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Database: UniProt
Entry: A0A2I2YM60_GORGO
LinkDB: A0A2I2YM60_GORGO
Original site: A0A2I2YM60_GORGO 
ID   A0A2I2YM60_GORGO        Unreviewed;       283 AA.
AC   A0A2I2YM60;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Calponin {ECO:0000256|RuleBase:RU361224};
GN   Name=CNN3 {ECO:0000313|Ensembl:ENSGGOP00000036016.1};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000036016.1, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000036016.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000036016.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000036016.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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, ECO:0000256|RuleBase:RU361224}.
CC   -!- SIMILARITY: Belongs to the calponin family.
CC       {ECO:0000256|ARBA:ARBA00009631, ECO:0000256|RuleBase:RU361224}.
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DR   EMBL; CABD030004664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2YM60; -.
DR   SMR; A0A2I2YM60; -.
DR   Ensembl; ENSGGOT00000053809.1; ENSGGOP00000036016.1; ENSGGOG00000013870.3.
DR   GeneTree; ENSGT00940000154539; -.
DR   Proteomes; UP000001519; Chromosome 1.
DR   Bgee; ENSGGOG00000013870; Expressed in testis and 6 other cell types or tissues.
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:SF24; CALPONIN; 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; Calponin-homology domain, CH-domain; 1.
DR   PROSITE; PS01052; CALPONIN_1; 2.
DR   PROSITE; PS51122; CALPONIN_2; 3.
DR   PROSITE; PS50021; CH; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|ARBA:ARBA00023203,
KW   ECO:0000256|RuleBase:RU361224};
KW   Calmodulin-binding {ECO:0000256|RuleBase:RU361224};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          26..133
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000259|PROSITE:PS50021"
FT   REGION          233..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..252
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   283 AA;  31384 MW;  7BA632697F3567CA CRC64;
     MTHFNKGPSY GLSAEVKNKI ASKYDHQAEE DLRNWIEEVT GMSIGTNFQL GLKDGIILCE
     LINKLQPGSV KKVNESSLNW PQAKTKGFHT TIDIGVKYAE KQTRRFDEGK LKAGQSVIGL
     QMGTNKCASQ AGMTAYGTRR HLYDPKMQTD KPFDQTTISL QMGTNKGASQ AGMLAPGTRR
     DIYDQKLTLQ PVDNSTISLQ MGTNKVASQK GMSVYGLGRQ VYDPKYCAAP TEPVIHNGSQ
     GTGTNGSEIS DSDYQAEYPD EYHGEYQDDY PRDYQYSDQG IDY
//
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