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

pH-responsive protein 1 (pH-regulated protein 1)

 PHR1_CANAL              Reviewed;         548 AA.
P43076; A0A1D8PM46; Q5A661;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
15-MAR-2017, sequence version 4.
30-AUG-2017, entry version 96.
RecName: Full=pH-responsive protein 1;
AltName: Full=pH-regulated protein 1;
Flags: Precursor;
Name=PHR1; OrderedLocusNames=CAALFM_C404530CA;
ORFNames=CaO19.11310, CaO19.3829;
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 [GENOMIC DNA].
STRAIN=SC5314 / ATCC MYA-2876;
PubMed=7823929; DOI=10.1128/MCB.15.2.601;
Saporito-Irwin S.M., Birse C.E., Sypherd P.S., Fonzi W.A.;
"PHR1, a pH-regulated gene of Candida albicans, is required for
morphogenesis.";
Mol. Cell. Biol. 15:601-613(1995).
[2]
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).
[3]
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).
[4]
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).
-!- FUNCTION: Required for apical cell growth and plays an essential
role in morphogenesis. May be integral to the pathogenic ability
of the organism.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor,
GPI-anchor {ECO:0000305}.
-!- INDUCTION: Strongly expressed under conditions of alkaline pH but
not expressed at any pH below 5.5.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M90812; AAA68196.1; -; Genomic_DNA.
EMBL; CP017626; AOW29201.1; -; Genomic_DNA.
RefSeq; XP_717233.2; XM_712140.2.
ProteinModelPortal; P43076; -.
SMR; P43076; -.
CAZy; CBM43; Carbohydrate-Binding Module Family 43.
CAZy; GH72; Glycoside Hydrolase Family 72.
PRIDE; P43076; -.
GeneID; 3641108; -.
KEGG; cal:CAALFM_C404530CA; -.
CGD; CAL0000177455; PHR1.
InParanoid; P43076; -.
OrthoDB; EOG092C1TYR; -.
PRO; PR:P43076; -.
Proteomes; UP000000559; Chromosome 4.
GO; GO:0046658; C:anchored component of plasma membrane; IDA:CGD.
GO; GO:0030428; C:cell septum; IDA:CGD.
GO; GO:0009986; C:cell surface; IDA:CGD.
GO; GO:0033101; C:cellular bud membrane; IDA:CGD.
GO; GO:0005621; C:cellular bud scar; IDA:CGD.
GO; GO:0005576; C:extracellular region; IDA:CGD.
GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
GO; GO:0045121; C:membrane raft; IDA:CGD.
GO; GO:0005886; C:plasma membrane; IDA:CGD.
GO; GO:0030445; C:yeast-form cell wall; IDA:CGD.
GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; ISA:CGD.
GO; GO:0042123; F:glucanosyltransferase activity; IDA:CGD.
GO; GO:0044406; P:adhesion of symbiont to host; IMP:CGD.
GO; GO:0031589; P:cell-substrate adhesion; IMP:CGD.
GO; GO:0035690; P:cellular response to drug; IMP:CGD.
GO; GO:0071467; P:cellular response to pH; IMP:CGD.
GO; GO:0044114; P:development of symbiont in host; IMP:CGD.
GO; GO:0044409; P:entry into host; IMP:CGD.
GO; GO:0030447; P:filamentous growth; IMP:CGD.
GO; GO:0044182; P:filamentous growth of a population of unicellular organisms; IMP:CGD.
GO; GO:0031505; P:fungal-type cell wall organization; IDA:CGD.
GO; GO:0044117; P:growth of symbiont in host; IMP:CGD.
GO; GO:0009405; P:pathogenesis; IMP:CGD.
GO; GO:0044407; P:single-species biofilm formation in or on host organism; IMP:CGD.
GO; GO:0044011; P:single-species biofilm formation on inanimate substrate; IMP:CGD.
InterPro; IPR004886; Glucanosyltransferase.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR012946; X8.
PANTHER; PTHR31468; PTHR31468; 1.
Pfam; PF03198; Glyco_hydro_72; 1.
Pfam; PF07983; X8; 1.
SMART; SM00768; X8; 1.
SUPFAM; SSF51445; SSF51445; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
GPI-anchor; Lipoprotein; Membrane; Reference proteome; Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 517 pH-responsive protein 1.
/FTId=PRO_0000010483.
PROPEP 518 548 Removed in mature form. {ECO:0000255}.
/FTId=PRO_0000010484.
COMPBIAS 453 499 Ser-rich.
COMPBIAS 500 517 Poly-Ser.
LIPID 517 517 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 41 41 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 173 173 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 261 261 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 82 111 {ECO:0000250|UniProtKB:Q06135}.
DISULFID 224 358 {ECO:0000250|UniProtKB:Q06135}.
DISULFID 242 273 {ECO:0000250|UniProtKB:Q06135}.
DISULFID 381 432 {ECO:0000250|UniProtKB:Q06135}.
DISULFID 390 456 {ECO:0000250|UniProtKB:Q06135}.
DISULFID 409 414 {ECO:0000250|UniProtKB:Q06135}.
CONFLICT 79 79 A -> R (in Ref. 1; AAA68196).
{ECO:0000305}.
SEQUENCE 548 AA; 59457 MW; 0836AD1428C5769A CRC64;
MYSLIKSLAT FATLFSLTLA KFESSTPPVE VVGNKFYFSN NGSQFLIRGI AYQQDAAGSV
SSGYDADPNR KYNDPLADAD ACKRDVKYFK ESNTNTLRVY AIDPDKDHEE CMKIFSDAGI
YIVADLSEPT VSINRNNPEW NLDLYKRYTK VIDKMQEYSN VLGFFAGNEV TNNRSNTDAS
AFVKAAIRDM KKYIKESDYR QIPVGYSSND DEEIRVAIAD YFSCGSLDDR ADFFGINMYE
WCGKSTFETS GYKDRTEEIK NLTIPAFFSE YGCNANRPRL FQEIGTLYSD KMTDVWSGGI
VYMYFEEANK YGLVSVDGNS VKTLSDYNNY KSEMNKISPS LAHTSTLSSS DASKTLQCPG
TAASTWKAAT NLPPTPDESY CDCISKSLEC VVADDVDKED YGDLFGQVCG YIDCSAISAD
GSKGEYGVAS FCSDKDRLSY VLNQYYLDQD KKSSACDFKG SASINSKASA SGSCKAVSGV
ATGKASSSGG SSKSGSSSAS ASGSSSSSTS SGSSSSSGVK ATQQMSMVKL VSIITIVTAF
VGGMSVVF


Related products :

Catalog number Product name Quantity
EIAAB10733 Ddit4,Dexamethasone-induced gene 2 protein,Dig2,DNA damage-inducible transcript 4 protein,HIF-1 responsive protein RTP801,Mouse,Mus musculus,Protein regulated in development and DNA damage response 1,
18-785-210207 HSP27 (Phospho-Ser82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210207 HSP27 (Phospho-Ser82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210206 HSP27 (Phospho-Ser78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210206 HSP27 (Phospho-Ser78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210205 HSP27 (Phospho-Ser15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210205 HSP27 (Phospho-Ser15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
EIAAB10743 DDIT4L,DNA damage-inducible transcript 4-like protein,HIF-1 responsive protein RTP801-like,Homo sapiens,Human,Protein regulated in development and DNA damage response 2,REDD2,REDD-2,RTP801L
10-002-38024 Hsp27 human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.1 mg
18-785-210210 HSP27 (Ab-82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210210 HSP27 (Ab-82) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210209 HSP27 (Ab-78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
18-785-210209 HSP27 (Ab-78) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210208 HSP27 (Ab-15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.05 mg
18-785-210208 HSP27 (Ab-15) - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg
10-002-38024 Hsp27 human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 1 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.05 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 0.01 mg
10-663-45494 Heat Shock Protein 27kD (HSP27) Human - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein N_A 1 mg
18-003-42935 Heat-shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg Protein A
18-003-43409 Heat shock protein beta-1 - HspB1; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27; Estrogen-regulated 24 kDa protein; 28 kDa heat shock protein Polyclonal 0.1 mg Protein A
EIAAB10730 Ddit4,DNA damage-inducible transcript 4 protein,HIF-1 responsive protein RTP801,Protein regulated in development and DNA damage response 1,Rat,Rattus norvegicus,Redd1,REDD-1,Rtp801
EIAAB10732 DDIT4,DNA damage-inducible transcript 4 protein,HIF-1 responsive protein RTP801,Homo sapiens,Human,Protein regulated in development and DNA damage response 1,REDD1,REDD-1,RTP801
U0693h CLIA 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive protein 2 96T
E0693h ELISA 28 kDa heat shock protein,Estrogen-regulated 24 kDa protein,Heat shock 27 kDa protein,Heat shock protein beta-1,Homo sapiens,HSP 27,HSP27,HSP28,HspB1,HSPB1,Human,SRP27,Stress-responsive protein 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