CNN2_PIG
ID CNN2_PIG Reviewed; 296 AA.
AC Q08094;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Calponin-2;
DE AltName: Full=Calponin H2, smooth muscle;
DE AltName: Full=Neutral calponin;
DE Flags: Fragment;
GN Name=CNN2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Smooth muscle;
RX PubMed=8370452; DOI=10.1016/0014-5793(93)80909-e;
RA Strasser P., Gimona M., Moessler H., Herzog M., Small J.V.;
RT "Mammalian calponin. Identification and expression of genetic variants.";
RL FEBS Lett. 330:13-18(1993).
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 -!- TISSUE SPECIFICITY: Smooth muscle, and tissues containing significant
CC amounts of smooth muscle.
CC -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}.
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DR EMBL; Z19539; CAA79599.1; -; mRNA.
DR PIR; S36148; S31483.
DR AlphaFoldDB; Q08094; -.
DR SMR; Q08094; -.
DR STRING; 9823.ENSSSCP00000027795; -.
DR PeptideAtlas; Q08094; -.
DR PRIDE; Q08094; -.
DR eggNOG; KOG2046; Eukaryota.
DR InParanoid; Q08094; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IBA:GO_Central.
DR GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
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..>296
FT /note="Calponin-2"
FT /id="PRO_0000204775"
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 275..296
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"
FT NON_TER 296
SQ SEQUENCE 296 AA; 32030 MW; 921164B374B50FDC CRC64;
MSSTQFNKGP SYGLSAEVKN RLLSKYDPQK EAELRSWIEG LTGLSIGPDF QKGLKDGIIL
CTLMNKLQPG SVPKINRSMQ NWHQLENLSN FIKAMVSYGM NPVDLFEAND LFESGNMTQV
QVSLLALAGK AKTKGLQSDV DIGVKYSEKQ QRNFDDATMK AGQCVIGLQM GTNKCASQSG
MTAYGTRRHL YDPKNHILPP MDHSTISLQM GTNKCASQVG MTAPGTRRHI YDTKLGTDKC
DNSSMSLQMG YTQGANQSGQ VFGLGRQIYD PKYCPQGPAA DGAPAAAGDC PGPGES