TAGL2_MOUSE
ID TAGL2_MOUSE Reviewed; 199 AA.
AC Q9WVA4; Q3TIB8; Q6A0C6; Q78ZX2; Q91VU2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 4.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Transgelin-2;
DE AltName: Full=SM22-beta;
GN Name=Tagln2; Synonyms=Kiaa0120;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Heart;
RX PubMed=12049783; DOI=10.1016/s0925-4773(02)00088-6;
RA Zhang J.C.L., Helmke B.P., Shum A., Du K., Yu W.W., Lu M.M., Davies P.F.,
RA Parmacek M.S.;
RT "SM22beta encodes a lineage-restricted cytoskeletal protein with a unique
RT developmentally regulated pattern of expression.";
RL Mech. Dev. 115:161-166(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RA Jin C.G., Chen W.F., Li Y., Zhang J., Qian X.P.;
RT "Molecular cloning of mouse transgelin gene.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and NOD; TISSUE=Bone marrow, and Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and NMRI; TISSUE=Colon, and Mammary tumor;
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 PROTEIN SEQUENCE OF 140-153.
RC TISSUE=Brain;
RA Lubec G., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND THR-180, AND
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 [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-182, 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).
CC -!- SIMILARITY: Belongs to the calponin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32170.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF465519; AAM54133.1; -; mRNA.
DR EMBL; AF149291; AAD37787.1; -; mRNA.
DR EMBL; AK172892; BAD32170.1; ALT_INIT; mRNA.
DR EMBL; AK151576; BAE30516.1; -; mRNA.
DR EMBL; AK167395; BAE39484.1; -; mRNA.
DR EMBL; AK167922; BAE39928.1; -; mRNA.
DR EMBL; AK171088; BAE42241.1; -; mRNA.
DR EMBL; CH466520; EDL39010.1; -; Genomic_DNA.
DR EMBL; BC009076; AAH09076.1; -; mRNA.
DR EMBL; BC049861; AAH49861.1; -; mRNA.
DR CCDS; CCDS35784.1; -.
DR RefSeq; NP_848713.1; NM_178598.2.
DR AlphaFoldDB; Q9WVA4; -.
DR SMR; Q9WVA4; -.
DR BioGRID; 203961; 6.
DR IntAct; Q9WVA4; 2.
DR MINT; Q9WVA4; -.
DR STRING; 10090.ENSMUSP00000106861; -.
DR iPTMnet; Q9WVA4; -.
DR PhosphoSitePlus; Q9WVA4; -.
DR SwissPalm; Q9WVA4; -.
DR CPTAC; non-CPTAC-3617; -.
DR EPD; Q9WVA4; -.
DR jPOST; Q9WVA4; -.
DR MaxQB; Q9WVA4; -.
DR PaxDb; Q9WVA4; -.
DR PeptideAtlas; Q9WVA4; -.
DR PRIDE; Q9WVA4; -.
DR ProteomicsDB; 262927; -.
DR Antibodypedia; 1099; 252 antibodies from 31 providers.
DR DNASU; 21346; -.
DR Ensembl; ENSMUST00000111228; ENSMUSP00000106859; ENSMUSG00000026547.
DR Ensembl; ENSMUST00000111230; ENSMUSP00000106861; ENSMUSG00000026547.
DR GeneID; 21346; -.
DR KEGG; mmu:21346; -.
DR UCSC; uc007dqp.1; mouse.
DR CTD; 8407; -.
DR MGI; MGI:1312985; Tagln2.
DR VEuPathDB; HostDB:ENSMUSG00000026547; -.
DR eggNOG; KOG2046; Eukaryota.
DR GeneTree; ENSGT00940000158886; -.
DR HOGENOM; CLU_055232_1_0_1; -.
DR InParanoid; Q9WVA4; -.
DR OMA; IQWITSQ; -.
DR OrthoDB; 861989at2759; -.
DR PhylomeDB; Q9WVA4; -.
DR TreeFam; TF313921; -.
DR BioGRID-ORCS; 21346; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Tagln2; mouse.
DR PRO; PR:Q9WVA4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9WVA4; protein.
DR Bgee; ENSMUSG00000026547; Expressed in pyloric antrum and 241 other tissues.
DR ExpressionAtlas; Q9WVA4; baseline and differential.
DR Genevisible; Q9WVA4; MM.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
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; IPR001061; TAGLN2.
DR PANTHER; PTHR18959:SF41; PTHR18959:SF41; 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; Direct protein sequencing; Isopeptide bond; Methylation;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P37802"
FT CHAIN 2..199
FT /note="Transgelin-2"
FT /id="PRO_0000204787"
FT DOMAIN 24..136
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 174..199
FT /note="Calponin-like"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P37802"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P37802"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P37802"
FT MOD_RES 20
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P37802"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 182
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 196
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P37802"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37802"
FT CONFLICT 46
FT /note="Q -> K (in Ref. 4; BAE39928)"
FT /evidence="ECO:0000305"
FT CONFLICT 192..199
FT /note="YGMPRQIL -> MGCHGDPLIILSLLPLPSMNG (in Ref. 2;
FT AAD37787)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 199 AA; 22395 MW; 3CA18C829CA2CC99 CRC64;
MANRGPSYGL SREVQQKIEK QYDADLEQIL IQWITTQCRE DVGQPQPGRE NFQKWLKDGT
VLCKLINSLY PEGQAPVKKI QASSMAFKQM EQISQFLQAA ERYGINTTDI FQTVDLWEGK
NMACVQRTLM NLGGLAVARD DGLFSGDPNW FPKKSKENPR NFSDNQLQEG KNVIGLQMGT
NRGASQAGMT GYGMPRQIL
