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

Smoothelin-like protein 1 (Calponin homology-associated smooth muscle protein) (CHASM)

 SMTL1_MOUSE             Reviewed;         459 AA.
Q99LM3;
05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
12-SEP-2018, entry version 121.
RecName: Full=Smoothelin-like protein 1;
AltName: Full=Calponin homology-associated smooth muscle protein;
Short=CHASM;
Name=Smtnl1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
[3]
PHOSPHORYLATION AT SER-301, AND MUTAGENESIS OF SER-301.
PubMed=15327999; DOI=10.1016/j.febslet.2004.08.002;
Borman M.A., MacDonald J.A., Haystead T.A.;
"Modulation of smooth muscle contractility by CHASM, a novel member of
the smoothelin family of proteins.";
FEBS Lett. 573:207-213(2004).
[4]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, PHOSPHORYLATION AT SER-301, DISRUPTION PHENOTYPE, INDUCTION,
AND MUTAGENESIS OF SER-301.
PubMed=18310078; DOI=10.1074/jbc.M708628200;
Wooldridge A.A., Fortner C.N., Lontay B., Akimoto T., Neppl R.L.,
Facemire C., Datto M.B., Kwon A., McCook E., Li P., Wang S.,
Thresher R.J., Miller S.E., Perriard J.C., Gavin T.P., Hickner R.C.,
Coffman T.M., Somlyo A.V., Yan Z., Haystead T.A.;
"Deletion of the protein kinase A/protein kinase G target SMTNL1
promotes an exercise-adapted phenotype in vascular smooth muscle.";
J. Biol. Chem. 283:11850-11859(2008).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION, INTERACTION WITH PPP1R12A, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, PHOSPHORYLATION AT SER-301, DEVELOPMENTAL STAGE,
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF SER-301.
PubMed=20634291; DOI=10.1074/jbc.M110.143966;
Lontay B., Bodoor K., Weitzel D.H., Loiselle D., Fortner C.,
Lengyel S., Zheng D., Devente J., Hickner R., Haystead T.A.;
"Smoothelin-like 1 protein regulates myosin phosphatase-targeting
subunit 1 expression during sexual development and pregnancy.";
J. Biol. Chem. 285:29357-29366(2010).
[7]
STRUCTURE BY NMR OF 346-459, AND CALMODULIN BINDING.
PubMed=18477568; DOI=10.1074/jbc.M800627200;
Ishida H., Borman M.A., Ostrander J., Vogel H.J., MacDonald J.A.;
"Solution structure of the calponin homology (CH) domain from the
smoothelin-like 1 protein: a unique apocalmodulin-binding mode and the
possible role of the C-terminal type-2 CH-domain in smooth muscle
relaxation.";
J. Biol. Chem. 283:20569-20578(2008).
-!- FUNCTION: Plays a role in the regulation of contractile properties
of both striated and smooth muscles. When unphosphorylated, may
inhibit myosin dephosphorylation. Phosphorylation at Ser-301
reduces this inhibitory activity. {ECO:0000269|PubMed:18310078,
ECO:0000269|PubMed:20634291}.
-!- SUBUNIT: Interacts with PPP1R12A. {ECO:0000269|PubMed:20634291}.
-!- INTERACTION:
P04268:TPM1 (xeno); NbExp=3; IntAct=EBI-8073484, EBI-8073544;
-!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band.
Cytoplasm, myofibril, sarcomere, M line. Nucleus. Note=Colocalizes
with MYH2. In its unphosphorylated state, localizes to the
cytoplasm. Phosphorylation at Ser-301 promotes translocation to
the nucleus.
-!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
skeletal muscles (at protein level). Within striated muscles,
significantly more expressed in soleus muscle compared with
plantaris muscle or white vastus (at protein level). 30-40% lower
expression in females than in males (at protein level). Expressed
in type 2a fibers, but not detected in fast twitch type 2b muscle
white vastus nor in oxidative type I/b heart muscle (at protein
level). Expressed within myometrial cells of the uterus, as well
as in the endometrial layer. In the aorta, confined to smooth
muscle cells. Not detected in endothelial cells.
{ECO:0000269|PubMed:18310078, ECO:0000269|PubMed:20634291}.
-!- DEVELOPMENTAL STAGE: Not detected in somites which give rise to
skeletal muscle at 10.5 dpc (at protein level). Expressed in
skeletal muscle of the tongue, diaphragm and axial muscles from
14.5 through 17.5 dpc (at protein level). Not detected in limb
buds (at protein level). Overall increase by up to 10-12-fold in
vascular and uterine smooth muscle during pregnancy (at protein
level). At day 13 of pregnancy, expression increases in striated
muscle by 2.5-fold compared with non-pregnant mice, and by about
2-fold over levels expressed in males (at protein level). At the
same time, dramatically increased in myometrial cells of the
uterus, in the endometrial layer and in aortal smooth muscle.
Steadily declines through parturition and the onset of lactation
(at protein level). {ECO:0000269|PubMed:18310078,
ECO:0000269|PubMed:20634291}.
-!- INDUCTION: Signficantly reduced by exercise in smooth and in
skeletal muscles. {ECO:0000269|PubMed:18310078}.
-!- PTM: Maximal phosphorylation of Ser-301 correlates with maximal
relaxation of aorta in response to acetylcholine.
{ECO:0000269|PubMed:15327999, ECO:0000269|PubMed:18310078,
ECO:0000269|PubMed:20634291}.
-!- DISRUPTION PHENOTYPE: Male mutant mice perform better than wild
type in exercise stress test after endurance training. Females do
not differ significantly during these tests. Even in the absence
of endurance exercise, mutant mice exhibit muscle fiber
adaptation, i.e. more type 2a fibers and lower levels of type 1b
fibers. Endothelium-dependent vasorelaxation of the aorta is
enhanced and responses to beta-adrenergic constriction are
reduced. Expression of PPP1R12A is 30-40-fold higher in mutant
mice than in wild-type littermates and exhibits a steady decline
as the animals become sexually mature (at protein level). During
pregnancy, by day 13, PPP1R12A expression is dramatically
increased to 6-14 times over the levels observed in pregnant wild-
type littermates (at protein level). PPP1R12B expression levels
are unaffected. In vascular smooth muscle, force development in
response to phenylephrine is reduced and both the rate and extent
of relaxation in response to acetylcholine are promoted. Myosin
dephosphorylation is promoted in mutant animals.
{ECO:0000269|PubMed:18310078, ECO:0000269|PubMed:20634291}.
-!- SIMILARITY: Belongs to the smoothelin 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; AL928914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002317; AAH02317.1; -; mRNA.
CCDS; CCDS16195.1; -.
RefSeq; NP_077192.1; NM_024230.2.
RefSeq; XP_006500172.1; XM_006500109.3.
UniGene; Mm.33452; -.
PDB; 2JV9; NMR; -; A=346-459.
PDB; 2K3S; NMR; -; A=346-459.
PDBsum; 2JV9; -.
PDBsum; 2K3S; -.
DisProt; DP00742; -.
ProteinModelPortal; Q99LM3; -.
SMR; Q99LM3; -.
IntAct; Q99LM3; 4.
MINT; Q99LM3; -.
STRING; 10090.ENSMUSP00000028471; -.
iPTMnet; Q99LM3; -.
PhosphoSitePlus; Q99LM3; -.
PaxDb; Q99LM3; -.
PeptideAtlas; Q99LM3; -.
PRIDE; Q99LM3; -.
Ensembl; ENSMUST00000028471; ENSMUSP00000028471; ENSMUSG00000027077.
GeneID; 68678; -.
KEGG; mmu:68678; -.
UCSC; uc008kjg.1; mouse.
CTD; 219537; -.
MGI; MGI:1915928; Smtnl1.
eggNOG; KOG4678; Eukaryota.
eggNOG; COG5069; LUCA.
GeneTree; ENSGT00760000118856; -.
HOGENOM; HOG000154352; -.
HOVERGEN; HBG095368; -.
InParanoid; Q99LM3; -.
OMA; LEWCRAM; -.
OrthoDB; EOG091G0YLR; -.
PhylomeDB; Q99LM3; -.
TreeFam; TF316716; -.
EvolutionaryTrace; Q99LM3; -.
PRO; PR:Q99LM3; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027077; Expressed in 49 organ(s), highest expression level in tarsal region.
CleanEx; MM_SMTNL1; -.
Genevisible; Q99LM3; MM.
GO; GO:0043292; C:contractile fiber; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031674; C:I band; IDA:MGI.
GO; GO:0031430; C:M band; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IPI:CAFA.
GO; GO:0051401; F:CH domain binding; IPI:CAFA.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0017020; F:myosin phosphatase regulator activity; ISO:MGI.
GO; GO:0008157; F:protein phosphatase 1 binding; IPI:UniProtKB.
GO; GO:0004864; F:protein phosphatase inhibitor activity; ISO:MGI.
GO; GO:0043621; F:protein self-association; IDA:CAFA.
GO; GO:0005523; F:tropomyosin binding; IPI:CAFA.
GO; GO:0048644; P:muscle organ morphogenesis; IMP:MGI.
GO; GO:0097756; P:negative regulation of blood vessel diameter; IMP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:CACAO.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
GO; GO:0045907; P:positive regulation of vasoconstriction; IMP:UniProtKB.
GO; GO:0014823; P:response to activity; IMP:MGI.
GO; GO:0042493; P:response to drug; IDA:MGI.
CDD; cd00014; CH; 1.
Gene3D; 1.10.418.10; -; 1.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
Pfam; PF00307; CH; 1.
SMART; SM00033; CH; 1.
SUPFAM; SSF47576; SSF47576; 1.
PROSITE; PS50021; CH; 1.
1: Evidence at protein level;
3D-structure; Calmodulin-binding; Coiled coil; Complete proteome;
Cytoplasm; Muscle protein; Nucleus; Phosphoprotein;
Reference proteome.
CHAIN 1 459 Smoothelin-like protein 1.
/FTId=PRO_0000317276.
DOMAIN 343 449 Calponin-homology (CH).
{ECO:0000255|PROSITE-ProRule:PRU00044}.
REGION 441 459 Calmodulin-binding.
COILED 124 154 {ECO:0000255}.
MOD_RES 301 301 Phosphoserine; by PKA and PKG.
{ECO:0000269|PubMed:15327999,
ECO:0000269|PubMed:18310078,
ECO:0000269|PubMed:20634291}.
MUTAGEN 301 301 S->A: Loss of phosphorylation. Loss of
nuclear localization.
{ECO:0000269|PubMed:15327999,
ECO:0000269|PubMed:18310078,
ECO:0000269|PubMed:20634291}.
HELIX 346 357 {ECO:0000244|PDB:2JV9}.
STRAND 360 362 {ECO:0000244|PDB:2JV9}.
HELIX 370 372 {ECO:0000244|PDB:2JV9}.
HELIX 376 383 {ECO:0000244|PDB:2JV9}.
STRAND 387 389 {ECO:0000244|PDB:2JV9}.
HELIX 392 394 {ECO:0000244|PDB:2JV9}.
HELIX 397 399 {ECO:0000244|PDB:2K3S}.
HELIX 400 415 {ECO:0000244|PDB:2JV9}.
HELIX 423 429 {ECO:0000244|PDB:2JV9}.
HELIX 434 451 {ECO:0000244|PDB:2JV9}.
SEQUENCE 459 AA; 49525 MW; 9E86D60605B7F28D CRC64;
MEQTEGNSSE DGTTVSPTAG NLETPGSQGI AEEVAEGTVG TSDKEGPSDW AEHLCKAASK
SGESGGSPGE ASILDELKTD LQGEARGKDE AQGDLAEEKV GKEDTTAASQ EDTGKKEETK
PEPNEVREKE EAMLASEKQK VDEKETNLES KEKSDVNDKA KPEPKEDAGA EVTVNEAETE
SQEEADVKDQ AKPELPEVDG KETGSDTKEL VEPESPTEEQ EQGKENESEE RAAVIPSSPE
EWPESPTDEG PSLSPDGLAP ESTGETSPSA SESSPSEVPG SPTEPQPSEK KKDRAPERRV
SAPSRPRGPR AQNRKAIMDK FGGAASGPTA LFRNTKAAGA AIGGVKNMLL EWCRAMTRNY
EHVDIQNFSS SWSSGMAFCA LIHKFFPEAF DYAELDPAKR RHNFTLAFST AEKLADCAQL
LEVDDMVRLA VPDSKCVYTY IQELYRSLVQ KGLVKTKKK


Related products :

Catalog number Product name Quantity
E2278m Calponin homology-associated smooth muscle protein,CHASM,Mouse,Mus musculus,Smoothelin-like protein 1,Smtnl1
E2278m ELISA Calponin homology-associated smooth muscle protein,CHASM,Mouse,Mus musculus,Smoothelin-like protein 1,Smtnl1 96T
U2278m CLIA Calponin homology-associated smooth muscle protein,CHASM,Mouse,Mus musculus,Smoothelin-like protein 1,Smtnl1 96T
U2278m CLIA kit Calponin homology-associated smooth muscle protein,CHASM,Mouse,Mus musculus,Smoothelin-like protein 1,Smtnl1 96T
E2278m ELISA kit Calponin homology-associated smooth muscle protein,CHASM,Mouse,Mus musculus,Smoothelin-like protein 1,Smtnl1 96T
E2278h Human Calponin Homology Associated Smooth Muscle P 96T
EIAAB08216 Calponin H2, smooth muscle,Calponin-2,CNN2,Homo sapiens,Human,Neutral calponin
EIAAB08212 Basic calponin,Calponin H1, smooth muscle,Calponin-1,CNN1,Homo sapiens,Human
EIAAB08214 Basic calponin,Calponin H1, smooth muscle,Calponin-1,Cnn1,Mouse,Mus musculus
EIAAB08213 Basic calponin,Calponin H1, smooth muscle,Calponin-1,Cnn1,Rat,Rattus norvegicus
EIAAB08210 Basic calponin,Bos taurus,Bovine,Calponin H1, smooth muscle,Calponin-1,CNN1
EIAAB08217 Bos taurus,Bovine,Calponin H2, smooth muscle,Calponin-2,CNN2,Neutral calponin
EIAAB08219 Calponin H2, smooth muscle,Calponin-2,Cnn2,Mouse,Mus musculus,Neutral calponin
EIAAB08218 Calponin H2, smooth muscle,Calponin-2,CNN2,Neutral calponin,Pig,Sus scrofa
EIAAB08211 Basic calponin,Calponin H1, smooth muscle,Calponin-1,CNN1,Pig,Sus scrofa
20-272-192067 Calponin - Mouse monoclonal [CALP] to Calponin; Calponin H1. smooth muscle; Basic calponin Monoclonal 0.5 ml
EIAAB10576 CLCP1,CUB, LCCL and coagulation factor V_VIII-homology domains protein 1,DCBLD2,Discoidin, CUB and LCCL domain-containing protein 2,Endothelial and smooth muscle cell-derived neuropilin-like protein,E
18-272-196201 DCBLD2 - Rabbit polyclonal to DCBLD2; Endothelial and smooth muscle cell-derived neuropilin-like protein; CUB. LCCL and coagulation factor V_VIII-homology domains protein 1 Polyclonal 0.05 mg
EIAAB08215 Calponin, smooth muscle,Calponin-1,Chicken,CNN1,Gallus gallus
RPR-129 Recombinant Human Calponin 1, Basic, Smooth Muscle 5
pro-1129 Recombinant Human Calponin 1, Basic, Smooth Muscle 1mg
pro-1129 Recombinant Human Calponin 1, Basic, Smooth Muscle 5
pro-1129 Recombinant Human Calponin 1, Basic, Smooth Muscle 20
CNN3 CNN1 Gene calponin 1, basic, smooth muscle
abx111335 Polyclonal Rabbit Calponin 1, Basic, Smooth Muscle Antibody 50 μl


 

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