TMOD2_MOUSE
ID TMOD2_MOUSE Reviewed; 351 AA.
AC Q9JKK7; Q3UH50; Q8BGX9; Q9CUK4; Q9JLH9;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Tropomodulin-2;
DE AltName: Full=Neuronal tropomodulin;
DE Short=N-Tmod;
GN Name=Tmod2;
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] (ISOFORM 1).
RA Conley C.A., Fowler V.M.;
RT "Identifying novel tropomodulin isoforms.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=10662549; DOI=10.1006/geno.1999.6061;
RA Cox P.R., Zoghbi H.Y.;
RT "Sequencing, expression analysis, and mapping of three unique human
RT tropomodulin genes and their mouse orthologs.";
RL Genomics 63:97-107(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, Hippocampus, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP PROTEIN SEQUENCE OF 31-51; 82-93 AND 258-279, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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).
CC -!- FUNCTION: Blocks the elongation and depolymerization of the actin
CC filaments at the pointed end. The Tmod/TM complex contributes to the
CC formation of the short actin protofilament, which in turn defines the
CC geometry of the membrane skeleton (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to the N-terminus of tropomyosin and to actin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9JKK7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JKK7-2; Sequence=VSP_024896, VSP_024897;
CC Name=3;
CC IsoId=Q9JKK7-3; Sequence=VSP_024895;
CC -!- TISSUE SPECIFICITY: Neuronal-tissue specific.
CC -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}.
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DR EMBL; AF237629; AAF45297.1; -; mRNA.
DR EMBL; AF177170; AAF31669.1; -; mRNA.
DR EMBL; AK015719; BAB29946.3; -; mRNA.
DR EMBL; AK076562; BAC36394.1; -; mRNA.
DR EMBL; AK079077; BAC37527.1; -; mRNA.
DR EMBL; AK147581; BAE28007.1; -; mRNA.
DR EMBL; AK164178; BAE37665.1; -; mRNA.
DR EMBL; BC061124; AAH61124.1; -; mRNA.
DR CCDS; CCDS23345.1; -. [Q9JKK7-1]
DR RefSeq; NP_001033799.1; NM_001038710.1. [Q9JKK7-1]
DR RefSeq; NP_057920.2; NM_016711.3. [Q9JKK7-1]
DR RefSeq; XP_006511330.1; XM_006511267.3. [Q9JKK7-1]
DR RefSeq; XP_006511331.1; XM_006511268.2. [Q9JKK7-1]
DR RefSeq; XP_017168948.1; XM_017313459.1. [Q9JKK7-1]
DR RefSeq; XP_017168949.1; XM_017313460.1.
DR AlphaFoldDB; Q9JKK7; -.
DR SMR; Q9JKK7; -.
DR BioGRID; 206139; 6.
DR IntAct; Q9JKK7; 5.
DR MINT; Q9JKK7; -.
DR STRING; 10090.ENSMUSP00000096152; -.
DR iPTMnet; Q9JKK7; -.
DR PhosphoSitePlus; Q9JKK7; -.
DR EPD; Q9JKK7; -.
DR MaxQB; Q9JKK7; -.
DR PaxDb; Q9JKK7; -.
DR PeptideAtlas; Q9JKK7; -.
DR PRIDE; Q9JKK7; -.
DR ProteomicsDB; 259438; -. [Q9JKK7-1]
DR ProteomicsDB; 259439; -. [Q9JKK7-2]
DR ProteomicsDB; 259440; -. [Q9JKK7-3]
DR Antibodypedia; 24900; 190 antibodies from 26 providers.
DR DNASU; 50876; -.
DR Ensembl; ENSMUST00000064433; ENSMUSP00000069956; ENSMUSG00000032186. [Q9JKK7-1]
DR Ensembl; ENSMUST00000098552; ENSMUSP00000096152; ENSMUSG00000032186. [Q9JKK7-1]
DR Ensembl; ENSMUST00000164100; ENSMUSP00000126739; ENSMUSG00000032186. [Q9JKK7-1]
DR Ensembl; ENSMUST00000215036; ENSMUSP00000150750; ENSMUSG00000032186. [Q9JKK7-1]
DR Ensembl; ENSMUST00000215614; ENSMUSP00000150413; ENSMUSG00000032186. [Q9JKK7-1]
DR GeneID; 50876; -.
DR KEGG; mmu:50876; -.
DR UCSC; uc009qsj.1; mouse. [Q9JKK7-1]
DR UCSC; uc009qsp.1; mouse. [Q9JKK7-2]
DR CTD; 29767; -.
DR MGI; MGI:1355335; Tmod2.
DR VEuPathDB; HostDB:ENSMUSG00000032186; -.
DR eggNOG; KOG3735; Eukaryota.
DR GeneTree; ENSGT00940000160631; -.
DR HOGENOM; CLU_031052_0_1_1; -.
DR InParanoid; Q9JKK7; -.
DR OMA; DCVPFTG; -.
DR OrthoDB; 1025132at2759; -.
DR PhylomeDB; Q9JKK7; -.
DR TreeFam; TF315841; -.
DR Reactome; R-MMU-390522; Striated Muscle Contraction.
DR BioGRID-ORCS; 50876; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Tmod2; mouse.
DR PRO; PR:Q9JKK7; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9JKK7; protein.
DR Bgee; ENSMUSG00000032186; Expressed in lateral septal nucleus and 193 other tissues.
DR ExpressionAtlas; Q9JKK7; baseline and differential.
DR Genevisible; Q9JKK7; MM.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0030016; C:myofibril; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005865; C:striated muscle thin filament; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0005523; F:tropomyosin binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0007611; P:learning or memory; IMP:MGI.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0030239; P:myofibril assembly; IBA:GO_Central.
DR GO; GO:0007270; P:neuron-neuron synaptic transmission; IMP:MGI.
DR GO; GO:0051694; P:pointed-end actin filament capping; IEA:InterPro.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; IMP:MGI.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR004934; TMOD.
DR InterPro; IPR030130; TMOD2.
DR PANTHER; PTHR10901; PTHR10901; 1.
DR PANTHER; PTHR10901:SF15; PTHR10901:SF15; 1.
DR Pfam; PF03250; Tropomodulin; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Phosphoprotein; Reference proteome.
FT CHAIN 1..351
FT /note="Tropomodulin-2"
FT /id="PRO_0000186132"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70566"
FT VAR_SEQ 1..191
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024895"
FT VAR_SEQ 165..240
FT /note="NVVKGEKAKPVFEEPPNPTNVEASLQQMKANDPSLQEVNLNNIKNIPIPTLK
FT EFAKSLETNTHVKKFSLAATRSND -> SKLTRALGAWEVPEPAWCMFHQAQCLVSASP
FT SVVTQGTQSYRTHIRGTSSSGEKKSIPDKFAQSAQNANKVFCSKG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024896"
FT VAR_SEQ 241..351
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024897"
FT CONFLICT 26..27
FT /note="EE -> KR (in Ref. 3; BAB29946)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="E -> K (in Ref. 3; BAB29946)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="E -> Q (in Ref. 1; AAF45297)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="S -> F (in Ref. 2; AAF31669)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 39511 MW; 640E9577D4C9CA16 CRC64;
MALPFQKGLE KYKNIDEDEL LGKLSEEELK QLENVLDDLD PESATLPAGF RQKDQTQKAA
TGPFDREHLL MYLEKEALEQ KDREDFVPFT GEKKGRVFIP KEKPVETRKE EKVTLDPELE
EALASASDTE LYDLAAVLGV HNLLNNPKFD EETTNGEGRK GPVRNVVKGE KAKPVFEEPP
NPTNVEASLQ QMKANDPSLQ EVNLNNIKNI PIPTLKEFAK SLETNTHVKK FSLAATRSND
PVALAFAEML KVNKTLKSLN VESNFITGTG ILALVEALRE NDTLTEIKID NQRQQLGTAV
EMEIAQMLEE NSRILKFGYQ FTKQGPRTRV AAAITKNNDL VRKKRVEGDR R
