CNN1_HUMAN
ID CNN1_HUMAN Reviewed; 297 AA.
AC P51911; B2R868; B4DUX6; O00638; Q15416; Q8IY93; Q99438;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Calponin-1;
DE AltName: Full=Basic calponin;
DE AltName: Full=Calponin H1, smooth muscle;
GN Name=CNN1;
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=Aorta;
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 [MRNA] (ISOFORM 1).
RX PubMed=9332369; DOI=10.1016/s0378-1119(97)00265-5;
RA Miano J.M., Krahe R., Garcia E., Elliott J.M., Olson E.N.;
RT "Expression, genomic structure and high resolution mapping to 19p13.2 of
RT the human smooth muscle cell calponin gene.";
RL Gene 197:215-224(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Aorta;
RA Takahashi K.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Pericardium, and Small intestine;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-297 (ISOFORM 1).
RC TISSUE=Placenta;
RA Kuromitsu J., Hayashizaki Y.;
RT "Systematic RLGS-M screening and identification of genes on chromosome 21
RT regulated by the dosage compensation in Down syndrome.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RA Takahashi K.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP STRUCTURE BY NMR OF 20-142.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CH domain of human calponin 1.";
RL Submitted (AUG-2005) to the PDB data bank.
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 -!- SUBUNIT: Part of cGMP kinase signaling complex at least composed of
CC ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and
CC ITPR1. {ECO:0000250}.
CC -!- INTERACTION:
CC P51911; A0A024R4Q5: TFPT; NbExp=4; IntAct=EBI-2873130, EBI-11527449;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P51911-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51911-2; Sequence=VSP_056948;
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; S80560; AAB35751.1; -; mRNA.
DR EMBL; U37019; AAC51780.1; -; mRNA.
DR EMBL; D17408; BAA04231.1; -; mRNA.
DR EMBL; AK300837; BAG62488.1; -; mRNA.
DR EMBL; AK313255; BAG36065.1; -; mRNA.
DR EMBL; AC008481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84229.1; -; Genomic_DNA.
DR EMBL; BC022015; AAH22015.1; -; mRNA.
DR EMBL; BC036307; AAH36307.2; -; mRNA.
DR EMBL; D86058; BAA12983.1; -; mRNA.
DR EMBL; D85611; BAA19538.1; -; Genomic_DNA.
DR CCDS; CCDS12263.1; -. [P51911-1]
DR PIR; G02142; G02142.
DR PIR; JC4500; JC4500.
DR RefSeq; NP_001290.2; NM_001299.5. [P51911-1]
DR RefSeq; NP_001295270.1; NM_001308341.1.
DR PDB; 1WYP; NMR; -; A=20-142.
DR PDBsum; 1WYP; -.
DR AlphaFoldDB; P51911; -.
DR SMR; P51911; -.
DR BioGRID; 107664; 35.
DR IntAct; P51911; 13.
DR MINT; P51911; -.
DR STRING; 9606.ENSP00000252456; -.
DR iPTMnet; P51911; -.
DR MetOSite; P51911; -.
DR PhosphoSitePlus; P51911; -.
DR BioMuta; CNN1; -.
DR DMDM; 2829431; -.
DR EPD; P51911; -.
DR jPOST; P51911; -.
DR MassIVE; P51911; -.
DR MaxQB; P51911; -.
DR PaxDb; P51911; -.
DR PeptideAtlas; P51911; -.
DR PRIDE; P51911; -.
DR ProteomicsDB; 5232; -.
DR ProteomicsDB; 56450; -. [P51911-1]
DR Antibodypedia; 1965; 1097 antibodies from 42 providers.
DR DNASU; 1264; -.
DR Ensembl; ENST00000252456.7; ENSP00000252456.1; ENSG00000130176.8. [P51911-1]
DR GeneID; 1264; -.
DR KEGG; hsa:1264; -.
DR MANE-Select; ENST00000252456.7; ENSP00000252456.1; NM_001299.6; NP_001290.2.
DR CTD; 1264; -.
DR DisGeNET; 1264; -.
DR GeneCards; CNN1; -.
DR HGNC; HGNC:2155; CNN1.
DR HPA; ENSG00000130176; Tissue enhanced (endometrium, intestine, seminal vesicle, smooth muscle).
DR MIM; 600806; gene.
DR neXtProt; NX_P51911; -.
DR OpenTargets; ENSG00000130176; -.
DR PharmGKB; PA26665; -.
DR VEuPathDB; HostDB:ENSG00000130176; -.
DR eggNOG; KOG2046; Eukaryota.
DR GeneTree; ENSGT00940000159680; -.
DR InParanoid; P51911; -.
DR OMA; GEPTHNH; -.
DR OrthoDB; 861989at2759; -.
DR PhylomeDB; P51911; -.
DR TreeFam; TF313921; -.
DR PathwayCommons; P51911; -.
DR SignaLink; P51911; -.
DR SIGNOR; P51911; -.
DR BioGRID-ORCS; 1264; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; CNN1; human.
DR EvolutionaryTrace; P51911; -.
DR GenomeRNAi; 1264; -.
DR Pharos; P51911; Tbio.
DR PRO; PR:P51911; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P51911; protein.
DR Bgee; ENSG00000130176; Expressed in saphenous vein and 151 other tissues.
DR ExpressionAtlas; P51911; baseline and differential.
DR Genevisible; P51911; HS.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IGI:BHF-UCL.
DR GO; GO:0006940; P:regulation of smooth muscle contraction; TAS: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 3D-structure; Actin-binding; Alternative splicing; Calmodulin-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..297
FT /note="Calponin-1"
FT /id="PRO_0000204767"
FT DOMAIN 28..131
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 MOD_RES 170
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000250"
FT MOD_RES 175
FT /note="Phosphoserine; by ROCK2"
FT /evidence="ECO:0000250"
FT MOD_RES 180
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000250"
FT MOD_RES 184
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000250"
FT MOD_RES 259
FT /note="Phosphothreonine; by ROCK2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..21
FT /note="MSSAHFNRGPAYGLSAEVKNK -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056948"
FT CONFLICT 57
FT /note="G -> S (in Ref. 8; BAA12983)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="E -> G (in Ref. 8; BAA12983)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="T -> S (in Ref. 2; AAC51780)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="Q -> P (in Ref. 8; BAA12983)"
FT /evidence="ECO:0000305"
FT HELIX 28..41
FT /evidence="ECO:0007829|PDB:1WYP"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:1WYP"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:1WYP"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1WYP"
FT HELIX 82..98
FT /evidence="ECO:0007829|PDB:1WYP"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1WYP"
FT HELIX 108..112
FT /evidence="ECO:0007829|PDB:1WYP"
FT HELIX 118..134
FT /evidence="ECO:0007829|PDB:1WYP"
SQ SEQUENCE 297 AA; 33170 MW; A949573543BC246C CRC64;
MSSAHFNRGP AYGLSAEVKN KLAQKYDHQR EQELREWIEG VTGRRIGNNF MDGLKDGIIL
CEFINKLQPG SVKKINESTQ NWHQLENIGN FIKAITKYGV KPHDIFEAND LFENTNHTQV
QSTLLALASM AKTKGNKVNV GVKYAEKQER KFEPGKLREG RNIIGLQMGT NKFASQQGMT
AYGTRRHLYD PKLGTDQPLD QATISLQMGT NKGASQAGMT APGTKRQIFE PGLGMEHCDT
LNVSLQMGSN KGASQRGMTV YGLPRQVYDP KYCLTPEYPE LGEPAHNHHA HNYYNSA
