CNN2_PONAB
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