CNN3_HUMAN
ID CNN3_HUMAN Reviewed; 329 AA.
AC Q15417; B4DFK6; B4DP09; F8WA86; Q6FHA7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Calponin-3;
DE AltName: Full=Calponin, acidic isoform;
GN Name=CNN3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=8526917; DOI=10.1006/bbrc.1995.2769;
RA Maguchi M., Nishida W., Kohara K., Kuwano A., Kondo I., Hiwada K.;
RT "Molecular cloning and gene mapping of human basic and acidic calponins.";
RL Biochem. Biophys. Res. Commun. 217:238-244(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 54-64, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-158, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15417-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15417-2; Sequence=VSP_055191;
CC Name=3;
CC IsoId=Q15417-3; Sequence=VSP_055192;
CC -!- TISSUE SPECIFICITY: Expressed in both non-smooth muscle tissues as well
CC as smooth muscle tissues.
CC -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}.
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DR EMBL; S80562; AAB35752.1; -; mRNA.
DR EMBL; AK312370; BAG35288.1; -; mRNA.
DR EMBL; AK294141; BAG57467.1; -; mRNA.
DR EMBL; AK298145; BAG60421.1; -; mRNA.
DR EMBL; AK316398; BAH14769.1; -; mRNA.
DR EMBL; CR541848; CAG46646.1; -; mRNA.
DR EMBL; AC093429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL359554; CAC36093.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73029.1; -; Genomic_DNA.
DR EMBL; BC025372; AAH25372.1; -; mRNA.
DR CCDS; CCDS30775.1; -. [Q15417-1]
DR CCDS; CCDS65592.1; -. [Q15417-2]
DR CCDS; CCDS65593.1; -. [Q15417-3]
DR PIR; JC4501; JC4501.
DR RefSeq; NP_001272984.1; NM_001286055.1. [Q15417-3]
DR RefSeq; NP_001272985.1; NM_001286056.1. [Q15417-2]
DR RefSeq; NP_001830.1; NM_001839.4. [Q15417-1]
DR RefSeq; XP_016855734.1; XM_017000245.1. [Q15417-2]
DR AlphaFoldDB; Q15417; -.
DR SMR; Q15417; -.
DR BioGRID; 107666; 34.
DR CORUM; Q15417; -.
DR IntAct; Q15417; 22.
DR MINT; Q15417; -.
DR STRING; 9606.ENSP00000359225; -.
DR GlyConnect; 1059; 6 N-Linked glycans (1 site).
DR GlyGen; Q15417; 2 sites, 5 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q15417; -.
DR MetOSite; Q15417; -.
DR PhosphoSitePlus; Q15417; -.
DR SwissPalm; Q15417; -.
DR BioMuta; CNN3; -.
DR DMDM; 6225157; -.
DR EPD; Q15417; -.
DR jPOST; Q15417; -.
DR MassIVE; Q15417; -.
DR MaxQB; Q15417; -.
DR PaxDb; Q15417; -.
DR PeptideAtlas; Q15417; -.
DR PRIDE; Q15417; -.
DR ProteomicsDB; 30452; -.
DR ProteomicsDB; 4050; -.
DR ProteomicsDB; 60582; -. [Q15417-1]
DR Antibodypedia; 4078; 232 antibodies from 35 providers.
DR DNASU; 1266; -.
DR Ensembl; ENST00000370206.9; ENSP00000359225.4; ENSG00000117519.16. [Q15417-1]
DR Ensembl; ENST00000394202.8; ENSP00000377752.4; ENSG00000117519.16. [Q15417-3]
DR Ensembl; ENST00000545882.5; ENSP00000440081.1; ENSG00000117519.16. [Q15417-2]
DR GeneID; 1266; -.
DR KEGG; hsa:1266; -.
DR MANE-Select; ENST00000370206.9; ENSP00000359225.4; NM_001839.5; NP_001830.1.
DR UCSC; uc001dqz.6; human. [Q15417-1]
DR CTD; 1266; -.
DR DisGeNET; 1266; -.
DR GeneCards; CNN3; -.
DR HGNC; HGNC:2157; CNN3.
DR HPA; ENSG00000117519; Low tissue specificity.
DR MIM; 602374; gene.
DR neXtProt; NX_Q15417; -.
DR OpenTargets; ENSG00000117519; -.
DR PharmGKB; PA26667; -.
DR VEuPathDB; HostDB:ENSG00000117519; -.
DR eggNOG; KOG2046; Eukaryota.
DR GeneTree; ENSGT00940000154539; -.
DR HOGENOM; CLU_055232_0_2_1; -.
DR InParanoid; Q15417; -.
DR OMA; TMTHFNK; -.
DR OrthoDB; 861989at2759; -.
DR PhylomeDB; Q15417; -.
DR TreeFam; TF313921; -.
DR PathwayCommons; Q15417; -.
DR SignaLink; Q15417; -.
DR SIGNOR; Q15417; -.
DR BioGRID-ORCS; 1266; 9 hits in 1069 CRISPR screens.
DR ChiTaRS; CNN3; human.
DR GenomeRNAi; 1266; -.
DR Pharos; Q15417; Tbio.
DR PRO; PR:Q15417; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15417; protein.
DR Bgee; ENSG00000117519; Expressed in ventricular zone and 203 other tissues.
DR ExpressionAtlas; Q15417; baseline and differential.
DR Genevisible; Q15417; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; HDA:BHF-UCL.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
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; IPR003096; SM22_calponin.
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 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Calmodulin-binding;
KW Direct protein sequencing; Methylation; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..329
FT /note="Calponin-3"
FT /id="PRO_0000204776"
FT DOMAIN 26..130
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 164..189
FT /note="Calponin-like 1"
FT REPEAT 204..229
FT /note="Calponin-like 2"
FT REPEAT 243..268
FT /note="Calponin-like 3"
FT REGION 279..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DAW9"
FT MOD_RES 158
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055191"
FT VAR_SEQ 83..128
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055192"
FT CONFLICT 21
FT /note="A -> S (in Ref. 2; BAG60421)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 36414 MW; F024E169E821A8D8 CRC64;
MTHFNKGPSY GLSAEVKNKI ASKYDHQAEE DLRNWIEEVT GMSIGPNFQL GLKDGIILCE
LINKLQPGSV KKVNESSLNW PQLENIGNFI KAIQAYGMKP HDIFEANDLF ENGNMTQVQT
TLVALAGLAK TKGFHTTIDI GVKYAEKQTR RFDEGKLKAG QSVIGLQMGT NKCASQAGMT
AYGTRRHLYD PKMQTDKPFD QTTISLQMGT NKGASQAGML APGTRRDIYD QKLTLQPVDN
STISLQMGTN KVASQKGMSV YGLGRQVYDP KYCAAPTEPV IHNGSQGTGT NGSEISDSDY
QAEYPDEYHG EYQDDYPRDY QYSDQGIDY
