CNN2_HUMAN
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 03-AUG-2022, entry version 195.
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}.
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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; 60.
DR IntAct; Q99439; 14.
DR MINT; Q99439; -.
DR STRING; 9606.ENSP00000263097; -.
DR ChEMBL; CHEMBL4295930; -.
DR GlyGen; Q99439; 2 sites, 1 O-linked glycan (1 site).
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; Q99439; -.
DR PeptideAtlas; Q99439; -.
DR PRIDE; Q99439; -.
DR ProteomicsDB; 78268; -. [Q99439-1]
DR ProteomicsDB; 78269; -. [Q99439-2]
DR Antibodypedia; 22499; 419 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 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; 861989at2759; -.
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; 262 hits in 1078 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 168 other tissues.
DR ExpressionAtlas; Q99439; baseline and differential.
DR Genevisible; Q99439; HS.
DR GO; GO:0005911; C:cell-cell junction; TAS:ProtInc.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
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:0045296; F:cadherin binding; 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: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; 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; IPR029974; CNN2.
DR InterPro; IPR003096; SM22_calponin.
DR PANTHER; PTHR46756:SF2; PTHR46756:SF2; 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; 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; 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
