ID   TAGL_HUMAN              Reviewed;         201 AA.
AC   Q01995; O15542;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   24-JAN-2024, entry version 208.
DE   RecName: Full=Transgelin;
DE   AltName: Full=22 kDa actin-binding protein;
DE   AltName: Full=Protein WS3-10;
DE   AltName: Full=Smooth muscle protein 22-alpha;
DE            Short=SM22-alpha;
GN   Name=TAGLN; Synonyms=SM22, WS3-10;
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].
RC   TISSUE=Fibroblast;
RX   PubMed=1520290; DOI=10.1016/s0006-291x(05)81449-4;
RA   Thweatt R., Lumpkin C.K. Jr., Goldstein S.;
RT   "A novel gene encoding a smooth muscle protein is overexpressed in
RT   senescent human fibroblasts.";
RL   Biochem. Biophys. Res. Commun. 187:1-7(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1872880;
RA   Nishida W., Kitami Y., Abe M., Kiwada K.;
RT   "Gene cloning and nucleotide sequence of SM22 alpha from the chicken
RT   gizzard smooth muscle.";
RL   Biochem. Int. 23:663-668(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9615232; DOI=10.1006/geno.1998.5267;
RA   Camoretti-Mercado B., Forsythe S.M., Lebeau M.M., Espinosa R.D. III,
RA   Vieira J.E., Halayko A.J., Willadsen S., Kurtz B., Ober C., Evans G.A.,
RA   Thweatt R., Shapiro S., Niu Q., Qin Y., Padrid P.A., Solway J.;
RT   "Expression and cytogenetic localization of the human SM22 gene (TAGLN).";
RL   Genomics 49:452-457(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Aorta, and Peripheral blood;
RX   PubMed=9276683; DOI=10.1093/oxfordjournals.jbchem.a021722;
RA   Yamamura H., Masuda H., Ikeda W., Tokuyama T., Takagi M., Shibata N.,
RA   Tatsuta M., Takahashi K.;
RT   "Structure and expression of the human SM22alpha gene, assignment of the
RT   gene to chromosome 11, and repression of the promoter activity by cytosine
RT   DNA methylation.";
RL   J. Biochem. 122:157-167(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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   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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, 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   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP   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   [10]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-183, 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: Actin cross-linking/gelling protein (By similarity). Involved
CC       in calcium interactions and contractile properties of the cell that may
CC       contribute to replicative senescence. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q01995; Q9H8Y8: GORASP2; NbExp=6; IntAct=EBI-1054248, EBI-739467;
CC       Q01995; P08069: IGF1R; NbExp=2; IntAct=EBI-1054248, EBI-475981;
CC       Q01995; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-1054248, EBI-717399;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Overexpressed in senescent human fibroblasts.
CC   -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/46168/TAGLN";
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DR   EMBL; M95787; AAA58351.1; -; mRNA.
DR   EMBL; M83106; AAA58375.1; -; mRNA.
DR   EMBL; AF013711; AAC21582.1; -; Genomic_DNA.
DR   EMBL; D17409; BAA21811.1; -; mRNA.
DR   EMBL; D84342; BAA21839.1; -; Genomic_DNA.
DR   EMBL; BC004927; AAH04927.1; -; mRNA.
DR   EMBL; BC065829; AAH65829.1; -; mRNA.
DR   CCDS; CCDS8381.1; -.
DR   PIR; JC5577; JS0774.
DR   RefSeq; NP_001001522.1; NM_001001522.1.
DR   RefSeq; NP_003177.2; NM_003186.3.
DR   AlphaFoldDB; Q01995; -.
DR   BMRB; Q01995; -.
DR   SMR; Q01995; -.
DR   BioGRID; 112739; 68.
DR   IntAct; Q01995; 292.
DR   MINT; Q01995; -.
DR   STRING; 9606.ENSP00000376678; -.
DR   DrugBank; DB11638; Artenimol.
DR   GlyGen; Q01995; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q01995; -.
DR   MetOSite; Q01995; -.
DR   PhosphoSitePlus; Q01995; -.
DR   SwissPalm; Q01995; -.
DR   BioMuta; TAGLN; -.
DR   DMDM; 3123283; -.
DR   REPRODUCTION-2DPAGE; IPI00216138; -.
DR   CPTAC; CPTAC-443; -.
DR   CPTAC; CPTAC-726; -.
DR   EPD; Q01995; -.
DR   jPOST; Q01995; -.
DR   MassIVE; Q01995; -.
DR   PaxDb; 9606-ENSP00000432282; -.
DR   PeptideAtlas; Q01995; -.
DR   ProteomicsDB; 58029; -.
DR   Pumba; Q01995; -.
DR   ABCD; Q01995; 1 sequenced antibody.
DR   Antibodypedia; 3666; 804 antibodies from 40 providers.
DR   CPTC; Q01995; 1 antibody.
DR   DNASU; 6876; -.
DR   Ensembl; ENST00000278968.10; ENSP00000278968.6; ENSG00000149591.17.
DR   Ensembl; ENST00000392951.9; ENSP00000376678.4; ENSG00000149591.17.
DR   Ensembl; ENST00000525531.5; ENSP00000432054.1; ENSG00000149591.17.
DR   Ensembl; ENST00000530649.5; ENSP00000431941.1; ENSG00000149591.17.
DR   Ensembl; ENST00000532870.5; ENSP00000432282.1; ENSG00000149591.17.
DR   GeneID; 6876; -.
DR   KEGG; hsa:6876; -.
DR   MANE-Select; ENST00000392951.9; ENSP00000376678.4; NM_003186.5; NP_003177.2.
DR   AGR; HGNC:11553; -.
DR   CTD; 6876; -.
DR   DisGeNET; 6876; -.
DR   GeneCards; TAGLN; -.
DR   HGNC; HGNC:11553; TAGLN.
DR   HPA; ENSG00000149591; Tissue enhanced (endometrium, intestine).
DR   MIM; 600818; gene.
DR   neXtProt; NX_Q01995; -.
DR   OpenTargets; ENSG00000149591; -.
DR   PharmGKB; PA36324; -.
DR   VEuPathDB; HostDB:ENSG00000149591; -.
DR   eggNOG; KOG2046; Eukaryota.
DR   GeneTree; ENSGT00940000155162; -.
DR   HOGENOM; CLU_055232_1_0_1; -.
DR   InParanoid; Q01995; -.
DR   OMA; VEWITVQ; -.
DR   OrthoDB; 11630at2759; -.
DR   PhylomeDB; Q01995; -.
DR   TreeFam; TF313921; -.
DR   PathwayCommons; Q01995; -.
DR   SignaLink; Q01995; -.
DR   SIGNOR; Q01995; -.
DR   BioGRID-ORCS; 6876; 7 hits in 1153 CRISPR screens.
DR   ChiTaRS; TAGLN; human.
DR   GeneWiki; TAGLN; -.
DR   GenomeRNAi; 6876; -.
DR   Pharos; Q01995; Tbio.
DR   PRO; PR:Q01995; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q01995; Protein.
DR   Bgee; ENSG00000149591; Expressed in saphenous vein and 202 other cell types or tissues.
DR   ExpressionAtlas; Q01995; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030855; P:epithelial cell differentiation; IDA:UniProtKB.
DR   GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR   CDD; cd21279; CH_TAGLN; 1.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 1.
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:SF16; TRANSGELIN; 1.
DR   Pfam; PF00402; Calponin; 1.
DR   Pfam; PF00307; CH; 1.
DR   PRINTS; PR00888; SM22CALPONIN.
DR   PRINTS; PR00890; TRANSGELIN.
DR   SMART; SM00033; CH; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   PROSITE; PS01052; CALPONIN_1; 1.
DR   PROSITE; PS51122; CALPONIN_2; 1.
DR   PROSITE; PS50021; CH; 1.
DR   UCD-2DPAGE; Q01995; -.
DR   Genevisible; Q01995; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Cytoplasm; Methylation; Muscle protein;
KW   Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..201
FT                   /note="Transgelin"
FT                   /id="PRO_0000204781"
FT   DOMAIN          24..137
FT                   /note="Calponin-homology (CH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   REPEAT          175..200
FT                   /note="Calponin-like"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         172
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P37804"
FT   MOD_RES         181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         183
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   VARIANT         182
FT                   /note="N -> S (in dbSNP:rs12284316)"
FT                   /id="VAR_048670"
FT   CONFLICT        49
FT                   /note="R -> P (in Ref. 1; AAA58351)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        72
FT                   /note="D -> E (in Ref. 2; AAA58375)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        104
FT                   /note="Y -> C (in Ref. 2; AAA58375)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        104
FT                   /note="Y -> S (in Ref. 1; AAA58351)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        179
FT                   /note="M -> V (in Ref. 2; AAA58375)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   201 AA;  22611 MW;  7AE9E7A9A45602C3 CRC64;
     MANKGPSYGM SREVQSKIEK KYDEELEERL VEWIIVQCGP DVGRPDRGRL GFQVWLKNGV
     ILSKLVNSLY PDGSKPVKVP ENPPSMVFKQ MEQVAQFLKA AEDYGVIKTD MFQTVDLFEG
     KDMAAVQRTL MALGSLAVTK NDGHYRGDPN WFMKKAQEHK REFTESQLQE GKHVIGLQMG
     SNRGASQAGM TGYGRPRQII S
//