TMOD2_RAT
ID TMOD2_RAT Reviewed; 351 AA.
AC P70566;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Tropomodulin-2;
DE AltName: Full=Neuronal tropomodulin;
DE Short=N-Tmod;
GN Name=Tmod2; Synonyms=Ntmod;
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=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8886980; DOI=10.1242/jcs.109.9.2299;
RA Watakabe A., Kobayashi R., Helfman D.M.;
RT "N-tropomodulin: a novel isoform of tropomodulin identified as the major
RT binding protein to brain tropomyosin.";
RL J. Cell Sci. 109:2299-2310(1996).
RN [2]
RP PROTEIN SEQUENCE OF 82-93 AND 238-251, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Chen W.-Q.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, 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: 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. Binds to
CC TMBr3 as well as to other low molecular mass tropomyosins (TM5a or
CC TM5), but not to high molecular mass tropomyosins (TM2 or TMBr1).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Neuronal-tissue specific.
CC -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}.
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DR EMBL; U59240; AAC52854.1; -; mRNA.
DR RefSeq; NP_113801.1; NM_031613.1.
DR RefSeq; XP_006243469.1; XM_006243407.3.
DR RefSeq; XP_006243470.1; XM_006243408.3.
DR RefSeq; XP_008764553.1; XM_008766331.2.
DR RefSeq; XP_017451363.1; XM_017595874.1.
DR AlphaFoldDB; P70566; -.
DR SMR; P70566; -.
DR BioGRID; 248623; 5.
DR IntAct; P70566; 3.
DR MINT; P70566; -.
DR STRING; 10116.ENSRNOP00000014124; -.
DR iPTMnet; P70566; -.
DR PhosphoSitePlus; P70566; -.
DR World-2DPAGE; 0004:P70566; -.
DR jPOST; P70566; -.
DR PaxDb; P70566; -.
DR PRIDE; P70566; -.
DR Ensembl; ENSRNOT00000014124; ENSRNOP00000014124; ENSRNOG00000010447.
DR GeneID; 58814; -.
DR KEGG; rno:58814; -.
DR UCSC; RGD:61948; rat.
DR CTD; 29767; -.
DR RGD; 61948; Tmod2.
DR eggNOG; KOG3735; Eukaryota.
DR GeneTree; ENSGT00940000160631; -.
DR HOGENOM; CLU_031052_0_1_1; -.
DR InParanoid; P70566; -.
DR OMA; DCVPFTG; -.
DR OrthoDB; 1025132at2759; -.
DR PhylomeDB; P70566; -.
DR TreeFam; TF315841; -.
DR Reactome; R-RNO-390522; Striated Muscle Contraction.
DR PRO; PR:P70566; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000010447; Expressed in frontal cortex and 15 other tissues.
DR Genevisible; P70566; RN.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0030016; C:myofibril; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0005523; F:tropomyosin binding; IDA:RGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
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; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..351
FT /note="Tropomodulin-2"
FT /id="PRO_0000186133"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 351 AA; 39492 MW; 24F5C67EA897983E CRC64;
MALPFQKGLE KYKNIDEDEL LGKLSEEELK QLENVLDDLD PESATLPAGF RQKDQTQKAA
TGPFDREHLL MYLEKEALEQ KDREDFVPFT GEKKGRVFIP KEKPVETRKE EKVTLDPELE
EALASASDTE LYDLAAVLGV HNLLNNPKFD EETTNGQGRK GPVRNVVKGE KAKPVFEEPP
NPTNVEASLQ QMKANDPSLQ EVNLNNIKNI PIPTLKEFAK ALETNTHVRK FSLAATRSND
PVALAFAEML KVNKTLKSLN VESNFITGAG ILALVEALRE NDTLTEIKID NQRQQLGTAV
EMEIAQMLEE NSRILKFGYQ FTKQGPRTRV AAAITKNNDL VRKKRVEGDR R