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Database: UniProt
Entry: A0A2K5J329_COLAP
LinkDB: A0A2K5J329_COLAP
Original site: A0A2K5J329_COLAP 
ID   A0A2K5J329_COLAP        Unreviewed;       263 AA.
AC   A0A2K5J329;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Calponin {ECO:0000256|RuleBase:RU361224};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000023220.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000023220.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- FUNCTION: Thin filament-associated protein that is implicated in the
CC       regulation and modulation of smooth muscle contraction. It is capable
CC       of binding to actin, calmodulin and tropomyosin. The interaction of
CC       calponin with actin inhibits the actomyosin Mg-ATPase activity.
CC       {ECO:0000256|ARBA:ARBA00025109, ECO:0000256|RuleBase:RU361224}.
CC   -!- SIMILARITY: Belongs to the calponin family.
CC       {ECO:0000256|ARBA:ARBA00009631, ECO:0000256|RuleBase:RU361224}.
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DR   AlphaFoldDB; A0A2K5J329; -.
DR   Ensembl; ENSCANT00000046206.1; ENSCANP00000023220.1; ENSCANG00000035016.1.
DR   OMA; MDRCTIS; -.
DR   Proteomes; UP000233080; Unplaced.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
DR   CDD; cd21283; CH_CNN2; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
DR   InterPro; IPR001997; Calponin/LIMCH1.
DR   InterPro; IPR000557; Calponin_repeat.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR003096; SM22_calponin.
DR   PANTHER; PTHR47385; CALPONIN; 1.
DR   PANTHER; PTHR47385:SF7; CALPONIN-2; 1.
DR   Pfam; PF00402; Calponin; 1.
DR   Pfam; PF00307; CH; 1.
DR   PRINTS; PR00889; CALPONIN.
DR   PRINTS; PR00888; SM22CALPONIN.
DR   SMART; SM00033; CH; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   PROSITE; PS01052; CALPONIN_1; 1.
DR   PROSITE; PS51122; CALPONIN_2; 1.
DR   PROSITE; PS50021; CH; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW   ECO:0000256|RuleBase:RU361224};
KW   Calmodulin-binding {ECO:0000256|RuleBase:RU361224};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233080};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          28..132
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   REGION          230..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   263 AA;  28764 MW;  5E389BC934DBADF4 CRC64;
     MSSTQFNKGP SYGLSAEVKN RLLSKYDPQK EAELRTWMEG PTGLSIGPDF EKGLKDGTIL
     CTLMNKLQLG SVPKINCSMQ NWHQLENLSN FIKAMVSYGM NPVDLFEAND LFKSGNMTQV
     QVSLLALAGK AKTKGLQSRS GMTTYGTRRH LHDPKNHILP PMDHSTISLQ MGTNKCASQV
     GMTAPGTRRH IYDTKLGTDK CDNSSMSLQM GYTQGANQSS QIHDPKYCPQ GTVADGAPSG
     AGDCPDPGEV PEYPPYYQEE ASY
//
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