ID G7Q1H1_MACFA Unreviewed; 207 AA.
AC G7Q1H1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Calponin-homology (CH) domain-containing protein {ECO:0000259|PROSITE:PS50021};
DE Flags: Fragment;
GN ORFNames=EGM_11881 {ECO:0000313|EMBL:EHH60509.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000313|EMBL:EHH60509.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH60509.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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}.
CC -!- SIMILARITY: Belongs to the calponin family.
CC {ECO:0000256|ARBA:ARBA00009631}.
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DR EMBL; CM001295; EHH60509.1; -; Genomic_DNA.
DR AlphaFoldDB; G7Q1H1; -.
DR Proteomes; UP000009130; Chromosome 20.
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 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; PS51122; CALPONIN_2; 1.
DR PROSITE; PS50021; CH; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 45..148
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHH60509.1"
FT NON_TER 207
FT /evidence="ECO:0000313|EMBL:EHH60509.1"
SQ SEQUENCE 207 AA; 23175 MW; 4255EDDAA69CD6E6 CRC64;
AHWSPPVGPV LPPHPPAVFS MQFNKGPSYW LSAEVKNRLL SKYDPQKEAE LRSWIEGLTS
LSISPNFQKG LKDRIILHTL MNKLQPGSVP MINRSMQNWH QRGNLSNFIK AIVSYGMNPM
NLFEANNLFE SGNMTQVLSL LALVGKAKTK GLQSRVDIGI GYSKQQEQNF DYNTTKAGHL
TISLQMGTNK CASQVGMTAP WTQQQIY
//
