ID   TAGL_RAT                Reviewed;         201 AA.
AC   P31232;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Transgelin;
DE   AltName: Full=Smooth muscle protein 22-alpha;
DE            Short=SM22-alpha;
GN   Name=Tagln; Synonyms=Sm22;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Aortic smooth muscle;
RX   PubMed=8508530; DOI=10.1161/01.res.73.1.193;
RA   Shanahan C.M., Weissberg P.L., Metcalfe J.C.;
RT   "Isolation of gene markers of differentiated and proliferating vascular
RT   smooth muscle cells.";
RL   Circ. Res. 73:193-204(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Aortic smooth muscle;
RX   PubMed=8359698; DOI=10.1016/0378-1119(93)90435-6;
RA   Nishida W., Kitami Y., Hiwada K.;
RT   "cDNA cloning and mRNA expression of calponin and SM22 in rat aorta smooth
RT   muscle cells.";
RL   Gene 130:297-302(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Aorta;
RX   PubMed=7954852; DOI=10.1002/cm.970280307;
RA   Prinjha R., Shapland C., Hsuan J., Totty N., Mason I., Lawson D.;
RT   "Cloning and sequencing of cDNAs encoding the actin cross-linking protein
RT   transgelin defines a new family of actin-associated proteins.";
RL   Cell Motil. Cytoskeleton 28:243-255(1994).
RN   [4]
RP   ERRATUM OF PUBMED:7954852.
RA   Prinjha R., Shapland C., Hsuan J., Totty N., Mason I., Lawson D.;
RL   Cell Motil. Cytoskeleton 29:383-383(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   PROTEIN SEQUENCE OF 162-172, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Actin cross-linking/gelling protein.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Smooth muscle and mesenchymal cells but not in
CC       skeletal muscle or lymphocytes.
CC   -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}.
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DR   EMBL; X71070; CAA50396.1; -; mRNA.
DR   EMBL; M83107; AAA40762.1; -; mRNA.
DR   EMBL; X64422; CAA45769.1; -; mRNA.
DR   EMBL; BC061770; AAH61770.1; -; mRNA.
DR   PIR; JN0774; JN0774.
DR   RefSeq; NP_113737.1; NM_031549.2.
DR   AlphaFoldDB; P31232; -.
DR   SMR; P31232; -.
DR   BioGRID; 247194; 3.
DR   IntAct; P31232; 6.
DR   STRING; 10116.ENSRNOP00000024030; -.
DR   iPTMnet; P31232; -.
DR   PhosphoSitePlus; P31232; -.
DR   jPOST; P31232; -.
DR   PaxDb; P31232; -.
DR   PRIDE; P31232; -.
DR   GeneID; 25123; -.
DR   KEGG; rno:25123; -.
DR   UCSC; RGD:3723; rat.
DR   CTD; 6876; -.
DR   RGD; 3723; Tagln.
DR   VEuPathDB; HostDB:ENSRNOG00000017628; -.
DR   eggNOG; KOG2046; Eukaryota.
DR   HOGENOM; CLU_055232_1_0_1; -.
DR   InParanoid; P31232; -.
DR   OrthoDB; 861989at2759; -.
DR   PhylomeDB; P31232; -.
DR   TreeFam; TF313921; -.
DR   PRO; PR:P31232; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000017628; Expressed in colon and 19 other tissues.
DR   ExpressionAtlas; P31232; baseline and differential.
DR   Genevisible; P31232; RN.
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; TAS:RGD.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; TAS:RGD.
DR   GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
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   Acetylation; Cytoplasm; Direct protein sequencing; Methylation;
KW   Muscle protein; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..201
FT                   /note="Transgelin"
FT                   /id="PRO_0000204783"
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   REGION          154..161
FT                   /note="Could be involved in actin-binding"
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:0000250|UniProtKB:P37804"
FT   MOD_RES         181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         183
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q01995"
SQ   SEQUENCE   201 AA;  22603 MW;  0D49B5296D9A125B CRC64;
     MANKGPSYGM SREVQSKIEK KYDEELEERL VEWIVMQCGP DVGRPDRGRL GFQVWLKNGV
     ILSKLVNSLY PEGSKPVKVP ENPPSMVFKQ MEQVAQFLKA AEDYGVTKTD MFQTVDLFEG
     KDMAAVQRTV MALGSLAVTK NDGHYRGDPN WFMKKAQEHK REFTDSQLQE GKHVIGLQMG
     SNRGASQAGM TGYGRPRQII S