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Protein

Smoothelin-like protein 1

Gene

Smtnl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

GO - Biological processi

  • muscle organ morphogenesis Source: MGI
  • negative regulation of transcription, DNA-templated Source: CACAO
  • negative regulation of vasodilation Source: UniProtKB
  • peptidyl-serine phosphorylation Source: MGI
  • positive regulation of vasoconstriction Source: UniProtKB
  • response to activity Source: MGI
  • response to drug Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Smoothelin-like protein 1
Alternative name(s):
Calponin homology-associated smooth muscle protein
Short name:
CHASM
Gene namesi
Name:Smtnl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1915928. Smtnl1.

Subcellular locationi

GO - Cellular componenti

  • contractile fiber Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • I band Source: MGI
  • M band Source: MGI
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi301 – 3011S → A: Loss of phosphorylation. Loss of nuclear localization. 3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 459459Smoothelin-like protein 1PRO_0000317276Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei301 – 3011Phosphoserine; by PKA and PKG3 Publications

Post-translational modificationi

Maximal phosphorylation of Ser-301 correlates with maximal relaxation of aorta in response to acetylcholine.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ99LM3.
PeptideAtlasiQ99LM3.
PRIDEiQ99LM3.

PTM databases

iPTMnetiQ99LM3.
PhosphoSiteiQ99LM3.

Expressioni

Tissue specificityi

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.2 Publications

Developmental stagei

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).2 Publications

Inductioni

Signficantly reduced by exercise in smooth and in skeletal muscles.1 Publication

Gene expression databases

BgeeiQ99LM3.
CleanExiMM_SMTNL1.
GenevisibleiQ99LM3. MM.

Interactioni

Subunit structurei

Interacts with PPP1R12A.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TPM1P042683EBI-8073484,EBI-8073544From a different organism.

GO - Molecular functioni

  • protein phosphatase 1 binding Source: UniProtKB

Protein-protein interaction databases

IntActiQ99LM3. 4 interactions.
MINTiMINT-7966054.
STRINGi10090.ENSMUSP00000028471.

Structurei

Secondary structure

1
459
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi346 – 35712Combined sources
Beta strandi360 – 3623Combined sources
Helixi370 – 3723Combined sources
Helixi376 – 3838Combined sources
Beta strandi387 – 3893Combined sources
Helixi392 – 3943Combined sources
Helixi397 – 3993Combined sources
Helixi400 – 41516Combined sources
Helixi423 – 4297Combined sources
Helixi434 – 45118Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JV9NMR-A346-459[»]
2K3SNMR-A346-459[»]
DisProtiDP00742.
ProteinModelPortaliQ99LM3.
SMRiQ99LM3. Positions 344-459.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99LM3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini343 – 446104CHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni441 – 45919Calmodulin-bindingAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili124 – 15431Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the smoothelin family.Curated
Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4678. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118856.
HOGENOMiHOG000154352.
HOVERGENiHBG095368.
InParanoidiQ99LM3.
OMAiCAQLLDV.
OrthoDBiEOG7C2R13.
PhylomeDBiQ99LM3.
TreeFamiTF316716.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001715. CH-domain.
[Graphical view]
PfamiPF00307. CH. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS50021. CH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99LM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQTEGNSSE DGTTVSPTAG NLETPGSQGI AEEVAEGTVG TSDKEGPSDW
60 70 80 90 100
AEHLCKAASK SGESGGSPGE ASILDELKTD LQGEARGKDE AQGDLAEEKV
110 120 130 140 150
GKEDTTAASQ EDTGKKEETK PEPNEVREKE EAMLASEKQK VDEKETNLES
160 170 180 190 200
KEKSDVNDKA KPEPKEDAGA EVTVNEAETE SQEEADVKDQ AKPELPEVDG
210 220 230 240 250
KETGSDTKEL VEPESPTEEQ EQGKENESEE RAAVIPSSPE EWPESPTDEG
260 270 280 290 300
PSLSPDGLAP ESTGETSPSA SESSPSEVPG SPTEPQPSEK KKDRAPERRV
310 320 330 340 350
SAPSRPRGPR AQNRKAIMDK FGGAASGPTA LFRNTKAAGA AIGGVKNMLL
360 370 380 390 400
EWCRAMTRNY EHVDIQNFSS SWSSGMAFCA LIHKFFPEAF DYAELDPAKR
410 420 430 440 450
RHNFTLAFST AEKLADCAQL LEVDDMVRLA VPDSKCVYTY IQELYRSLVQ

KGLVKTKKK
Length:459
Mass (Da):49,525
Last modified:June 1, 2001 - v1
Checksum:i9E86D60605B7F28D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL928914 Genomic DNA. Translation: CAM23315.1.
BC002317 mRNA. Translation: AAH02317.1.
CCDSiCCDS16195.1.
RefSeqiNP_077192.1. NM_024230.2.
XP_006500172.1. XM_006500109.2.
UniGeneiMm.33452.

Genome annotation databases

EnsembliENSMUST00000028471; ENSMUSP00000028471; ENSMUSG00000027077.
GeneIDi68678.
KEGGimmu:68678.
UCSCiuc008kjg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL928914 Genomic DNA. Translation: CAM23315.1.
BC002317 mRNA. Translation: AAH02317.1.
CCDSiCCDS16195.1.
RefSeqiNP_077192.1. NM_024230.2.
XP_006500172.1. XM_006500109.2.
UniGeneiMm.33452.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JV9NMR-A346-459[»]
2K3SNMR-A346-459[»]
DisProtiDP00742.
ProteinModelPortaliQ99LM3.
SMRiQ99LM3. Positions 344-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99LM3. 4 interactions.
MINTiMINT-7966054.
STRINGi10090.ENSMUSP00000028471.

PTM databases

iPTMnetiQ99LM3.
PhosphoSiteiQ99LM3.

Proteomic databases

PaxDbiQ99LM3.
PeptideAtlasiQ99LM3.
PRIDEiQ99LM3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028471; ENSMUSP00000028471; ENSMUSG00000027077.
GeneIDi68678.
KEGGimmu:68678.
UCSCiuc008kjg.1. mouse.

Organism-specific databases

CTDi219537.
MGIiMGI:1915928. Smtnl1.

Phylogenomic databases

eggNOGiKOG4678. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118856.
HOGENOMiHOG000154352.
HOVERGENiHBG095368.
InParanoidiQ99LM3.
OMAiCAQLLDV.
OrthoDBiEOG7C2R13.
PhylomeDBiQ99LM3.
TreeFamiTF316716.

Miscellaneous databases

EvolutionaryTraceiQ99LM3.
PROiQ99LM3.
SOURCEiSearch...

Gene expression databases

BgeeiQ99LM3.
CleanExiMM_SMTNL1.
GenevisibleiQ99LM3. MM.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001715. CH-domain.
[Graphical view]
PfamiPF00307. CH. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS50021. CH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "Modulation of smooth muscle contractility by CHASM, a novel member of the smoothelin family of proteins."
    Borman M.A., MacDonald J.A., Haystead T.A.
    FEBS Lett. 573:207-213(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-301, MUTAGENESIS OF SER-301.
  4. "Deletion of the protein kinase A/protein kinase G target SMTNL1 promotes an exercise-adapted phenotype in vascular smooth muscle."
    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.
    J. Biol. Chem. 283:11850-11859(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT SER-301, DISRUPTION PHENOTYPE, INDUCTION, MUTAGENESIS OF SER-301.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue and Lung.
  6. "Smoothelin-like 1 protein regulates myosin phosphatase-targeting subunit 1 expression during sexual development and pregnancy."
    Lontay B., Bodoor K., Weitzel D.H., Loiselle D., Fortner C., Lengyel S., Zheng D., Devente J., Hickner R., Haystead T.A.
    J. Biol. Chem. 285:29357-29366(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PPP1R12A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-301, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-301.
  7. "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."
    Ishida H., Borman M.A., Ostrander J., Vogel H.J., MacDonald J.A.
    J. Biol. Chem. 283:20569-20578(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 346-459, CALMODULIN BINDING.

Entry informationi

Entry nameiSMTL1_MOUSE
AccessioniPrimary (citable) accession number: Q99LM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.