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

Subtilisin-like protease SBT1.2 (EC 3.4.21.-) (Cucumisin-like serine protease SDD1) (Protein STOMATAL DENSITY AND DISTRIBUTION 1) (Subtilase subfamily 1 member 2) (AtSBT1.2) (Subtilisin-like protease SDD1)

 SBT12_ARATH             Reviewed;         775 AA.
O64495;
08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
23-MAY-2018, entry version 123.
RecName: Full=Subtilisin-like protease SBT1.2 {ECO:0000303|PubMed:16193095};
EC=3.4.21.- {ECO:0000305};
AltName: Full=Cucumisin-like serine protease SDD1;
AltName: Full=Protein STOMATAL DENSITY AND DISTRIBUTION 1;
AltName: Full=Subtilase subfamily 1 member 2 {ECO:0000303|PubMed:16193095};
Short=AtSBT1.2 {ECO:0000303|PubMed:16193095};
AltName: Full=Subtilisin-like protease SDD1 {ECO:0000303|PubMed:10809670};
Flags: Precursor;
Name=SBT1.2 {ECO:0000303|PubMed:16193095};
Synonyms=SDD1 {ECO:0000303|PubMed:10809670};
OrderedLocusNames=At1g04110 {ECO:0000312|Araport:AT1G04110};
ORFNames=F20D22.12 {ECO:0000303|PubMed:11130712};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
PubMed=10809670; DOI=10.1101/gad.14.9.1119;
Berger D., Altmann T.;
"A subtilisin-like serine protease involved in the regulation of
stomatal density and distribution in Arabidopsis thaliana.";
Genes Dev. 14:1119-1131(2000).
[4]
FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND PROBABLE SUBCELLULAR
LOCATION.
STRAIN=cv. C24;
PubMed=12119372; DOI=10.1105/tpc.001016;
Von Groll U., Berger D., Altmann T.;
"The subtilisin-like serine protease SDD1 mediates cell-to-cell
signaling during Arabidopsis stomatal development.";
Plant Cell 14:1527-1539(2002).
[5]
DISRUPTION PHENOTYPE.
PubMed=12554730; DOI=10.1093/jxb/erg087;
Schlueter U., Muschak M., Berger D., Altmann T.;
"Photosynthetic performance of an Arabidopsis mutant with elevated
stomatal density (sdd1-1) under different light regimes.";
J. Exp. Bot. 54:867-874(2003).
[6]
GENE FAMILY, AND NOMENCLATURE.
PubMed=16193095; DOI=10.1371/journal.pcbi.0010040;
Rautengarten C., Steinhauser D., Bussis D., Stintzi A., Schaller A.,
Kopka J., Altmann T.;
"Inferring hypotheses on functional relationships of genes: Analysis
of the Arabidopsis thaliana subtilase gene family.";
PLoS Comput. Biol. 1:E40-E40(2005).
[7]
REVIEW.
PubMed=18266617; DOI=10.1111/j.1469-8137.2007.02351.x;
Casson S., Gray J.E.;
"Influence of environmental factors on stomatal development.";
New Phytol. 178:9-23(2008).
[8]
REVIEW.
PubMed=19565615; DOI=10.1002/bies.200800231;
Serna L.;
"Cell fate transitions during stomatal development.";
Bioessays 31:865-873(2009).
[9]
FUNCTION.
STRAIN=cv. Columbia;
PubMed=20056678; DOI=10.1242/dev.040931;
Abrash E.B., Bergmann D.C.;
"Regional specification of stomatal production by the putative ligand
CHALLAH.";
Development 137:447-455(2010).
[10]
FUNCTION, AND INDUCTION BY GTL1.
STRAIN=cv. Columbia;
PubMed=21169508; DOI=10.1105/tpc.110.078691;
Yoo C.Y., Pence H.E., Jin J.B., Miura K., Gosney M.J., Hasegawa P.M.,
Mickelbart M.V.;
"The Arabidopsis GTL1 transcription factor regulates water use
efficiency and drought tolerance by modulating stomatal density via
transrepression of SDD1.";
Plant Cell 22:4128-4141(2010).
-!- FUNCTION: Serine protease involved in the negative regulation of
stomatal density and distribution. Not active on EPFL6 (AC Q1PEY6)
(PubMed:20056678). Positive regulator of water use efficiency
(WUE). {ECO:0000269|PubMed:10809670, ECO:0000269|PubMed:12119372,
ECO:0000269|PubMed:20056678, ECO:0000269|PubMed:21169508}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
{ECO:0000305}. Cell membrane {ECO:0000305}; Peripheral membrane
protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Mostly expressed in leaves and cotyledons
(especially in epidermal cells), and, to a lower extent, in floral
buds, stems, and siliques. Strongly expressed in stomatal
precursor cells (meristemoids and guard mother cells).
{ECO:0000269|PubMed:10809670, ECO:0000269|PubMed:12119372}.
-!- INDUCTION: Negatively feedback controlled by components of an
SDD1-dependent signaling pathway. Repressed by GTL1.
{ECO:0000269|PubMed:12119372, ECO:0000269|PubMed:21169508}.
-!- DISRUPTION PHENOTYPE: Increased stomatal density and formation of
clustered stomata by enhanced stomatal development initiation and
extension of stomatal cell lineages. No major impact on
photosynthesis, except 30% higher CO2 assimilation rates in low-
light-adapted plants exposed to high light intensities.
{ECO:0000269|PubMed:10809670, ECO:0000269|PubMed:12554730}.
-!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AC002411; AAC16749.1; -; Genomic_DNA.
EMBL; CP002684; AEE27657.1; -; Genomic_DNA.
PIR; T00962; T00962.
RefSeq; NP_563701.1; NM_100292.2.
UniGene; At.65883; -.
ProteinModelPortal; O64495; -.
SMR; O64495; -.
STRING; 3702.AT1G04110.1; -.
MEROPS; S08.084; -.
PaxDb; O64495; -.
EnsemblPlants; AT1G04110.1; AT1G04110.1; AT1G04110.
GeneID; 839287; -.
Gramene; AT1G04110.1; AT1G04110.1; AT1G04110.
KEGG; ath:AT1G04110; -.
Araport; AT1G04110; -.
TAIR; locus:2020245; AT1G04110.
eggNOG; ENOG410IEU2; Eukaryota.
eggNOG; COG1404; LUCA.
HOGENOM; HOG000238262; -.
InParanoid; O64495; -.
OMA; EMITRRV; -.
OrthoDB; EOG09360306; -.
PhylomeDB; O64495; -.
PRO; PR:O64495; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; O64495; differential.
Genevisible; O64495; AT.
GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
GO; GO:0009897; C:external side of plasma membrane; IDA:TAIR.
GO; GO:0004252; F:serine-type endopeptidase activity; ISS:TAIR.
GO; GO:0042127; P:regulation of cell proliferation; IMP:TAIR.
GO; GO:0010103; P:stomatal complex morphogenesis; IMP:TAIR.
CDD; cd04852; Peptidases_S8_3; 1.
Gene3D; 3.30.70.80; -; 1.
Gene3D; 3.40.50.200; -; 2.
InterPro; IPR003137; PA_domain.
InterPro; IPR000209; Peptidase_S8/S53_dom.
InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
InterPro; IPR023828; Peptidase_S8_Ser-AS.
InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
InterPro; IPR034197; Peptidases_S8_3.
InterPro; IPR010259; S8pro/Inhibitor_I9.
InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
Pfam; PF05922; Inhibitor_I9; 1.
Pfam; PF02225; PA; 1.
Pfam; PF00082; Peptidase_S8; 1.
PRINTS; PR00723; SUBTILISIN.
SUPFAM; SSF52743; SSF52743; 2.
PROSITE; PS00138; SUBTILASE_SER; 1.
2: Evidence at transcript level;
Apoplast; Cell membrane; Complete proteome; Glycoprotein; Hydrolase;
Membrane; Protease; Reference proteome; Secreted; Serine protease;
Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 775 Subtilisin-like protease SBT1.2.
/FTId=PRO_0000405797.
DOMAIN 127 587 Peptidase S8.
DOMAIN 388 470 PA.
ACT_SITE 146 146 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10082}.
ACT_SITE 222 222 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10082}.
ACT_SITE 552 552 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU10082}.
CARBOHYD 472 472 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 544 544 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 652 652 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 775 AA; 83776 MW; 7740B20397C7C211 CRC64;
MEPKPFFLCI IFLLFCSSSS EILQKQTYIV QLHPNSETAK TFASKFDWHL SFLQEAVLGV
EEEEEEPSSR LLYSYGSAIE GFAAQLTESE AEILRYSPEV VAVRPDHVLQ VQTTYSYKFL
GLDGFGNSGV WSKSRFGQGT IIGVLDTGVW PESPSFDDTG MPSIPRKWKG ICQEGESFSS
SSCNRKLIGA RFFIRGHRVA NSPEESPNMP REYISARDST GHGTHTASTV GGSSVSMANV
LGNGAGVARG MAPGAHIAVY KVCWFNGCYS SDILAAIDVA IQDKVDVLSL SLGGFPIPLY
DDTIAIGTFR AMERGISVIC AAGNNGPIES SVANTAPWVS TIGAGTLDRR FPAVVRLANG
KLLYGESLYP GKGIKNAGRE VEVIYVTGGD KGSEFCLRGS LPREEIRGKM VICDRGVNGR
SEKGEAVKEA GGVAMILANT EINQEEDSID VHLLPATLIG YTESVLLKAY VNATVKPKAR
IIFGGTVIGR SRAPEVAQFS ARGPSLANPS ILKPDMIAPG VNIIAAWPQN LGPTGLPYDS
RRVNFTVMSG TSMSCPHVSG ITALIRSAYP NWSPAAIKSA LMTTADLYDR QGKAIKDGNK
PAGVFAIGAG HVNPQKAINP GLVYNIQPVD YITYLCTLGF TRSDILAITH KNVSCNGILR
KNPGFSLNYP SIAVIFKRGK TTEMITRRVT NVGSPNSIYS VNVKAPEGIK VIVNPKRLVF
KHVDQTLSYR VWFVLKKKNR GGKVASFAQG QLTWVNSHNL MQRVRSPISV TLKTN


Related products :

Catalog number Product name Quantity
EIAAB40101 Homo sapiens,Human,Matriptase,Membrane-type serine protease 1,MT-SP1,Prostamin,PRSS14,Serine protease 14,Serine protease TADG-15,SNC19,ST14,Suppressor of tumorigenicity 14 protein,TADG15,Tumor-associa
EIAAB32605 Disp,Distal intestinal serine protease,Prss30,Rat,Rattus norvegicus,Serine protease 30,Tmprss8,Tmsp1,TMSP-1,Tmsp-1,Transmembrane serine protease 1,Transmembrane serine protease 8
U2234h CLIA kit Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
U2234h CLIA Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
E2234h ELISA Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
E2234h ELISA kit Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
E2234r ELISA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
U2234r CLIA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
E2234m ELISA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
U2234m CLIA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234m ELISA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
U2234r CLIA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
U2234m CLIA Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus 96T
E2234r ELISA kit Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus 96T
E2234h Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2
EIAAB32606 Disp,Distal intestinal serine protease,Mouse,Mus musculus,Prss30,Serine protease 30,Tmprss8,Transmembrane serine protease 8
E2234r Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Rat,Rattus norvegicus
E2234m Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,Masp2,MASP-2,MBL-associated serine protease 2,Mouse,Mus musculus
E0691h ELISA Homo sapiens,Human,Kallikrein-6,KLK6,Neurosin,Protease M,PRSS18,PRSS9,Serine protease 18,Serine protease 9,SP59,Zyme 96T
E0691h ELISA kit Homo sapiens,Human,Kallikrein-6,KLK6,Neurosin,Protease M,PRSS18,PRSS9,Serine protease 18,Serine protease 9,SP59,Zyme 96T
U0691h CLIA Homo sapiens,Human,Kallikrein-6,KLK6,Neurosin,Protease M,PRSS18,PRSS9,Serine protease 18,Serine protease 9,SP59,Zyme 96T
EIAAB42592 Adrenal secretory serine protease,Airway trypsin-like protease,AsP,AT,Mat,Mouse,Mus musculus,Tmprss11d,Transmembrane protease serine 11D
EIAAB42593 Adrenal secretory serine protease,Airway trypsin-like protease,AsP,AT,Rat,Rat,Rattus norvegicus,Tmprss11d,Transmembrane protease serine 11D
30-350 ST14 is an epithelial-derived, integral membrane serine protease. This protease forms a complex with the Kunitz-type serine protease inhibitor, HAI-1, and is found to be activated by sphingosine 1-pho 0.05 mg
EIAAB43231 CAPH2,Channel-activating protease 2,Homo sapiens,Human,Membrane-type serine protease 2,MT-SP2,TMPRSS3,TMPRSS4,Transmembrane protease serine 4,UNQ776_PRO1570


 

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