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   14-OCT-2015, entry version 139.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; 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
RT   gene 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/6; 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=Swiss;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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,
RC   Pancreas, 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-172, AND IDENTIFICATION BY
RP   MASS 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.,
RA   Zhang Y., 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   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}.
CC   -!- SIMILARITY: Contains 1 calponin-like repeat. {ECO:0000255|PROSITE-
CC       ProRule:PRU00474}.
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00044}.
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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   UniGene; Mm.283283; -.
DR   PDB; 1UJO; NMR; -; A=24-154.
DR   PDBsum; 1UJO; -.
DR   ProteinModelPortal; P37804; -.
DR   SMR; P37804; 24-154.
DR   BioGrid; 203960; 1.
DR   IntAct; P37804; 3.
DR   MINT; MINT-4136841; -.
DR   STRING; 10090.ENSMUSP00000034590; -.
DR   PhosphoSite; P37804; -.
DR   REPRODUCTION-2DPAGE; IPI00226515; -.
DR   MaxQB; P37804; -.
DR   PaxDb; P37804; -.
DR   PRIDE; P37804; -.
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   eggNOG; COG5199; -.
DR   GeneTree; ENSGT00550000074447; -.
DR   HOGENOM; HOG000232113; -.
DR   HOVERGEN; HBG005186; -.
DR   InParanoid; P37804; -.
DR   OMA; VEWIVVQ; -.
DR   OrthoDB; EOG718KD9; -.
DR   PhylomeDB; P37804; -.
DR   TreeFam; TF313921; -.
DR   EvolutionaryTrace; P37804; -.
DR   NextBio; 300528; -.
DR   PRO; PR:P37804; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   Bgee; P37804; -.
DR   CleanEx; MM_TAGLN; -.
DR   Genevisible; P37804; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030855; P:epithelial cell differentiation; ISO:MGI.
DR   Gene3D; 1.10.418.10; -; 1.
DR   InterPro; IPR000557; Calponin_repeat.
DR   InterPro; IPR001715; CH-domain.
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; Complete proteome; Cytoplasm;
KW   Muscle protein; Phosphoprotein; Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000255}.
FT   CHAIN         2    201       Transgelin.
FT                                /FTId=PRO_0000204782.
FT   DOMAIN       24    137       CH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00044}.
FT   REPEAT      175    200       Calponin-like.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:Q01995,
FT                                ECO:0000255}.
FT   MOD_RES     166    166       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q01995}.
FT   MOD_RES     172    172       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     181    181       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q01995}.
FT   CONFLICT     44     44       R -> A (in Ref. 2; no nucleotide entry).
FT                                {ECO:0000305}.
FT   HELIX        25     38       {ECO:0000244|PDB:1UJO}.
FT   STRAND       47     51       {ECO:0000244|PDB:1UJO}.
FT   HELIX        52     55       {ECO:0000244|PDB:1UJO}.
FT   HELIX        60     69       {ECO:0000244|PDB:1UJO}.
FT   TURN         72     74       {ECO:0000244|PDB:1UJO}.
FT   HELIX        87    104       {ECO:0000244|PDB:1UJO}.
FT   STRAND      108    110       {ECO:0000244|PDB:1UJO}.
FT   HELIX       114    118       {ECO:0000244|PDB:1UJO}.
FT   HELIX       123    140       {ECO:0000244|PDB:1UJO}.
FT   TURN        150    152       {ECO:0000244|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
//