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

Candidapepsin-10 (EC 3.4.23.24) (ACP 10) (Aspartate protease 10) (Secreted aspartic protease 10)

 CAR10_CANAL             Reviewed;         453 AA.
Q5A651; A0A1D8PM25;
13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 1.
22-NOV-2017, entry version 89.
RecName: Full=Candidapepsin-10;
EC=3.4.23.24;
AltName: Full=ACP 10;
AltName: Full=Aspartate protease 10;
AltName: Full=Secreted aspartic protease 10;
Flags: Precursor;
Name=SAP10; Synonyms=YPS3; OrderedLocusNames=CAALFM_C404470WA;
ORFNames=CaO19.11320, CaO19.3839;
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Debaryomycetaceae;
Candida/Lodderomyces clade; Candida.
NCBI_TaxID=237561;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=15123810; DOI=10.1073/pnas.0401648101;
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S.,
Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T.,
Davis R.W., Scherer S.;
"The diploid genome sequence of Candida albicans.";
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
[2]
GENOME REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
Chibana H., Nantel A., Magee P.T.;
"Assembly of the Candida albicans genome into sixteen supercontigs
aligned on the eight chromosomes.";
Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME
REANNOTATION.
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
"Assembly of a phased diploid Candida albicans genome facilitates
allele-specific measurements and provides a simple model for repeat
and indel structure.";
Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
[4]
GLYCOSYLATION, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=16269404; DOI=10.1074/jbc.M509297200;
Albrecht A., Felk A., Pichova I., Naglik J.R., Schaller M.,
de Groot P., Maccallum D., Odds F.C., Schafer W., Klis F., Monod M.,
Hube B.;
"Glycosylphosphatidylinositol-anchored proteases of Candida albicans
target proteins necessary for both cellular processes and host-
pathogen interactions.";
J. Biol. Chem. 281:688-694(2006).
[5]
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=21646240; DOI=10.1093/jb/mvr073;
Aoki W., Kitahara N., Miura N., Morisaka H., Yamamoto Y., Kuroda K.,
Ueda M.;
"Comprehensive characterization of secreted aspartic proteases encoded
by a virulence gene family in Candida albicans.";
J. Biochem. 150:431-438(2011).
-!- FUNCTION: Secreted aspartic peptidases (SAPs) are a group of ten
acidic hydrolases considered as key virulence factors. These
enzymes supply the fungus with nutrient amino acids as well as are
able to degrade the selected host's proteins involved in the
immune defense. Required for cell surface integrity and cell
separation during budding. {ECO:0000269|PubMed:16269404}.
-!- CATALYTIC ACTIVITY: Preferential cleavage at the carboxyl of
hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-
Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates
trypsinogen, and degrades keratin. {ECO:0000269|PubMed:21646240}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6.0. {ECO:0000269|PubMed:21646240};
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16269404}. Cell
membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
-!- PTM: O-glycosylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; CP017626; AOW29196.1; -; Genomic_DNA.
RefSeq; XP_717243.1; XM_712150.2.
ProteinModelPortal; Q5A651; -.
SMR; Q5A651; -.
MEROPS; A01.085; -.
PRIDE; Q5A651; -.
EnsemblFungi; AOW29196; AOW29196; CAALFM_C404470WA.
GeneID; 3641126; -.
KEGG; cal:CAALFM_C404470WA; -.
CGD; CAL0000201140; SAP10.
InParanoid; Q5A651; -.
KO; K06005; -.
OrthoDB; EOG092C3KPP; -.
PRO; PR:Q5A651; -.
Proteomes; UP000000559; Chromosome 4.
GO; GO:0046658; C:anchored component of plasma membrane; IDA:CGD.
GO; GO:0009986; C:cell surface; IDA:CGD.
GO; GO:0005576; C:extracellular region; IDA:CGD.
GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:CGD.
GO; GO:0044406; P:adhesion of symbiont to host; IMP:CGD.
GO; GO:0031505; P:fungal-type cell wall organization; IMP:CGD.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0006508; P:proteolysis; IDA:CGD.
CDD; cd05474; SAP_like; 1.
Gene3D; 2.40.70.10; -; 2.
InterPro; IPR001461; Aspartic_peptidase_A1.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR033121; PEPTIDASE_A1.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
InterPro; IPR033876; SAP-like.
PANTHER; PTHR13683; PTHR13683; 1.
Pfam; PF00026; Asp; 1.
PRINTS; PR00792; PEPSIN.
SUPFAM; SSF50630; SSF50630; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
PROSITE; PS51767; PEPTIDASE_A1; 1.
1: Evidence at protein level;
Aspartyl protease; Cell membrane; Cleavage on pair of basic residues;
Complete proteome; Disulfide bond; Glycoprotein; GPI-anchor;
Hydrolase; Lipoprotein; Membrane; Protease; Reference proteome;
Repeat; Secreted; Signal; Virulence; Zymogen.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 429 Candidapepsin-10.
/FTId=PRO_0000424306.
PROPEP 430 453 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000424307.
DOMAIN 52 372 Peptidase A1. {ECO:0000255|PROSITE-
ProRule:PRU01103}.
REGION 70 72 Inhibitor binding. {ECO:0000250}.
REGION 138 139 Inhibitor binding. {ECO:0000250}.
REGION 266 270 Inhibitor binding. {ECO:0000250}.
ACT_SITE 70 70 {ECO:0000255|PROSITE-ProRule:PRU10094}.
ACT_SITE 266 266 {ECO:0000255|PROSITE-ProRule:PRU10094}.
LIPID 429 429 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 128 128 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 168 168 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 208 208 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 211 211 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 245 245 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 287 287 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 424 424 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 85 112 {ECO:0000250}.
DISULFID 301 333 {ECO:0000250}.
SEQUENCE 453 AA; 49333 MW; D26DDFF460BCFC37 CRC64;
MDLVIMNFVF LLYLTSVVKC SIKLDFNKVS TPSKYTKRDA LPMPLINDKI LYTTELEIGS
NKDKVSVSID TGSYDLWVMS NDAVCYKVSE FQTEGAPQLP DIFNDIDQDY SCTFNGTYNS
KSSKTFKNTS EDFSIGYVDG SAAQGVWGYD SVQFGQYGVT GLKIGIANRS SVSDGILGIG
IANGYDNFPV LLQKQGLINK IAYSVYLNSS NSTTGTILFG AIDHAKYKGA LSTVPVDSKS
QLSVNVTNLK TKNGNVASGG HSILLDTGST FSIFPDEWID ALGHSLNATY DEDESVYEIE
CDGYDEHFFG FSIGDSDFSV PIQDLKTEKD GQCYLAIMSN SVIGGGGILF GDDILRQIYL
VYDLQDMTIS VAPVVYTEDE DIEEILNPNE DQNEVPTSTS FTQSASSSGS QPSSTISGEN
MDKNTTSSSS GNCQTRSWIA ILSALFLVYI HII


Related products :

Catalog number Product name Quantity
18-661-15088 Beta-secretase 2 - EC 3.4.23.45; Beta-site APP-cleaving enzyme 2; Aspartyl protease 1; Asp 1; ASP1; Membrane-associated aspartic protease 1; Memapsin-1; Down region aspartic protease Polyclonal 0.1 mg
18-661-15089 Beta-secretase 2 - EC 3.4.23.45; Beta-site APP-cleaving enzyme 2; Aspartyl protease 1; Asp 1; ASP1; Membrane-associated aspartic protease 1; Memapsin-1; Down region aspartic protease Polyclonal 0.1 mg
orb90001 GST_HRV Protease Protease Recombinant is fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes subset of sequences whic 100 IU
orb90006 Tobacco Etch Virus Protease protein Recombinant TEV Protease (rTEV) is site-specific protease purified from E.coli The protease can be used for the removal of affinity tags from fusion proteins. The s 300 IU
orb82817 PreScission Protease enzyme PreScission Protease is a fusion protein of Glutathione S-Transferase (GST) and Human Rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes a subset of 1000 U
orb82840 Tobacco Etch Virus Protease enzyme Recombinant TEV Protease (rTEV) is a site-specific protease purified from E. coli by the affinity tag, GST tag. The protease can be used for the removal of affinity 1000 IU
E2015h ELISA Apoptotic cysteine protease,Apoptotic protease Mch-5,CAP4,CASP8,CASP-8,Caspase-8,FADD-homologous ICE_ced-3-like protease,FADD-like ICE,FLICE,Homo sapiens,Human,ICE-like apoptotic protease 5,MACH 96T
U2015h CLIA Apoptotic cysteine protease,Apoptotic protease Mch-5,CAP4,CASP8,CASP-8,Caspase-8,FADD-homologous ICE_ced-3-like protease,FADD-like ICE,FLICE,Homo sapiens,Human,ICE-like apoptotic protease 5,MACH, 96T
E2015h ELISA kit Apoptotic cysteine protease,Apoptotic protease Mch-5,CAP4,CASP8,CASP-8,Caspase-8,FADD-homologous ICE_ced-3-like protease,FADD-like ICE,FLICE,Homo sapiens,Human,ICE-like apoptotic protease 5 96T
EIAAB37886 DEN1,Deneddylase-1,FKSG8,Homo sapiens,Human,NEDD8-specific protease 1,NEDP1,Protease, cysteine 2,PRSC2,SENP8,Sentrin_SUMO-specific protease SENP8,Sentrin-specific protease 8
U2015h CLIA kit Apoptotic cysteine protease,Apoptotic protease Mch-5,CAP4,CASP8,CASP-8,Caspase-8,FADD-homologous ICE_ced-3-like protease,FADD-like ICE,FLICE,Homo sapiens,Human,ICE-like apoptotic protease 5, 96T
E1812h ELISA kit AEPLC,ALP56,Asp 1,ASP1,ASP21,Aspartic-like protease 56 kDa,Aspartyl protease 1,BACE2,Beta-secretase 2,Beta-site amyloid precursor protein cleaving enzyme 2,Beta-site APP cleaving enzyme 2,C 96T
U1812h CLIA kit AEPLC,ALP56,Asp 1,ASP1,ASP21,Aspartic-like protease 56 kDa,Aspartyl protease 1,BACE2,Beta-secretase 2,Beta-site amyloid precursor protein cleaving enzyme 2,Beta-site APP cleaving enzyme 2,CD 96T
U1812m CLIA Asp 1,ASP1,Aspartyl protease 1,Bace2,Beta-secretase 2,Beta-site amyloid precursor protein cleaving enzyme 2,Beta-site APP cleaving enzyme 2,Memapsin-1,Membrane-associated aspartic protease 1,Mous 96T
U0718r CLIA Asp 2,ASP2,Aspartyl protease 2,Bace,Bace1,Beta-secretase 1,Beta-site amyloid precursor protein cleaving enzyme 1,Beta-site APP cleaving enzyme 1,Memapsin-2,Membrane-associated aspartic protease 2 96T
E0718r ELISA Asp 2,ASP2,Aspartyl protease 2,Bace,Bace1,Beta-secretase 1,Beta-site amyloid precursor protein cleaving enzyme 1,Beta-site APP cleaving enzyme 1,Memapsin-2,Membrane-associated aspartic protease 96T
U0718m CLIA Asp 2,ASP2,Aspartyl protease 2,Bace,Bace1,Beta-secretase 1,Beta-site amyloid precursor protein cleaving enzyme 1,Beta-site APP cleaving enzyme 1,Memapsin-2,Membrane-associated aspartic protease 2 96T
E0718m ELISA Asp 2,ASP2,Aspartyl protease 2,Bace,Bace1,Beta-secretase 1,Beta-site amyloid precursor protein cleaving enzyme 1,Beta-site APP cleaving enzyme 1,Memapsin-2,Membrane-associated aspartic protease 96T
U1812h CLIA AEPLC,ALP56,Asp 1,ASP1,ASP21,Aspartic-like protease 56 kDa,Aspartyl protease 1,BACE2,Beta-secretase 2,Beta-site amyloid precursor protein cleaving enzyme 2,Beta-site APP cleaving enzyme 2,CDA13,D 96T
E1812h ELISA AEPLC,ALP56,Asp 1,ASP1,ASP21,Aspartic-like protease 56 kDa,Aspartyl protease 1,BACE2,Beta-secretase 2,Beta-site amyloid precursor protein cleaving enzyme 2,Beta-site APP cleaving enzyme 2,CDA13, 96T
U1812m CLIA kit Asp 1,ASP1,Aspartyl protease 1,Bace2,Beta-secretase 2,Beta-site amyloid precursor protein cleaving enzyme 2,Beta-site APP cleaving enzyme 2,Memapsin-1,Membrane-associated aspartic protease 1 96T
E1812m ELISA kit Asp 1,ASP1,Aspartyl protease 1,Bace2,Beta-secretase 2,Beta-site amyloid precursor protein cleaving enzyme 2,Beta-site APP cleaving enzyme 2,Memapsin-1,Membrane-associated aspartic protease 96T
E1812m ELISA Asp 1,ASP1,Aspartyl protease 1,Bace2,Beta-secretase 2,Beta-site amyloid precursor protein cleaving enzyme 2,Beta-site APP cleaving enzyme 2,Memapsin-1,Membrane-associated aspartic protease 1,Mou 96T
18-661-15090 Beta-secretase 1 - EC 3.4.23.46; Beta-site APP cleaving enzyme 1; Beta-site amyloid precursor protein cleaving enzyme 1; Membrane-associated aspartic protease 2; Memapsin-2; Aspartyl protease 2; Asp 2 0.1 mg
U0691h CLIA Homo sapiens,Human,Kallikrein-6,KLK6,Neurosin,Protease M,PRSS18,PRSS9,Serine protease 18,Serine protease 9,SP59,Zyme 96T


 

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