Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Calponin-1

Gene

CNN1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Calponin-1
Alternative name(s):
Calponin, smooth muscle
Gene namesi
Name:CNN1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292Calponin-1PRO_0000204771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei170 – 1701Phosphothreonine; by ROCK21 Publication
Modified residuei175 – 1751Phosphoserine; by PKC, CaMK2 and ROCK22 Publications
Modified residuei180 – 1801Phosphothreonine; by ROCK21 Publication
Modified residuei184 – 1841Phosphothreonine; by PKC and CaMK22 Publications
Modified residuei184 – 1841Phosphothreonine; by ROCK22 Publications
Modified residuei259 – 2591Phosphothreonine; by ROCK21 Publication

Post-translational modificationi

Phosphorylation by PKC or CaM kinase II reduces the binding of calponin to F-actin and tropomyosin.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP26932.

PTM databases

iPTMnetiP26932.

Expressioni

Tissue specificityi

Smooth muscle, and tissues containing significant amounts of smooth muscle.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTA1P681355EBI-8602797,EBI-367540From a different organism.

Protein-protein interaction databases

IntActiP26932. 1 interaction.
MINTiMINT-2880197.

Structurei

Secondary structure

1
292
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 4211Combined sources
Helixi50 – 567Combined sources
Helixi59 – 679Combined sources
Helixi82 – 9817Combined sources
Helixi102 – 1043Combined sources
Helixi108 – 1136Combined sources
Helixi118 – 13316Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H67NMR-A28-134[»]
ProteinModelPortaliP26932.
SMRiP26932. Positions 13-150.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26932.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 131104CHPROSITE-ProRule annotationAdd
BLAST
Repeati164 – 18926Calponin-like 1Add
BLAST
Repeati204 – 22926Calponin-like 2Add
BLAST
Repeati243 – 26826Calponin-like 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni185 – 1939Calmodulin-bindingCurated

Sequence similaritiesi

Belongs to the calponin family.Curated
Contains 3 calponin-like repeats.PROSITE-ProRule annotation
Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOVERGENiHBG005186.
InParanoidiP26932.
PhylomeDBiP26932.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001997. Calponin/LIMCH1.
IPR000557. Calponin_repeat.
IPR001715. CH-domain.
IPR003096. SM22_calponin.
[Graphical view]
PfamiPF00402. Calponin. 3 hits.
PF00307. CH. 1 hit.
[Graphical view]
PRINTSiPR00889. CALPONIN.
PR00888. SM22CALPONIN.
SMARTiSM00033. CH. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS01052. CALPONIN_1. 3 hits.
PS51122. CALPONIN_2. 3 hits.
PS50021. CH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Alpha (identifier: P26932-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSNANFNRGP AYGLSAEVKN KLAQKYDPQT ERQLRVWIEG ATGRRIGDNF
60 70 80 90 100
MDGLKDGVIL CELINKLQPG SVQKVNDPVQ NWHKLENIGN FLRAIKHYGV
110 120 130 140 150
KPHDIFEAND LFENTNHTQV QSTLIALASQ AKTKGNNVGL GVKYAEKQQR
160 170 180 190 200
RFQPEKLREG RNIIGLQMGT NKFASQQGMT AYGTRRHLYD PKLGTDQPLD
210 220 230 240 250
QATISLQMGT NKGASQAGMT APGTKRQIFE PSLGMERCDT NIIGLQMGSN
260 270 280 290
KGASQQGMTV YGLPRQVYDP KYCDAPGLLG EDGLNHSFYN SQ
Length:292
Mass (Da):32,361
Last modified:September 19, 2003 - v2
Checksum:iA80E55FE5966DAC6
GO
Isoform Beta (identifier: P26932-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     217-256: Missing.

Show »
Length:252
Mass (Da):28,154
Checksum:i10E36CD5D211DB0B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661K → T in AAA48651 (PubMed:2071603).Curated
Sequence conflicti66 – 661K → T in AAA48652 (PubMed:2071603).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei217 – 25640Missing in isoform Beta. CuratedVSP_000756Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63559 mRNA. Translation: AAA48651.1.
M63560 mRNA. Translation: AAA48652.1.
PIRiA39871.
RefSeqiNP_990847.1. NM_205516.1.
UniGeneiGga.873.

Genome annotation databases

GeneIDi396522.
KEGGigga:396522.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M63559 mRNA. Translation: AAA48651.1.
M63560 mRNA. Translation: AAA48652.1.
PIRiA39871.
RefSeqiNP_990847.1. NM_205516.1.
UniGeneiGga.873.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H67NMR-A28-134[»]
ProteinModelPortaliP26932.
SMRiP26932. Positions 13-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP26932. 1 interaction.
MINTiMINT-2880197.

PTM databases

iPTMnetiP26932.

Proteomic databases

PRIDEiP26932.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396522.
KEGGigga:396522.

Organism-specific databases

CTDi1264.

Phylogenomic databases

HOVERGENiHBG005186.
InParanoidiP26932.
PhylomeDBiP26932.

Miscellaneous databases

EvolutionaryTraceiP26932.
NextBioi20816559.
PROiP26932.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
InterProiIPR001997. Calponin/LIMCH1.
IPR000557. Calponin_repeat.
IPR001715. CH-domain.
IPR003096. SM22_calponin.
[Graphical view]
PfamiPF00402. Calponin. 3 hits.
PF00307. CH. 1 hit.
[Graphical view]
PRINTSiPR00889. CALPONIN.
PR00888. SM22CALPONIN.
SMARTiSM00033. CH. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS01052. CALPONIN_1. 3 hits.
PS51122. CALPONIN_2. 3 hits.
PS50021. CH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular cloning and sequence analysis of smooth muscle calponin."
    Takahashi K., Nadal-Ginard B.
    J. Biol. Chem. 266:13284-13288(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Gizzard smooth muscle.
  2. "Calponin: thin filament-linked regulation of smooth muscle contraction."
    Winder S.J., Walsh M.P.
    Cell. Signal. 5:677-686(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Gizzard smooth muscle.
  3. "Mapping of the functional domains in the amino-terminal region of calponin."
    Mezgueldi M., Fattoum A., Derancourt J., Kassab R.
    J. Biol. Chem. 267:15943-15951(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 7-21; 52-66 AND 183-194.
  4. Cited for: PROTEIN SEQUENCE OF 157-192 AND 252-271, PHOSPHORYLATION AT THR-170; SER-175; THR-180; THR-184 AND THR-259.
  5. "Characterization of wild type and mutant chicken gizzard alpha calponin expressed in E. coli."
    Gong B.J., Mabuchi K., Takahashi K., Nadal-Ginard B., Tao T.
    J. Biochem. 114:453-456(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, MUTAGENESIS.
  6. "Calponin phosphorylation in vitro and in intact muscle."
    Winder S.J., Allen B.G., Fraser E.D., Kang H.M., Kargacin G.J., Walsh M.P.
    Biochem. J. 296:827-836(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-175.
  7. "Identification of the regulatory site in smooth muscle calponin that is phosphorylated by protein kinase C."
    Nakamura F., Mino T., Yamamoto J., Naka M., Tanaka T.
    J. Biol. Chem. 268:6194-6201(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-184.
  8. "Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin:calponin."
    Bramham J., Hodgkinson J.L., Smith B.O., Uhrin D., Barlow P.N., Winder S.J.
    Structure 10:249-258(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 27-134.

Entry informationi

Entry nameiCNN1_CHICK
AccessioniPrimary (citable) accession number: P26932
Secondary accession number(s): P26933, Q9PSG0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: September 19, 2003
Last modified: January 20, 2016
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.