR-51; MET-132; PRO-236; ASN-249; THR-406; SER-439 AND
VAL-440.
PubMed=8968752; DOI=10.1093/hmg/5.12.1977;
Zhou X.Y., van der Spoel A., Rottier R., Hale G., Willemsen R.,
Berry G.T., Strisciuglio P., Morrone A., Zammarchi E., Andria G.,
d'Azzo A.;
"Molecular and biochemical analysis of protective protein/cathepsin A
mutations: correlation with clinical severity in galactosialidosis.";
Hum. Mol. Genet. 5:1977-1987(1996).
[16]
VARIANT GSL GLU-453.
PubMed=10944848; DOI=10.1007/s100380070027;
Takiguchi K., Itoh K., Shimmoto M., Ozand P.T., Doi H., Sakuraba H.;
"Structural and functional study of K453E mutant protective
protein/cathepsin A causing the late infantile form of
galactosialidosis.";
J. Hum. Genet. 45:200-206(2000).
-!- FUNCTION: Protective protein appears to be essential for both the
activity of beta-galactosidase and neuraminidase, it associates
with these enzymes and exerts a protective function necessary for
their stability and activity. This protein is also a
carboxypeptidase and can deamidate tachykinins.
{ECO:0000269|PubMed:1907282}.
-!- CATALYTIC ACTIVITY: Release of a C-terminal amino acid with broad
specificity. {ECO:0000255|PROSITE-ProRule:PRU10074,
ECO:0000255|PROSITE-ProRule:PRU10075}.
-!- SUBUNIT: Heterodimer of a 32 kDa chain and a 20 kDa chain;
disulfide-linked.
-!- SUBCELLULAR LOCATION: Lysosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P10619-1; Sequence=Displayed;
Name=2;
IsoId=P10619-2; Sequence=VSP_054832;
Note=Gene prediction based on EST data.;
-!- DISEASE: Galactosialidosis (GSL) [MIM:256540]: A lysosomal storage
disease associated with a combined deficiency of beta-
galactosidase and neuraminidase, secondary to a defect in
cathepsin A. All patients have clinical manifestations typical of
a lysosomal disorder, such as coarse facies, cherry red spots,
vertebral changes, foam cells in the bone marrow, and vacuolated
lymphocytes. Three phenotypic subtypes are recognized. The early
infantile form is associated with fetal hydrops, edema, ascites,
visceromegaly, skeletal dysplasia, and early death. The late
infantile type is characterized by hepatosplenomegaly, growth
retardation, cardiac involvement, and a normal or mildly affected
mental state. The juvenile/adult form is characterized by
myoclonus, ataxia, angiokeratoma, mental retardation, neurologic
deterioration, absence of visceromegaly, and long survival.
{ECO:0000269|PubMed:10944848, ECO:0000269|PubMed:1756715,
ECO:0000269|PubMed:8514852, ECO:0000269|PubMed:8968752}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M22960; AAA36476.1; -; mRNA.
EMBL; AK312898; BAG35745.1; -; mRNA.
EMBL; AL008726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000597; AAH00597.1; -; mRNA.
EMBL; BC093009; AAH93009.1; -; mRNA.
CCDS; CCDS46609.1; -. [P10619-1]
PIR; A31589; A31589.
RefSeq; NP_000299.2; NM_000308.3.
RefSeq; NP_001121167.1; NM_001127695.2. [P10619-1]
RefSeq; NP_001161066.1; NM_001167594.2.
UniGene; Hs.609336; -.
PDB; 1IVY; X-ray; 2.20 A; A/B=29-480.
PDB; 3BP4; X-ray; 1.85 A; C=2-10.
PDB; 3BP7; X-ray; 1.80 A; C=2-10.
PDB; 3BXN; X-ray; 1.86 A; C=2-10.
PDB; 4AZ0; X-ray; 2.17 A; A=29-326, B=327-480.
PDB; 4AZ3; X-ray; 2.04 A; A=29-326, B=327-480.
PDB; 4CI9; X-ray; 1.58 A; A=29-480.
PDB; 4CIA; X-ray; 1.98 A; A=29-480.
PDB; 4CIB; X-ray; 1.89 A; A=29-480.
PDB; 4MWS; X-ray; 2.80 A; A/B=29-480.
PDB; 4MWT; X-ray; 3.85 A; A/B=29-480.
PDBsum; 1IVY; -.
PDBsum; 3BP4; -.
PDBsum; 3BP7; -.
PDBsum; 3BXN; -.
PDBsum; 4AZ0; -.
PDBsum; 4AZ3; -.
PDBsum; 4CI9; -.
PDBsum; 4CIA; -.
PDBsum; 4CIB; -.
PDBsum; 4MWS; -.
PDBsum; 4MWT; -.
ProteinModelPortal; P10619; -.
SMR; P10619; -.
BioGrid; 111472; 41.
CORUM; P10619; -.
IntAct; P10619; 13.
STRING; 9606.ENSP00000361562; -.
BindingDB; P10619; -.
ChEMBL; CHEMBL6115; -.
GuidetoPHARMACOLOGY; 1581; -.
ESTHER; human-CTSA; Carboxypeptidase_S10.
MEROPS; S10.002; -.
GlyConnect; 1477; -.
iPTMnet; P10619; -.
PhosphoSitePlus; P10619; -.
SwissPalm; P10619; -.
BioMuta; CTSA; -.
DMDM; 20178316; -.
OGP; P10619; -.
EPD; P10619; -.
MaxQB; P10619; -.
PaxDb; P10619; -.
PeptideAtlas; P10619; -.
PRIDE; P10619; -.
ProteomicsDB; 52619; -.
TopDownProteomics; P10619-1; -. [P10619-1]
TopDownProteomics; P10619-2; -. [P10619-2]
DNASU; 5476; -.
Ensembl; ENST00000191018; ENSP00000191018; ENSG00000064601. [P10619-1]
Ensembl; ENST00000372459; ENSP00000361537; ENSG00000064601. [P10619-1]
Ensembl; ENST00000646241; ENSP00000493613; ENSG00000064601. [P10619-1]
GeneID; 5476; -.
KEGG; hsa:5476; -.
UCSC; uc002xqj.5; human. [P10619-1]
CTD; 5476; -.
DisGeNET; 5476; -.
EuPathDB; HostDB:ENSG00000064601.16; -.
GeneCards; CTSA; -.
HGNC; HGNC:9251; CTSA.
HPA; CAB024930; -.
HPA; HPA031068; -.
MalaCards; CTSA; -.
MIM; 256540; phenotype.
MIM; 613111; gene.
neXtProt; NX_P10619; -.
OpenTargets; ENSG00000064601; -.
Orphanet; 351; Galactosialidosis.
PharmGKB; PA33572; -.
eggNOG; KOG1282; Eukaryota.
eggNOG; COG2939; LUCA.
GeneTree; ENSGT00880000138014; -.
HOVERGEN; HBG053652; -.
InParanoid; P10619; -.
KO; K13289; -.
PhylomeDB; P10619; -.
TreeFam; TF323769; -.
BRENDA; 3.4.16.5; 2681.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-4085001; Sialic acid metabolism.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SABIO-RK; P10619; -.
SignaLink; P10619; -.
ChiTaRS; CTSA; human.
EvolutionaryTrace; P10619; -.
GeneWiki; Cathepsin_A; -.
GenomeRNAi; 5476; -.
PRO; PR:P10619; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000064601; Expressed in 230 organ(s), highest expression level in right adrenal gland.
CleanEx; HS_CTSA; -.
ExpressionAtlas; P10619; baseline and differential.
Genevisible; P10619; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005764; C:lysosome; NAS:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0004180; F:carboxypeptidase activity; TAS:ProtInc.
GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
GO; GO:0004308; F:exo-alpha-sialidase activity; TAS:Reactome.
GO; GO:0004185; F:serine-type carboxypeptidase activity; IMP:ParkinsonsUK-UCL.
GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
GO; GO:1904715; P:negative regulation of chaperone-mediated autophagy; IGI:ParkinsonsUK-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0006508; P:proteolysis; IDA:ParkinsonsUK-UCL.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IBA:GO_Central.
GO; GO:1904714; P:regulation of chaperone-mediated autophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0031647; P:regulation of protein stability; IMP:ParkinsonsUK-UCL.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR001563; Peptidase_S10.
InterPro; IPR033124; Ser_caboxypep_his_AS.
InterPro; IPR018202; Ser_caboxypep_ser_AS.
PANTHER; PTHR11802; PTHR11802; 1.
Pfam; PF00450; Peptidase_S10; 1.
PRINTS; PR00724; CRBOXYPTASEC.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS00560; CARBOXYPEPT_SER_HIS; 1.
PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Carboxypeptidase;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Glycoprotein; Hydrolase; Lysosome; Protease;
Reference proteome; Signal; Zymogen.
SIGNAL 1 28 {ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:1694176}.
CHAIN 29 480 Lysosomal protective protein.
/FTId=PRO_0000004274.
CHAIN 29 326 Lysosomal protective protein 32 kDa
chain.
/FTId=PRO_0000004275.
CHAIN 327 480 Lysosomal protective protein 20 kDa
chain.
/FTId=PRO_0000004276.
ACT_SITE 178 178
ACT_SITE 400 400 {ECO:0000250}.
ACT_SITE 457 457
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:19159218}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 88 362
DISULFID 240 256
DISULFID 241 246
DISULFID 281 331
VAR_SEQ 102 118 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_054832.
VARIANT 49 49 Q -> R (in GSL; dbSNP:rs137854541).
{ECO:0000269|PubMed:8514852}.
/FTId=VAR_001385.
VARIANT 51 51 S -> Y (in GSL).
{ECO:0000269|PubMed:8968752}.
/FTId=VAR_063018.
VARIANT 65 65 W -> R (in GSL; dbSNP:rs28934603).
{ECO:0000269|PubMed:8514852}.
/FTId=VAR_001386.
VARIANT 90 90 S -> L (in GSL; dbSNP:rs137854542).
{ECO:0000269|PubMed:8514852}.
/FTId=VAR_001387.
VARIANT 132 132 V -> M (in GSL; dbSNP:rs137854545).
{ECO:0000269|PubMed:8968752}.
/FTId=VAR_063019.
VARIANT 236 236 L -> P (in GSL; dbSNP:rs137854546).
{ECO:0000269|PubMed:8968752}.
/FTId=VAR_063020.
VARIANT 249 249 Y -> N (in GSL; small amount of activity;
dbSNP:rs137854544).
{ECO:0000269|PubMed:8514852,
ECO:0000269|PubMed:8968752}.
/FTId=VAR_001388.
VARIANT 395 395 Y -> C (in GSL; loss of activity;
dbSNP:rs137854543).
{ECO:0000269|PubMed:8514852}.
/FTId=VAR_001389.
VARIANT 406 406 M -> T (in GSL; dbSNP:rs137854548).
{ECO:0000269|PubMed:8968752}.
/FTId=VAR_063021.
VARIANT 439 439 G -> S (in GSL; dbSNP:rs137854547).
{ECO:0000269|PubMed:8968752}.
/FTId=VAR_063022.
VARIANT 440 440 F -> V (in GSL; dbSNP:rs137854540).
{ECO:0000269|PubMed:1756715,
ECO:0000269|PubMed:8968752}.
/FTId=VAR_001390.
VARIANT 453 453 K -> E (in GSL; dbSNP:rs137854549).
{ECO:0000269|PubMed:10944848}.
/FTId=VAR_063023.
MUTAGEN 178 178 S->A: Inactivates the enzyme.
{ECO:0000269|PubMed:1907282}.
MUTAGEN 457 457 H->Q: Inactivates the enzyme.
{ECO:0000269|PubMed:1907282}.
CONFLICT 19 19 Missing (in Ref. 4; AAH00597).
{ECO:0000305}.
CONFLICT 56 56 G -> S (in Ref. 1; AAA36476).
{ECO:0000305}.
HELIX 31 33 {ECO:0000244|PDB:4CI9}.
STRAND 41 43 {ECO:0000244|PDB:4CIA}.
STRAND 49 55 {ECO:0000244|PDB:4CI9}.
STRAND 60 67 {ECO:0000244|PDB:4CI9}.
TURN 73 75 {ECO:0000244|PDB:4CI9}.
STRAND 78 82 {ECO:0000244|PDB:4CI9}.
TURN 85 87 {ECO:0000244|PDB:4CI9}.
HELIX 91 96 {ECO:0000244|PDB:4CI9}.
STRAND 99 103 {ECO:0000244|PDB:4CI9}.
STRAND 110 112 {ECO:0000244|PDB:4CI9}.
HELIX 117 119 {ECO:0000244|PDB:4CI9}.
STRAND 120 126 {ECO:0000244|PDB:4CI9}.
STRAND 136 139 {ECO:0000244|PDB:1IVY}.
HELIX 146 163 {ECO:0000244|PDB:4CI9}.
HELIX 165 167 {ECO:0000244|PDB:4CI9}.
STRAND 168 170 {ECO:0000244|PDB:4MWS}.
STRAND 172 177 {ECO:0000244|PDB:4CI9}.
HELIX 180 192 {ECO:0000244|PDB:4CI9}.
STRAND 199 206 {ECO:0000244|PDB:4CI9}.
HELIX 211 224 {ECO:0000244|PDB:4CI9}.
HELIX 230 240 {ECO:0000244|PDB:4CI9}.
HELIX 254 268 {ECO:0000244|PDB:4CI9}.
STRAND 269 271 {ECO:0000244|PDB:4CI9}.
STRAND 286 292 {ECO:0000244|PDB:1IVY}.
STRAND 295 298 {ECO:0000244|PDB:1IVY}.
HELIX 315 317 {ECO:0000244|PDB:1IVY}.
HELIX 318 321 {ECO:0000244|PDB:1IVY}.
STRAND 324 327 {ECO:0000244|PDB:1IVY}.
HELIX 335 341 {ECO:0000244|PDB:4CI9}.
HELIX 344 349 {ECO:0000244|PDB:4CI9}.
HELIX 364 369 {ECO:0000244|PDB:4CI9}.
STRAND 375 377 {ECO:0000244|PDB:4CI9}.
HELIX 378 386 {ECO:0000244|PDB:4CI9}.
STRAND 391 397 {ECO:0000244|PDB:4CI9}.
STRAND 401 403 {ECO:0000244|PDB:4CI9}.
HELIX 405 414 {ECO:0000244|PDB:4CI9}.
STRAND 424 429 {ECO:0000244|PDB:4CI9}.
HELIX 431 433 {ECO:0000244|PDB:4CI9}.
STRAND 435 444 {ECO:0000244|PDB:4CI9}.
STRAND 447 452 {ECO:0000244|PDB:4CI9}.
HELIX 459 462 {ECO:0000244|PDB:4CI9}.
HELIX 464 475 {ECO:0000244|PDB:4CI9}.
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


Related products :

Catalog number Product name Quantity
EIAAB32011 Carboxypeptidase C,Carboxypeptidase L,Cathepsin A,CTSA,Homo sapiens,Human,Lysosomal protective protein,PPCA,PPGB,Protective protein cathepsin A,Protective protein for beta-galactosidase
EIAAB32013 Carboxypeptidase C,Carboxypeptidase L,Cathepsin A,Ctsa,Lysosomal protective protein,Mouse,Mus musculus,PPCA,Ppgb,Protective protein cathepsin A,Protective protein for beta-galactosidase
EIAAB32012 Bos taurus,Bovine,Cathepsin A,CTSA,Lysosomal protective protein,PPGB
EH1853 Lysosomal protective protein Elisa Kit 96T
E02L0309 Rat Lysosomal protective protein ELISA 96T/kit
E14L0309 Sheep Lysosomal protective protein ELISA 96T/kit
E12L0309 Chicken Lysosomal protective protein ELISA 96T/kit
E01L0309 Human Lysosomal protective protein ELISA 96T/kit
E03L0309 Mouse Lysosomal protective protein ELISA 96T/kit
E04L0309 Rabbit Lysosomal protective protein ELISA 96T/kit
E08L0309 Canine Lysosomal protective protein ELISA 96T/kit
E05L0309 Guinea Pig Lysosomal protective protein ELISA 96T/kit
E11L0309 Bovine Lysosomal protective protein ELISA 96T/kit
E06L0309 Goat Lysosomal protective protein ELISA 96T/kit
E09L0309 Monkey Lysosomal protective protein ELISA 96T/kit
E07L0309 Porcine Lysosomal protective protein ELISA 96T/kit
20-272-192185 beta Galactosidase - Mouse monoclonal [BG - 02] to beta Galactosidase; EC 3.4.16.5; Cathepsin A; Carboxypeptidase C; Protective protein for beta-galactosidase Monoclonal 0.1 mg
20-272-191989 beta Galactosidase - Mouse monoclonal [DC1 4C7] to beta Galactosidase; EC 3.4.16.5; Cathepsin A; Carboxypeptidase C; Protective protein for beta-galactosidase Monoclonal 0.1 mg
18-272-196702 beta Galactosidase - Rabbit polyclonal to beta Galactosidase; EC 3.4.16.5; Cathepsin A; Carboxypeptidase C; Protective protein for beta-galactosidase Polyclonal 0.1 mg
20-272-190060 beta Galactosidase - Mouse monoclonal [2E9] to beta Galactosidase; EC 3.4.16.5; Cathepsin A; Carboxypeptidase C; Protective protein for beta-galactosidase Monoclonal 0.1 mg
18-272-196853 beta Galactosidase - Rabbit polyclonal to beta Galactosidase; EC 3.4.16.5; Cathepsin A; Carboxypeptidase C; Protective protein for beta-galactosidase Polyclonal 1 mg
CSB-EL006184HU Human Lysosomal protective protein(CTSA) ELISA kit 96T
CSB-EL006184MO Mouse Lysosomal protective protein(CTSA) ELISA kit 96T
CSB-EL006184BO Bovine Lysosomal protective protein(CTSA) ELISA kit 96T
bs-6040R Rabbit Anti-Lysosomal Protective Protein Polyclonal Antibody 100ul


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur