ID   CNN2_PONAB              Reviewed;         309 AA.
AC   Q5RFN6;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Calponin-2;
DE   AltName: Full=Calponin H2, smooth muscle;
DE   AltName: Full=Neutral calponin;
GN   Name=CNN2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR857117; CAH89421.1; -; mRNA.
DR   RefSeq; NP_001124601.1; NM_001131129.1.
DR   AlphaFoldDB; Q5RFN6; -.
DR   SMR; Q5RFN6; -.
DR   STRING; 9601.ENSPPYP00000010439; -.
DR   Ensembl; ENSPPYT00000010852; ENSPPYP00000010439; ENSPPYG00000009302.
DR   GeneID; 100171437; -.
DR   KEGG; pon:100171437; -.
DR   CTD; 1265; -.
DR   eggNOG; KOG2046; Eukaryota.
DR   GeneTree; ENSGT00940000154355; -.
DR   HOGENOM; CLU_055232_0_2_1; -.
DR   InParanoid; Q5RFN6; -.
DR   OMA; GKQIGPD; -.
DR   OrthoDB; 861989at2759; -.
DR   TreeFam; TF313921; -.
DR   Proteomes; UP000001595; Chromosome 19.
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:0032970; P:regulation of actin filament-based process; 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_0000232498"
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          283..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;  33697 MW;  0D767E9040190A5F CRC64;
     MSSTQFNKGP SYGLSAEVKN RLLSKYDPQK EAELRTWIEG LTGLSIGPDF QKGLKDGTIL
     CTLMNKLQPG SVPKINRSMQ NWHQLENLSN FIKAMVSYGM NPVDLFEAND LFESGNMTQV
     QVSLLALAGK AKTKGLQSGV DIGVKYSEKQ ERNFDDATMK AGQCVIGLQM GTNKCASQSG
     MTAYGTRRHL YDPKNHILPP MDHSTISLQM GTNKCASQVG MTAPGTRRHI YDTKLGTDKC
     DNSSMSLQMG YTQGANQSGQ VFGLGRQIYD PKYCPQGTVA DGAPSGTGDC PDPGEVPEYP
     PYYQEEAGY