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   27-MAR-2024, entry version 139.
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   GlyGen; P70566; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P70566; -.
DR   PhosphoSitePlus; P70566; -.
DR   jPOST; P70566; -.
DR   PaxDb; 10116-ENSRNOP00000014124; -.
DR   Ensembl; ENSRNOT00000014124.4; ENSRNOP00000014124.2; ENSRNOG00000010447.5.
DR   Ensembl; ENSRNOT00055012489; ENSRNOP00055009910; ENSRNOG00055007487.
DR   Ensembl; ENSRNOT00060031466; ENSRNOP00060025536; ENSRNOG00060018326.
DR   Ensembl; ENSRNOT00065028415; ENSRNOP00065022475; ENSRNOG00065017026.
DR   GeneID; 58814; -.
DR   KEGG; rno:58814; -.
DR   UCSC; RGD:61948; rat.
DR   AGR; RGD:61948; -.
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   OrthoDB; 2883785at2759; -.
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 cell types or tissues.
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:0005865; C:striated muscle thin filament; IBA:GO_Central.
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; Ribonuclease Inhibitor; 1.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR004934; TMOD.
DR   PANTHER; PTHR10901; TROPOMODULIN; 1.
DR   PANTHER; PTHR10901:SF15; TROPOMODULIN-2; 1.
DR   Pfam; PF03250; Tropomodulin; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   World-2DPAGE; 0004:P70566; -.
DR   Genevisible; P70566; RN.
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
//