ID   TMOD2_HUMAN             Reviewed;         351 AA.
AC   Q9NZR1; B4DEW6;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Tropomodulin-2;
DE   AltName: Full=Neuronal tropomodulin;
DE            Short=N-Tmod;
GN   Name=TMOD2; Synonyms=NTMOD;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Retina;
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 14-23; 82-93; 194-208 AND 238-251, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
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   -!- INTERACTION:
CC       Q9NZR1; D3DTS7: PMP22; NbExp=3; IntAct=EBI-4289968, EBI-25882629;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NZR1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NZR1-2; Sequence=VSP_041506;
CC   -!- TISSUE SPECIFICITY: Neuronal-tissue specific.
CC       {ECO:0000269|PubMed:10662549}.
CC   -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}.
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DR   EMBL; AF177169; AAF31668.1; -; mRNA.
DR   EMBL; AK293823; BAG57227.1; -; mRNA.
DR   EMBL; AC026770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090971; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC064961; AAH64961.1; -; mRNA.
DR   CCDS; CCDS10144.1; -. [Q9NZR1-1]
DR   CCDS; CCDS45260.1; -. [Q9NZR1-2]
DR   RefSeq; NP_001136357.1; NM_001142885.1. [Q9NZR1-2]
DR   RefSeq; NP_055363.1; NM_014548.3. [Q9NZR1-1]
DR   AlphaFoldDB; Q9NZR1; -.
DR   SMR; Q9NZR1; -.
DR   BioGRID; 118900; 69.
DR   IntAct; Q9NZR1; 24.
DR   STRING; 9606.ENSP00000249700; -.
DR   GlyGen; Q9NZR1; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q9NZR1; -.
DR   PhosphoSitePlus; Q9NZR1; -.
DR   BioMuta; TMOD2; -.
DR   DMDM; 23396886; -.
DR   UCD-2DPAGE; Q9NZR1; -.
DR   EPD; Q9NZR1; -.
DR   jPOST; Q9NZR1; -.
DR   MassIVE; Q9NZR1; -.
DR   MaxQB; Q9NZR1; -.
DR   PaxDb; Q9NZR1; -.
DR   PeptideAtlas; Q9NZR1; -.
DR   PRIDE; Q9NZR1; -.
DR   ProteomicsDB; 83490; -. [Q9NZR1-1]
DR   ProteomicsDB; 83491; -. [Q9NZR1-2]
DR   Antibodypedia; 24900; 190 antibodies from 26 providers.
DR   DNASU; 29767; -.
DR   Ensembl; ENST00000249700.9; ENSP00000249700.4; ENSG00000128872.10. [Q9NZR1-1]
DR   Ensembl; ENST00000435126.6; ENSP00000404590.2; ENSG00000128872.10. [Q9NZR1-2]
DR   GeneID; 29767; -.
DR   KEGG; hsa:29767; -.
DR   MANE-Select; ENST00000249700.9; ENSP00000249700.4; NM_014548.4; NP_055363.1.
DR   UCSC; uc002abk.4; human. [Q9NZR1-1]
DR   CTD; 29767; -.
DR   DisGeNET; 29767; -.
DR   GeneCards; TMOD2; -.
DR   HGNC; HGNC:11872; TMOD2.
DR   HPA; ENSG00000128872; Tissue enriched (brain).
DR   MIM; 602928; gene.
DR   neXtProt; NX_Q9NZR1; -.
DR   OpenTargets; ENSG00000128872; -.
DR   PharmGKB; PA36573; -.
DR   VEuPathDB; HostDB:ENSG00000128872; -.
DR   eggNOG; KOG3735; Eukaryota.
DR   GeneTree; ENSGT00940000160631; -.
DR   HOGENOM; CLU_031052_0_1_1; -.
DR   InParanoid; Q9NZR1; -.
DR   OMA; DCVPFTG; -.
DR   OrthoDB; 1025132at2759; -.
DR   PhylomeDB; Q9NZR1; -.
DR   TreeFam; TF315841; -.
DR   PathwayCommons; Q9NZR1; -.
DR   Reactome; R-HSA-390522; Striated Muscle Contraction.
DR   SignaLink; Q9NZR1; -.
DR   BioGRID-ORCS; 29767; 15 hits in 1078 CRISPR screens.
DR   ChiTaRS; TMOD2; human.
DR   GeneWiki; TMOD2; -.
DR   GenomeRNAi; 29767; -.
DR   Pharos; Q9NZR1; Tbio.
DR   PRO; PR:Q9NZR1; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q9NZR1; protein.
DR   Bgee; ENSG00000128872; Expressed in Brodmann (1909) area 23 and 164 other tissues.
DR   ExpressionAtlas; Q9NZR1; baseline and differential.
DR   Genevisible; Q9NZR1; HS.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0030016; C:myofibril; IBA:GO_Central.
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; IEA:UniProtKB-KW.
DR   GO; GO:0005523; F:tropomyosin binding; IBA:GO_Central.
DR   GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR   GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR   GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR   GO; GO:0030239; P:myofibril assembly; IBA:GO_Central.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0007270; P:neuron-neuron synaptic transmission; IEA:Ensembl.
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; IEA:Ensembl.
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_0000186131"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P70566"
FT   VAR_SEQ         209..244
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041506"
FT   VARIANT         63
FT                   /note="P -> A (in dbSNP:rs34791185)"
FT                   /id="VAR_052399"
FT   CONFLICT        284
FT                   /note="L -> M (in Ref. 2; BAG57227)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   351 AA;  39595 MW;  547004595FCD6385 CRC64;
     MALPFQKELE KYKNIDEDEL LGKLSEEELK QLENVLDDLD PESAMLPAGF RQKDQTQKAA
     TGPFDREHLL MYLEKEALEQ KDREDFVPFT GEKKGRVFIP KEKPIETRKE EKVTLDPELE
     EALASASDTE LYDLAAVLGV HNLLNNPKFD EETANNKGGK GPVRNVVKGE KVKPVFEEPP
     NPTNVEISLQ QMKANDPSLQ EVNLNNIKNI PIPTLREFAK ALETNTHVKK FSLAATRSND
     PVAIAFADML KVNKTLTSLN IESNFITGTG ILALVEALKE NDTLTEIKID NQRQQLGTAV
     EMEIAQMLEE NSRILKFGYQ FTKQGPRTRV AAAITKNNDL VRKKRVEADR R