ID   CNN2_BOVIN              Reviewed;         309 AA.
AC   Q3SYU6;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Calponin-2;
DE   AltName: Full=Calponin H2, smooth muscle;
DE   AltName: Full=Neutral calponin;
GN   Name=CNN2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}.
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DR   EMBL; BC103380; AAI03381.1; -; mRNA.
DR   RefSeq; NP_001030497.1; NM_001035420.1.
DR   AlphaFoldDB; Q3SYU6; -.
DR   SMR; Q3SYU6; -.
DR   STRING; 9913.ENSBTAP00000027670; -.
DR   PaxDb; Q3SYU6; -.
DR   PeptideAtlas; Q3SYU6; -.
DR   PRIDE; Q3SYU6; -.
DR   Ensembl; ENSBTAT00000027670; ENSBTAP00000027670; ENSBTAG00000020764.
DR   GeneID; 539019; -.
DR   KEGG; bta:539019; -.
DR   CTD; 1265; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020764; -.
DR   VGNC; VGNC:27509; CNN2.
DR   eggNOG; KOG2046; Eukaryota.
DR   GeneTree; ENSGT00940000154355; -.
DR   HOGENOM; CLU_055232_0_2_1; -.
DR   InParanoid; Q3SYU6; -.
DR   OMA; GKQIGPD; -.
DR   OrthoDB; 861989at2759; -.
DR   Proteomes; UP000009136; Chromosome 7.
DR   Bgee; ENSBTAG00000020764; Expressed in blood and 105 other tissues.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0001725; C:stress fiber; IEA:Ensembl.
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   GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR   GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR   GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR   GO; GO:1905517; P:macrophage migration; IEA:Ensembl.
DR   GO; GO:1905522; P:negative regulation of macrophage migration; IEA:Ensembl.
DR   GO; GO:0050765; P:negative regulation of phagocytosis; IEA:Ensembl.
DR   GO; GO:0006909; P:phagocytosis; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0032970; P:regulation of actin filament-based process; IEA:Ensembl.
DR   GO; GO:0070663; P:regulation of leukocyte proliferation; IEA:Ensembl.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   CDD; cd00014; CH; 1.
DR   Gene3D; 1.10.418.10; -; 1.
DR   InterPro; IPR001997; Calponin/LIMCH1.
DR   InterPro; IPR000557; Calponin_repeat.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR029974; CNN2.
DR   InterPro; IPR003096; SM22_calponin.
DR   PANTHER; PTHR46756:SF2; PTHR46756:SF2; 1.
DR   Pfam; PF00402; Calponin; 3.
DR   Pfam; PF00307; CH; 1.
DR   PRINTS; PR00889; CALPONIN.
DR   PRINTS; PR00888; SM22CALPONIN.
DR   SMART; SM00033; CH; 1.
DR   SUPFAM; SSF47576; SSF47576; 1.
DR   PROSITE; PS01052; CALPONIN_1; 3.
DR   PROSITE; PS51122; CALPONIN_2; 3.
DR   PROSITE; PS50021; CH; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Actin-binding; Calmodulin-binding; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q99439"
FT   CHAIN           2..309
FT                   /note="Calponin-2"
FT                   /id="PRO_0000232497"
FT   DOMAIN          28..132
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REPEAT          166..191
FT                   /note="Calponin-like 1"
FT   REPEAT          206..231
FT                   /note="Calponin-like 2"
FT   REPEAT          245..269
FT                   /note="Calponin-like 3"
FT   REGION          273..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99439"
FT   MOD_RES         8
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99439"
FT   MOD_RES         25
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99439"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99439"
SQ   SEQUENCE   309 AA;  33438 MW;  02DA2779BB7E5E5A CRC64;
     MSSTQFNKGP SYGLSAEVKN RLQSKYDPQK EAELRSWIEG LTGLSVGPDF QKGLKDGIIL
     CTLMNKLQPG SVPKINRSMQ NWHQLENLSN FIKAMVSYGM NPVDLFEAND LFESGNLTQV
     QVSLLALAGK AKTKGLQSGV DIGVKYSEKQ ERNFDDATMK AGQCVIGLQM GTNKCASQSG
     MTAYGTRRHL YDPKNHILPP MDHSTISLQM GTNKCASQVG MTAPGTRRHI YDTKLGTDKC
     DNSSMSLQMG YTQGANQSGQ VFGLGRQIYD PKYCPQGPAA DGAPAAAGDG PGPGEPSECP
     PYYQEEAGY