ID CNN2_HUMAN Reviewed; 309 AA. AC Q99439; A5D8U8; A6NFI4; D6W5X9; Q92578; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 204. DE RecName: Full=Calponin-2; DE AltName: Full=Calponin H2, smooth muscle; DE AltName: Full=Neutral calponin; GN Name=CNN2; 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=Heart; RX PubMed=8889829; DOI=10.1093/oxfordjournals.jbchem.a021428; RA Masuda H., Tanaka K., Takagi M., Ohgami K., Sakamaki T., Shibata N., RA Takahashi K.; RT "Molecular cloning and characterization of human non-smooth muscle RT calponin."; RL J. Biochem. 120:415-424(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Uterus; 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 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 [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-202 (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=9001224; DOI=10.1128/mcb.17.2.707; RA Kuromitsu J., Yamashita H., Kataoka H., Takahara T., Muramatsu M., RA Sekine T., Okamoto N., Furuichi Y., Hayashizaki Y.; RT "A unique downregulation of h2-calponin gene expression in Down syndrome: a RT possible attenuation mechanism for fetal survival by methylation at the CpG RT island in the trisomic chromosome 21."; RL Mol. Cell. Biol. 17:707-712(1997). RN [7] RP PROTEIN SEQUENCE OF 2-21. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8 AND LYS-25, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [9] 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 [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] RP STRUCTURE BY NMR OF 20-152. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the CH domain of human calponin-2."; 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. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q99439-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99439-2; Sequence=VSP_042941; CC -!- TISSUE SPECIFICITY: Heart and smooth muscle. CC -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D83735; BAA12090.1; -; mRNA. DR EMBL; AK126391; BAG54322.1; -; mRNA. DR EMBL; AC004528; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC011558; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471139; EAW69565.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69567.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69570.1; -; Genomic_DNA. DR EMBL; BC141818; AAI41819.1; -; mRNA. DR EMBL; BC141833; AAI41834.1; -; mRNA. DR EMBL; D86059; BAA20887.1; -; mRNA. DR CCDS; CCDS12053.1; -. [Q99439-1] DR CCDS; CCDS12054.1; -. [Q99439-2] DR PIR; JC4906; JC4906. DR RefSeq; NP_001290428.1; NM_001303499.1. DR RefSeq; NP_001290430.1; NM_001303501.1. DR RefSeq; NP_004359.1; NM_004368.3. [Q99439-1] DR RefSeq; NP_958434.1; NM_201277.2. [Q99439-2] DR PDB; 1WYN; NMR; -; A=20-152. DR PDBsum; 1WYN; -. DR AlphaFoldDB; Q99439; -. DR SMR; Q99439; -. DR BioGRID; 107665; 82. DR IntAct; Q99439; 15. DR MINT; Q99439; -. DR STRING; 9606.ENSP00000456436; -. DR ChEMBL; CHEMBL4295930; -. DR GlyGen; Q99439; 3 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q99439; -. DR MetOSite; Q99439; -. DR PhosphoSitePlus; Q99439; -. DR SwissPalm; Q99439; -. DR BioMuta; CNN2; -. DR DMDM; 6226844; -. DR OGP; Q99439; -. DR CPTAC; CPTAC-337; -. DR CPTAC; CPTAC-338; -. DR EPD; Q99439; -. DR jPOST; Q99439; -. DR MassIVE; Q99439; -. DR MaxQB; Q99439; -. DR PaxDb; 9606-ENSP00000263097; -. DR PeptideAtlas; Q99439; -. DR PRIDE; Q99439; -. DR ProteomicsDB; 78268; -. [Q99439-1] DR ProteomicsDB; 78269; -. [Q99439-2] DR Pumba; Q99439; -. DR Antibodypedia; 22499; 484 antibodies from 38 providers. DR DNASU; 1265; -. DR Ensembl; ENST00000263097.9; ENSP00000263097.2; ENSG00000064666.15. [Q99439-1] DR Ensembl; ENST00000348419.7; ENSP00000340129.2; ENSG00000064666.15. [Q99439-2] DR GeneID; 1265; -. DR KEGG; hsa:1265; -. DR MANE-Select; ENST00000263097.9; ENSP00000263097.2; NM_004368.4; NP_004359.1. DR UCSC; uc002lqu.4; human. [Q99439-1] DR AGR; HGNC:2156; -. DR CTD; 1265; -. DR DisGeNET; 1265; -. DR GeneCards; CNN2; -. DR HGNC; HGNC:2156; CNN2. DR HPA; ENSG00000064666; Low tissue specificity. DR MIM; 602373; gene. DR neXtProt; NX_Q99439; -. DR NIAGADS; ENSG00000064666; -. DR OpenTargets; ENSG00000064666; -. DR PharmGKB; PA26666; -. DR VEuPathDB; HostDB:ENSG00000064666; -. DR eggNOG; KOG2046; Eukaryota. DR GeneTree; ENSGT00940000154355; -. DR HOGENOM; CLU_055232_0_2_1; -. DR InParanoid; Q99439; -. DR OrthoDB; 11630at2759; -. DR PhylomeDB; Q99439; -. DR TreeFam; TF313921; -. DR PathwayCommons; Q99439; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation. DR SignaLink; Q99439; -. DR BioGRID-ORCS; 1265; 266 hits in 1156 CRISPR screens. DR ChiTaRS; CNN2; human. DR EvolutionaryTrace; Q99439; -. DR GenomeRNAi; 1265; -. DR Pharos; Q99439; Tbio. DR PRO; PR:Q99439; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q99439; Protein. DR Bgee; ENSG00000064666; Expressed in granulocyte and 170 other cell types or tissues. DR ExpressionAtlas; Q99439; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central. DR GO; GO:0005911; C:cell-cell junction; TAS:ProtInc. DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome. DR GO; GO:0001725; C:stress fiber; IDA:MGI. DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome. DR GO; GO:0003779; F:actin binding; TAS:ProtInc. DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central. DR GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro. DR GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:MGI. DR GO; GO:0007010; P:cytoskeleton organization; TAS:ProtInc. DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl. DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl. DR GO; GO:1905517; P:macrophage migration; IEA:Ensembl. DR GO; GO:1905522; P:negative regulation of macrophage migration; IEA:Ensembl. DR GO; GO:0050765; P:negative regulation of phagocytosis; IEA:Ensembl. DR GO; GO:0006909; P:phagocytosis; IEA:Ensembl. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0032970; P:regulation of actin filament-based process; IDA:MGI. DR GO; GO:0070663; P:regulation of leukocyte proliferation; IEA:Ensembl. DR GO; GO:0042060; P:wound healing; IEA:Ensembl. DR CDD; cd21283; CH_CNN2; 1. 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:SF17; CALPONIN-3; 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; 3. DR PROSITE; PS51122; CALPONIN_2; 3. DR PROSITE; PS50021; CH; 1. DR Genevisible; Q99439; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Actin-binding; Alternative splicing; KW Calmodulin-binding; Direct protein sequencing; Phosphoprotein; KW Reference proteome; Repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..309 FT /note="Calponin-2" FT /id="PRO_0000204773" 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 283..309 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 8 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 25 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 138 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 131..169 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042941" FT CONFLICT 52 FT /note="K -> R (in Ref. 6; BAA20887)" FT /evidence="ECO:0000305" FT CONFLICT 142 FT /note="I -> V (in Ref. 6; BAA20887)" FT /evidence="ECO:0000305" FT CONFLICT 165 FT /note="V -> G (in Ref. 6; BAA20887)" FT /evidence="ECO:0000305" FT CONFLICT 182..183 FT /note="TA -> HL (in Ref. 6; BAA20887)" FT /evidence="ECO:0000305" FT CONFLICT 187..202 FT /note="RRHLYDPKNHILPPMD -> AGISMTPRTISCPPWT (in Ref. 6; FT BAA20887)" FT /evidence="ECO:0000305" FT HELIX 30..42 FT /evidence="ECO:0007829|PDB:1WYN" FT HELIX 50..55 FT /evidence="ECO:0007829|PDB:1WYN" FT HELIX 59..67 FT /evidence="ECO:0007829|PDB:1WYN" FT HELIX 81..98 FT /evidence="ECO:0007829|PDB:1WYN" FT STRAND 102..104 FT /evidence="ECO:0007829|PDB:1WYN" FT HELIX 108..112 FT /evidence="ECO:0007829|PDB:1WYN" FT HELIX 118..131 FT /evidence="ECO:0007829|PDB:1WYN" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:1WYN" SQ SEQUENCE 309 AA; 33697 MW; 0D767E9040190A5F CRC64; MSSTQFNKGP SYGLSAEVKN RLLSKYDPQK EAELRTWIEG LTGLSIGPDF QKGLKDGTIL CTLMNKLQPG SVPKINRSMQ NWHQLENLSN FIKAMVSYGM NPVDLFEAND LFESGNMTQV QVSLLALAGK AKTKGLQSGV DIGVKYSEKQ ERNFDDATMK AGQCVIGLQM GTNKCASQSG MTAYGTRRHL YDPKNHILPP MDHSTISLQM GTNKCASQVG MTAPGTRRHI YDTKLGTDKC DNSSMSLQMG YTQGANQSGQ VFGLGRQIYD PKYCPQGTVA DGAPSGTGDC PDPGEVPEYP PYYQEEAGY //