ID TMOD4_HUMAN Reviewed; 345 AA. AC Q9NZQ9; Q5JR83; Q8WVL3; Q9UKH2; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 16-MAY-2012, entry version 85. DE RecName: Full=Tropomodulin-4; DE AltName: Full=Skeletal muscle tropomodulin; DE Short=Sk-Tmod; GN Name=TMOD4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=99428519; PubMed=10497209; DOI=10.1074/jbc.274.40.28466; RA Almenar-Queralt A., Lee A., Conley C.A., Ribas de Pouplana L., RA Fowler V.M.; RT "Identification of a novel tropomodulin isoform, skeletal RT tropomodulin, that caps actin filament pointed ends in fast skeletal RT muscle."; RL J. Biol. Chem. 274:28466-28475(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RX MEDLINE=20130118; 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 [GENOMIC DNA]. RA Durling H.J., Laing N.G.; RT "Homo sapiens tropomodulin 4 (TMOD4) genomic sequence."; RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Cox P.R., Siddique T., Zoghbi H.Y.; RT "Genomic organization of tropomodulins 2 and 4 and intergenic splicing RT of YL-1 and TMOD4."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- FUNCTION: Blocks the elongation and depolymerization of the actin CC filaments at the pointed end. The Tmod/TM complex contributes to CC the formation of the short actin protofilament, which in turn CC defines the geometry of the membrane skeleton. CC -!- SUBUNIT: Binds to the N-terminus of tropomyosin and to actin. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal msucle. CC -!- SIMILARITY: Belongs to the tropomodulin family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF165217; AAF01277.1; -; mRNA. DR EMBL; AF177173; AAF31672.1; -; mRNA. DR EMBL; AF321183; AAK06765.1; -; Genomic_DNA. DR EMBL; AF393375; AAM73676.1; -; Genomic_DNA. DR EMBL; AL592424; CAI16383.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53465.1; -; Genomic_DNA. DR EMBL; BC017810; AAH17810.1; -; mRNA. DR IPI; IPI00303200; -. DR RefSeq; NP_037485.2; NM_013353.2. DR UniGene; Hs.709681; -. DR ProteinModelPortal; Q9NZQ9; -. DR SMR; Q9NZQ9; 179-344. DR STRING; Q9NZQ9; -. DR PhosphoSite; Q9NZQ9; -. DR DMDM; 23396885; -. DR PRIDE; Q9NZQ9; -. DR DNASU; 29765; -. DR Ensembl; ENST00000295314; ENSP00000295314; ENSG00000163157. DR GeneID; 29765; -. DR KEGG; hsa:29765; -. DR UCSC; uc001exb.3; human. DR CTD; 29765; -. DR GeneCards; GC01M151142; -. DR H-InvDB; HIX0001052; -. DR HGNC; HGNC:11874; TMOD4. DR HPA; HPA028203; -. DR MIM; 605834; gene. DR neXtProt; NX_Q9NZQ9; -. DR PharmGKB; PA36575; -. DR eggNOG; NOG329422; -. DR GeneTree; ENSGT00550000074341; -. DR HOGENOM; HOG000261624; -. DR HOVERGEN; HBG056172; -. DR InParanoid; Q9NZQ9; -. DR KO; K10370; -. DR OMA; TNTYVRS; -. DR OrthoDB; EOG4255T7; -. DR PhylomeDB; Q9NZQ9; -. DR NextBio; 52264; -. DR ArrayExpress; Q5JR83; -. DR Bgee; Q9NZQ9; -. DR CleanEx; HS_TMOD4; -. DR Genevestigator; Q9NZQ9; -. DR GermOnline; ENSG00000163157; Homo sapiens. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW. DR GO; GO:0005523; F:tropomyosin binding; TAS:ProtInc. DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc. DR InterPro; IPR004934; Tropomodulin. DR PANTHER; PTHR10901; Tropomodulin; 1. DR Pfam; PF03250; Tropomodulin; 1. PE 2: Evidence at transcript level; KW Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton; KW Polymorphism; Reference proteome. FT CHAIN 1 345 Tropomodulin-4. FT /FTId=PRO_0000186136. FT VARIANT 336 336 N -> S (in dbSNP:rs11800088). FT /FTId=VAR_052400. FT CONFLICT 283 283 T -> I (in Ref. 1; AAF01277). FT CONFLICT 309 309 C -> R (in Ref. 7; AAH17810). SQ SEQUENCE 345 AA; 39335 MW; 3ACE2692EF52E2CB CRC64; MSSYQKELEK YRDIDEDEIL RTLSPEELEQ LDCELQEMDP ENMLLPAGLR QRDQTKKSPT GPLDREALLQ YLEQQALEVK ERDDLVPFTG EKKGKPYIQP KREIPAEEQI TLEPELEEAL AHATDAEMCD IAAILDMYTL MSNKQYYDAL CSGEICNTEG ISSVVQPDKY KPVPDEPPNP TNIEEILKRV RSNDKELEEV NLNNIQDIPI PMLSELCEAM KANTYVRSFS LVATRSGDPI ANAVADMLRE NRSLQSLNIE SNFISSTGLM AVLKAVRENA TLTELRVDNQ RQWPGDAVEM EMATVLEQCP SIVRFGYHFT QQGPRARAAQ AMTRNNELRR QQKKR //