ID TMO4_HUMAN STANDARD; PRT; 345 AA. AC Q9NZQ9; Q8WVL3; Q9UKH2; DT 15-JUN-2002 (Rel. 41, Created) DT 15-JUN-2002 (Rel. 41, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE Skeletal muscle tropomodulin (Sk-Tmod) (Tropomodulin 4). GN TMOD4. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99428519; PubMed=10497209; 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 SEQUENCE FROM N.A., AND TISSUE SPECIFICITY. RX MEDLINE=20130118; PubMed=10662549; 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 SEQUENCE FROM N.A. 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 SEQUENCE FROM N.A. RC TISSUE=Skeletal muscle; RA Strausberg R.; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. 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 -!- 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; -. DR EMBL; AF177173; AAF31672.1; -. DR EMBL; AF321183; AAK06765.1; -. DR EMBL; BC017810; AAH17810.1; -. DR Genew; HGNC:11874; TMOD4. DR MIM; 605834; -. DR InterPro; IPR004934; Tropomodulin. DR Pfam; PF03250; Tropomodulin; 1. KW Cytoskeleton; Actin-binding. FT CONFLICT 283 283 T -> I (IN REF. 1). FT CONFLICT 309 309 C -> R (IN REF. 4). 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 //