TAGL_MOUSE
ID TAGL_MOUSE Reviewed; 201 AA.
AC P37804; Q545W0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Transgelin;
DE AltName: Full=Actin-associated protein p27;
DE AltName: Full=Smooth muscle protein 22-alpha;
DE Short=SM22-alpha;
GN Name=Tagln; Synonyms=Sm22, Sm22a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=7768949; DOI=10.1074/jbc.270.22.13460;
RA Solway J., Seltzer J., Samaha F.F., Kim S., Alger L.E., Niu Q.,
RA Morrisey E.E., Ip H.S., Parmacek M.S.;
RT "Structure and expression of a smooth muscle cell-specific gene, SM22
RT alpha.";
RL J. Biol. Chem. 270:13460-13469(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2924801; DOI=10.1016/0014-4827(89)90108-0;
RA Almendral J.M., Santaren J.F., Perera J., Zerial M., Bravo R.;
RT "Expression, cloning and cDNA sequence of a fibroblast serum-regulated gene
RT encoding a putative actin-associated protein (p27).";
RL Exp. Cell Res. 181:518-530(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Moessler H., Mericskay M., Li Z., Nagl S., Small J.V., Paulin D.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SWR/J;
RX PubMed=8575061; DOI=10.1161/01.res.78.2.188;
RA Li L., Miano J.M., Cserjesi P., Olson E.N.;
RT "SM22 alpha, a marker of adult smooth muscle, is expressed in multiple
RT myogenic lineages during embryogenesis.";
RL Circ. Res. 78:188-195(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, Ovary, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-172, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-183, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
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).
RN [10]
RP STRUCTURE BY NMR OF 24-154.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CH domain from mouse transgelin.";
RL Submitted (SEP-2004) to the PDB data bank.
CC -!- FUNCTION: Actin cross-linking/gelling protein. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By growth factors.
CC -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}.
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DR EMBL; L41170; AAA79165.1; -; Genomic_DNA.
DR EMBL; L41169; AAA79165.1; JOINED; Genomic_DNA.
DR EMBL; L41154; AAA79166.1; -; mRNA.
DR EMBL; Z68618; CAA92941.1; -; Genomic_DNA.
DR EMBL; U36588; AAC52418.1; -; mRNA.
DR EMBL; AK002880; BAB22427.1; -; mRNA.
DR EMBL; AK077235; BAC36700.1; -; mRNA.
DR EMBL; BC003795; AAH03795.1; -; mRNA.
DR CCDS; CCDS23137.1; -.
DR PIR; A57015; A57015.
DR PIR; A60598; A60598.
DR RefSeq; NP_035656.1; NM_011526.5.
DR PDB; 1UJO; NMR; -; A=24-154.
DR PDBsum; 1UJO; -.
DR AlphaFoldDB; P37804; -.
DR BMRB; P37804; -.
DR SMR; P37804; -.
DR BioGRID; 203960; 14.
DR IntAct; P37804; 2.
DR MINT; P37804; -.
DR STRING; 10090.ENSMUSP00000034590; -.
DR iPTMnet; P37804; -.
DR PhosphoSitePlus; P37804; -.
DR SwissPalm; P37804; -.
DR REPRODUCTION-2DPAGE; IPI00226515; -.
DR CPTAC; non-CPTAC-3751; -.
DR EPD; P37804; -.
DR jPOST; P37804; -.
DR MaxQB; P37804; -.
DR PaxDb; P37804; -.
DR PeptideAtlas; P37804; -.
DR PRIDE; P37804; -.
DR ProteomicsDB; 262928; -.
DR Antibodypedia; 3666; 718 antibodies from 40 providers.
DR DNASU; 21345; -.
DR Ensembl; ENSMUST00000034590; ENSMUSP00000034590; ENSMUSG00000032085.
DR GeneID; 21345; -.
DR KEGG; mmu:21345; -.
DR UCSC; uc009pgs.2; mouse.
DR CTD; 6876; -.
DR MGI; MGI:106012; Tagln.
DR VEuPathDB; HostDB:ENSMUSG00000032085; -.
DR eggNOG; KOG2046; Eukaryota.
DR GeneTree; ENSGT00940000155162; -.
DR HOGENOM; CLU_055232_1_0_1; -.
DR InParanoid; P37804; -.
DR OMA; AYKHPEW; -.
DR OrthoDB; 861989at2759; -.
DR PhylomeDB; P37804; -.
DR TreeFam; TF313921; -.
DR BioGRID-ORCS; 21345; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Tagln; mouse.
DR EvolutionaryTrace; P37804; -.
DR PRO; PR:P37804; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P37804; protein.
DR Bgee; ENSMUSG00000032085; Expressed in aorta tunica media and 241 other tissues.
DR ExpressionAtlas; P37804; baseline and differential.
DR Genevisible; P37804; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:MGI.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR000557; Calponin_repeat.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR003096; SM22_calponin.
DR InterPro; IPR029976; TAGLN.
DR PANTHER; PTHR18959:SF40; PTHR18959:SF40; 1.
DR Pfam; PF00402; Calponin; 1.
DR Pfam; PF00307; CH; 1.
DR PRINTS; PR00888; SM22CALPONIN.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS01052; CALPONIN_1; 1.
DR PROSITE; PS51122; CALPONIN_2; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Methylation; Muscle protein;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..201
FT /note="Transgelin"
FT /id="PRO_0000204782"
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:0000250|UniProtKB:Q01995, ECO:0000255"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01995"
FT MOD_RES 172
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01995"
FT MOD_RES 183
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 44
FT /note="R -> A (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 25..38
FT /evidence="ECO:0007829|PDB:1UJO"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:1UJO"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:1UJO"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:1UJO"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1UJO"
FT HELIX 87..104
FT /evidence="ECO:0007829|PDB:1UJO"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1UJO"
FT HELIX 114..118
FT /evidence="ECO:0007829|PDB:1UJO"
FT HELIX 123..140
FT /evidence="ECO:0007829|PDB:1UJO"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:1UJO"
SQ SEQUENCE 201 AA; 22576 MW; 465F732D706F760A CRC64;
MANKGPSYGM SREVQSKIEK KYDEELEERL VEWIVVQCGP DVGRPDRGRL GFQVWLKNGV
ILSKLVNSLY PEGSKPVKVP ENPPSMVFKQ MEQVAQFLKA AEDYGVIKTD MFQTVDLYEG
KDMAAVQRTL MALGSLAVTK NDGNYRGDPN WFMKKAQEHK RDFTDSQLQE GKHVIGLQMG
SNRGASQAGM TGYGRPRQII S
