ID   TAGL_BOVIN              Reviewed;         201 AA.
AC   Q9TS87; Q2KJH8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Transgelin;
DE   AltName: Full=25 kDa F-actin-binding protein;
DE   AltName: Full=Smooth muscle protein 22-alpha;
DE            Short=SM22-alpha;
GN   Name=TAGLN; Synonyms=SM22;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 21-153 AND 160-200.
RC   TISSUE=Aorta;
RX   PubMed=8117285; DOI=10.1006/bbrc.1994.1180;
RA   Kobayashi R., Kubota T., Hidaka H.;
RT   "Purification, characterization, and partial sequence analysis of a new 25-
RT   kDa actin-binding protein from bovine aorta: a SM22 homolog.";
RL   Biochem. Biophys. Res. Commun. 198:1275-1280(1994).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC105336; AAI05337.1; -; mRNA.
DR   RefSeq; NP_001039614.1; NM_001046149.1.
DR   RefSeq; XP_005215887.1; XM_005215830.3.
DR   AlphaFoldDB; Q9TS87; -.
DR   SMR; Q9TS87; -.
DR   STRING; 9913.ENSBTAP00000009469; -.
DR   PaxDb; Q9TS87; -.
DR   PeptideAtlas; Q9TS87; -.
DR   PRIDE; Q9TS87; -.
DR   Ensembl; ENSBTAT00000009469; ENSBTAP00000009469; ENSBTAG00000007196.
DR   GeneID; 513463; -.
DR   KEGG; bta:513463; -.
DR   CTD; 6876; -.
DR   VEuPathDB; HostDB:ENSBTAG00000007196; -.
DR   VGNC; VGNC:35585; TAGLN.
DR   eggNOG; KOG2046; Eukaryota.
DR   GeneTree; ENSGT00940000155162; -.
DR   HOGENOM; CLU_055232_1_0_1; -.
DR   InParanoid; Q9TS87; -.
DR   OMA; AYKHPEW; -.
DR   OrthoDB; 861989at2759; -.
DR   TreeFam; TF313921; -.
DR   Proteomes; UP000009136; Chromosome 15.
DR   Bgee; ENSBTAG00000007196; Expressed in aorta and 106 other tissues.
DR   ExpressionAtlas; Q9TS87; baseline and differential.
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; IEA:Ensembl.
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; Actin-binding; Cytoplasm; Direct protein sequencing;
KW   Methylation; 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_0000204780"
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:0000250|UniProtKB:P37804"
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:0000250|UniProtKB:Q01995"
FT   CONFLICT        67
FT                   /note="N -> F (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        72
FT                   /note="D -> L (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        196
FT                   /note="P -> M (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   201 AA;  22599 MW;  0DCA866D5E3109BB CRC64;
     MANKGPSYGM SREVQSKIEK KYDEELEERL VEWIVMQCGP DVGRPDRGRL GFQVWLKNGV
     ILSKLVNSLY PDGSKPVKVP ENPPSMVFKQ MEQVAQFLKA AEDYGVTKTD MFQTVDLFEG
     KDLAAVQRTL MALGSLAVTK NDGHYRGDPN WFMKKAQEHK REFTESQLQE GKHVIGLQMG
     SNRGASQAGM TGYGRPRQII S