Full text data of TMOD1
TMOD1
(D9S57E, TMOD)
[Confidence: high (present in two of the MS resources)]
Tropomodulin-1 (Erythrocyte tropomodulin; E-Tmod)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Tropomodulin-1 (Erythrocyte tropomodulin; E-Tmod)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00002375
IPI00002375 Tropomodulin 1 Tropomodulin 1 membrane 2 8 2 1 3 n/a 2 n/a 27 n/a 1 n/a 3 1 n/a n/a n/a 11 8 9 cytoskeleton n/a found at its expected molecular weight found at molecular weight
IPI00002375 Tropomodulin 1 Tropomodulin 1 membrane 2 8 2 1 3 n/a 2 n/a 27 n/a 1 n/a 3 1 n/a n/a n/a 11 8 9 cytoskeleton n/a found at its expected molecular weight found at molecular weight
UniProt
P28289
ID TMOD1_HUMAN Reviewed; 359 AA.
AC P28289; B2RB77; Q9BUF1;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-1992, sequence version 1.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Tropomodulin-1;
DE AltName: Full=Erythrocyte tropomodulin;
DE Short=E-Tmod;
GN Name=TMOD1; Synonyms=D9S57E, TMOD;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Fetal liver;
RX PubMed=1370827;
RA Sung L.A., Fowler V.M., Lambert K., Sussman M.A., Karr D., Chien S.;
RT "Molecular cloning and characterization of human fetal liver
RT tropomodulin. A tropomyosin-binding protein.";
RL J. Biol. Chem. 267:2616-2621(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11054557; DOI=10.1016/S0378-1119(00)00327-9;
RA Chu X., Thompson D., Yee L.J., Sung L.A.;
RT "Genomic organization of mouse and human erythrocyte tropomodulin
RT genes encoding the pointed end capping protein for the actin
RT filaments.";
RL Gene 256:271-281(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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).
RN [6]
RP FUNCTION, AND INTERACTION WITH TPM3.
RX PubMed=8002995; DOI=10.1006/bbrc.1994.1747;
RA Sung L.A., Lin J.J.-C.;
RT "Erythrocyte tropomodulin binds to the N-terminus of hTM5, a
RT tropomyosin isoform encoded by the gamma-tropomyosin gene.";
RL Biochem. Biophys. Res. Commun. 201:627-634(1994).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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. May play an
CC important role in regulating the organization of actin filaments
CC by preferentially binding to a specific tropomyosin isoform at its
CC N-terminus.
CC -!- SUBUNIT: Binds to the N-terminus of isoforms 2/3 of TPM3 and to
CC actin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Highly expressed in the erythrocyte, heart and
CC skeletal muscle.
CC -!- SIMILARITY: Belongs to the tropomodulin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M77016; AAA61224.1; -; mRNA.
DR EMBL; AF288155; AAG30124.1; -; Genomic_DNA.
DR EMBL; AF288147; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AF288148; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AF288149; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AF288150; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AF288151; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AF288152; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AF288153; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AF288154; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AK314533; BAG37124.1; -; mRNA.
DR EMBL; AL162385; CAI12854.1; -; Genomic_DNA.
DR EMBL; BC002660; AAH02660.1; -; mRNA.
DR PIR; A42336; A42336.
DR RefSeq; NP_001159588.1; NM_001166116.1.
DR RefSeq; NP_003266.1; NM_003275.3.
DR UniGene; Hs.404289; -.
DR UniGene; Hs.723236; -.
DR ProteinModelPortal; P28289; -.
DR SMR; P28289; 179-344.
DR IntAct; P28289; 1.
DR STRING; 9606.ENSP00000259365; -.
DR PhosphoSite; P28289; -.
DR DMDM; 135922; -.
DR PaxDb; P28289; -.
DR PeptideAtlas; P28289; -.
DR PRIDE; P28289; -.
DR DNASU; 7111; -.
DR Ensembl; ENST00000259365; ENSP00000259365; ENSG00000136842.
DR Ensembl; ENST00000395211; ENSP00000378637; ENSG00000136842.
DR GeneID; 7111; -.
DR KEGG; hsa:7111; -.
DR UCSC; uc004axk.2; human.
DR CTD; 7111; -.
DR GeneCards; GC09P100263; -.
DR HGNC; HGNC:11871; TMOD1.
DR HPA; HPA051202; -.
DR MIM; 190930; gene.
DR neXtProt; NX_P28289; -.
DR PharmGKB; PA36572; -.
DR eggNOG; NOG329422; -.
DR HOGENOM; HOG000261624; -.
DR HOVERGEN; HBG056172; -.
DR InParanoid; P28289; -.
DR KO; K10370; -.
DR OMA; RQKDQTK; -.
DR OrthoDB; EOG7D59Q1; -.
DR PhylomeDB; P28289; -.
DR Reactome; REACT_17044; Muscle contraction.
DR ChiTaRS; TMOD1; human.
DR GeneWiki; TMOD1; -.
DR GenomeRNAi; 7111; -.
DR NextBio; 27835; -.
DR PRO; PR:P28289; -.
DR ArrayExpress; P28289; -.
DR Bgee; P28289; -.
DR CleanEx; HS_TMOD1; -.
DR Genevestigator; P28289; -.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0030016; C:myofibril; IEA:Ensembl.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
DR GO; GO:0030239; P:myofibril assembly; IEA:Ensembl.
DR InterPro; IPR004934; Tropomodulin.
DR PANTHER; PTHR10901; PTHR10901; 1.
DR Pfam; PF03250; Tropomodulin; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Reference proteome.
FT CHAIN 1 359 Tropomodulin-1.
FT /FTId=PRO_0000186128.
FT REGION 39 138 Tropomyosin-binding (Potential).
FT CONFLICT 17 17 E -> K (in Ref. 5; AAH02660).
FT CONFLICT 76 76 K -> E (in Ref. 3; BAG37124).
FT CONFLICT 289 289 N -> S (in Ref. 3; BAG37124).
SQ SEQUENCE 359 AA; 40569 MW; 732B7D7798B88A48 CRC64;
MSYRRELEKY RDLDEDEILG ALTEEELRTL ENELDELDPD NALLPAGLRQ KDQTTKAPTG
PFKREELLDH LEKQAKEFKD REDLVPYTGE KRGKVWVPKQ KPLDPVLESV TLEPELEEAL
ANASDAELCD IAAILGMHTL MSNQQYYQAL SSSSIMNKEG LNSVIKPTQY KPVPDEEPNS
TDVEETLERI KNNDPKLEEV NLNNIRNIPI PTLKAYAEAL KENSYVKKFS IVGTRSNDPV
AYALAEMLKE NKVLKTLNVE SNFISGAGIL RLVEALPYNT SLVEMKIDNQ SQPLGNKVEM
EIVSMLEKNA TLLKFGYHFT QQGPRLRASN AMMNNNDLVR KRRLADLTGP IIPKCRSGV
//
ID TMOD1_HUMAN Reviewed; 359 AA.
AC P28289; B2RB77; Q9BUF1;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-1992, sequence version 1.
DT 22-JAN-2014, entry version 115.
DE RecName: Full=Tropomodulin-1;
DE AltName: Full=Erythrocyte tropomodulin;
DE Short=E-Tmod;
GN Name=TMOD1; Synonyms=D9S57E, TMOD;
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], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Fetal liver;
RX PubMed=1370827;
RA Sung L.A., Fowler V.M., Lambert K., Sussman M.A., Karr D., Chien S.;
RT "Molecular cloning and characterization of human fetal liver
RT tropomodulin. A tropomyosin-binding protein.";
RL J. Biol. Chem. 267:2616-2621(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11054557; DOI=10.1016/S0378-1119(00)00327-9;
RA Chu X., Thompson D., Yee L.J., Sung L.A.;
RT "Genomic organization of mouse and human erythrocyte tropomodulin
RT genes encoding the pointed end capping protein for the actin
RT filaments.";
RL Gene 256:271-281(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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).
RN [6]
RP FUNCTION, AND INTERACTION WITH TPM3.
RX PubMed=8002995; DOI=10.1006/bbrc.1994.1747;
RA Sung L.A., Lin J.J.-C.;
RT "Erythrocyte tropomodulin binds to the N-terminus of hTM5, a
RT tropomyosin isoform encoded by the gamma-tropomyosin gene.";
RL Biochem. Biophys. Res. Commun. 201:627-634(1994).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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. May play an
CC important role in regulating the organization of actin filaments
CC by preferentially binding to a specific tropomyosin isoform at its
CC N-terminus.
CC -!- SUBUNIT: Binds to the N-terminus of isoforms 2/3 of TPM3 and to
CC actin.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Highly expressed in the erythrocyte, heart and
CC skeletal muscle.
CC -!- SIMILARITY: Belongs to the tropomodulin family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M77016; AAA61224.1; -; mRNA.
DR EMBL; AF288155; AAG30124.1; -; Genomic_DNA.
DR EMBL; AF288147; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AF288148; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AF288149; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AF288150; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AF288151; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AF288152; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AF288153; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AF288154; AAG30124.1; JOINED; Genomic_DNA.
DR EMBL; AK314533; BAG37124.1; -; mRNA.
DR EMBL; AL162385; CAI12854.1; -; Genomic_DNA.
DR EMBL; BC002660; AAH02660.1; -; mRNA.
DR PIR; A42336; A42336.
DR RefSeq; NP_001159588.1; NM_001166116.1.
DR RefSeq; NP_003266.1; NM_003275.3.
DR UniGene; Hs.404289; -.
DR UniGene; Hs.723236; -.
DR ProteinModelPortal; P28289; -.
DR SMR; P28289; 179-344.
DR IntAct; P28289; 1.
DR STRING; 9606.ENSP00000259365; -.
DR PhosphoSite; P28289; -.
DR DMDM; 135922; -.
DR PaxDb; P28289; -.
DR PeptideAtlas; P28289; -.
DR PRIDE; P28289; -.
DR DNASU; 7111; -.
DR Ensembl; ENST00000259365; ENSP00000259365; ENSG00000136842.
DR Ensembl; ENST00000395211; ENSP00000378637; ENSG00000136842.
DR GeneID; 7111; -.
DR KEGG; hsa:7111; -.
DR UCSC; uc004axk.2; human.
DR CTD; 7111; -.
DR GeneCards; GC09P100263; -.
DR HGNC; HGNC:11871; TMOD1.
DR HPA; HPA051202; -.
DR MIM; 190930; gene.
DR neXtProt; NX_P28289; -.
DR PharmGKB; PA36572; -.
DR eggNOG; NOG329422; -.
DR HOGENOM; HOG000261624; -.
DR HOVERGEN; HBG056172; -.
DR InParanoid; P28289; -.
DR KO; K10370; -.
DR OMA; RQKDQTK; -.
DR OrthoDB; EOG7D59Q1; -.
DR PhylomeDB; P28289; -.
DR Reactome; REACT_17044; Muscle contraction.
DR ChiTaRS; TMOD1; human.
DR GeneWiki; TMOD1; -.
DR GenomeRNAi; 7111; -.
DR NextBio; 27835; -.
DR PRO; PR:P28289; -.
DR ArrayExpress; P28289; -.
DR Bgee; P28289; -.
DR CleanEx; HS_TMOD1; -.
DR Genevestigator; P28289; -.
DR GO; GO:0030863; C:cortical cytoskeleton; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0030016; C:myofibril; IEA:Ensembl.
DR GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR GO; GO:0030049; P:muscle filament sliding; TAS:Reactome.
DR GO; GO:0030239; P:myofibril assembly; IEA:Ensembl.
DR InterPro; IPR004934; Tropomodulin.
DR PANTHER; PTHR10901; PTHR10901; 1.
DR Pfam; PF03250; Tropomodulin; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Reference proteome.
FT CHAIN 1 359 Tropomodulin-1.
FT /FTId=PRO_0000186128.
FT REGION 39 138 Tropomyosin-binding (Potential).
FT CONFLICT 17 17 E -> K (in Ref. 5; AAH02660).
FT CONFLICT 76 76 K -> E (in Ref. 3; BAG37124).
FT CONFLICT 289 289 N -> S (in Ref. 3; BAG37124).
SQ SEQUENCE 359 AA; 40569 MW; 732B7D7798B88A48 CRC64;
MSYRRELEKY RDLDEDEILG ALTEEELRTL ENELDELDPD NALLPAGLRQ KDQTTKAPTG
PFKREELLDH LEKQAKEFKD REDLVPYTGE KRGKVWVPKQ KPLDPVLESV TLEPELEEAL
ANASDAELCD IAAILGMHTL MSNQQYYQAL SSSSIMNKEG LNSVIKPTQY KPVPDEEPNS
TDVEETLERI KNNDPKLEEV NLNNIRNIPI PTLKAYAEAL KENSYVKKFS IVGTRSNDPV
AYALAEMLKE NKVLKTLNVE SNFISGAGIL RLVEALPYNT SLVEMKIDNQ SQPLGNKVEM
EIVSMLEKNA TLLKFGYHFT QQGPRLRASN AMMNNNDLVR KRRLADLTGP IIPKCRSGV
//
MIM
190930
*RECORD*
*FIELD* NO
190930
*FIELD* TI
*190930 TROPOMODULIN; TMOD
;;E-TROPOMODULIN; ETMOD
*FIELD* TX
CLONING
Sung et al. (1991, 1992) cloned the tropomodulin gene from human
read morereticulocyte and fetal liver cDNA libraries.
By Northern blot analysis, Sung et al. (1996) showed that the TMOD gene
is expressed in major human tissues at different levels in the following
order: heart and skeletal muscle much greater than in brain, lung, and
pancreas, which is greater than in placenta, liver, and kidney. They
pointed to structural similarities between tropomodulin and the 64-kD
autoantigen in Graves disease (139080) and suggested that the 2 genes
evolved from a common ancestral gene.
Chu et al. (2000) noted that erythrocyte TMOD is a 359-amino acid
globular protein.
By RNA dot blot analysis, Conley et al. (2001) confirmed expression of
ETMOD in almost every tissue tested, with highest abundance in fetal and
adult heart and skeletal muscle.
GENE FUNCTION
Human erythrocyte tropomodulin is a 43-kD tropomyosin-regulating protein
(Gilligan and Bennett, 1993). It may modulate the association of
tropomyosin with the spectrin-actin complex in the erythrocyte membrane
skeleton, and thus the viscoelastic properties of erythrocytes.
Tropomodulin is associated with the pointed end of the actin filaments
(Fowler et al., 1993). Sung et al. (1996) stated that it binds
specifically to the N terminus of tropomyosin and blocks the elongation
and depolarization of tropomyosin-coated actin filaments.
Conley (2001) found that both Tmod and Smlmod (LMOD1; 602715)
cofractionated with tropomyosin in the Triton-insoluble cytoskeleton
fraction of rabbit stomach smooth muscle, and both were solubilized by
high salt. Immunofluorescent localization found Smlmod present along the
length of actin filaments of rat intestinal smooth muscle, while Tmod
stained in a punctate pattern distinct from that of actin filaments or
the dense body marker, alpha-actinin (see 102575). Hypercontraction of
rat intestinal smooth muscle with 10 mM Ca(2+) caused both Smlmod and
Tmod to associate near alpha-actinin at the periphery of actin-rich
contraction bands.
GENE STRUCTURE
Using PCR methods to obtain TMOD genomic clones, Chu et al. (2000)
determined that the TMOD gene contains 9 exons. Chu et al. (2000)
suggested that the use of alternative promoters may account for
tissue-specific expression and regulation.
MAPPING
Sung et al. (1991) mapped the TMOD gene to 9q22.2-q22.3 by in situ
hybridization. By interspecific backcross linkage analysis, Pilz et al.
(1995) mapped the Tmod gene to mouse chromosome 4, and White et al.
(1995) used recombinant inbred strains to map the gene to a region
within 1.0 cM of Mup1 (major urinary protein-1) on chromosome 4.
Lench et al. (1996) created an EST- and STS-based YAC contig map of
9q22.3 and showed that it contains the following genes in this order
(from centromere to telomere): TMOD, XPA (611153), ALDOB (612724), BAAT
(602938). All 4 of these genes map to a syntenic region of mouse
chromosome 4 and are situated in the same order as their counterparts on
human 9q22.3.
*FIELD* RF
1. Chu, X.; Thompson, D.; Yee, L. J.; Sung, L. A.: Genomic organization
of mouse and human erythrocyte tropomodulin genes encoding the pointed
end capping protein for the actin filaments. Gene 256: 271-281,
2000.
2. Conley, C. A.: Leiomodin and tropomodulin in smooth muscle. Am.
J. Physiol. Cell Physiol. 280: C1645-C1656, 2001.
3. Conley, C. A.; Fritz-Six, K. L.; Almenar-Queralt, A.; Fowler, V.
M.: Leiomodins: larger members of the tropomodulin (Tmod) gene family. Genomics 73:
127-139, 2001.
4. Fowler, V. M.; Sussmann, M. A.; Miller, P. G.; Flucher, B. E.;
Daniels, M. P.: Tropomodulin is associated with the free (pointed)
ends of the thin filaments in rat skeletal muscle. J. Cell Biol. 120:
411-420, 1993.
5. Gilligan, D. M.; Bennett, V.: The junctional complex of the membrane
skeleton. Semin. Hemat. 30: 74-83, 1993.
6. Lench, N. J.; Telford, E. A.; Andersen, S. E.; Moynihan, T. P.;
Robinson, P. A.; Markham, A. F.: An EST and STS-based YAC contig
map of human chromosome 9q22.3 Genomics 38: 199-205, 1996.
7. Pilz, A.; Woodward, K.; Povey, S.; Abbott, C.: Comparative mapping
of 50 human chromosome 9 loci in the laboratory mouse. Genomics 25:
139-149, 1995.
8. Sung, L. A.; Fan, Y.-S.; Lin, C. C.: Gene assignment, expression,
and homology of human tropomodulin. Genomics 34: 92-96, 1996.
9. Sung, L. A.; Fan, Y. S.; Lambert, K.; Fowler, V.; Chien, S.; Lin,
C.: Assignment of human erythrocyte tropomodulin gene to q22 of chromosome
9. (Abstract) Cytogenet. Cell Genet. 58: 1944, 1991.
10. Sung, L. A.; Fowler, V. M.; Lambert, K.; Chien, S.: Molecular
cloning of human erythroid tropomodulin. (Abstract) FASEB J. 5:
A1625, 1991.
11. Sung, L. A.; Fowler, V. M.; Lambert, K.; Sussman, M. A.; Karr,
D.; Chien, S.: Molecular cloning and characterization of human fetal
liver tropomodulin: a tropomyosin-binding protein. J. Biol. Chem. 267:
2616-2621, 1992.
12. White, R. A.; Dowler, L. L.; Woo, M.; Adkison, L. R.; Pal, S.;
Gershon, D.; Fowler, V. M.: The tropomodulin (Tmod) gene maps to
chromosome 4, closely linked to Mup1. Mammalian Genome 6: 332-333,
1995.
*FIELD* CN
Patricia A. Hartz - updated: 8/5/2003
Paul J. Converse - updated: 2/28/2001
Victor A. McKusick - updated: 1/29/1999
*FIELD* CD
Victor A. McKusick: 9/17/1991
*FIELD* ED
carol: 04/14/2009
carol: 7/12/2007
mgross: 8/5/2003
carol: 4/12/2001
mgross: 2/28/2001
carol: 2/2/1999
terry: 1/29/1999
psherman: 8/4/1998
terry: 1/17/1997
terry: 6/21/1996
terry: 6/5/1996
terry: 6/3/1996
mark: 6/15/1995
terry: 2/7/1995
carol: 2/18/1993
supermim: 3/16/1992
carol: 2/20/1992
carol: 9/17/1991
*RECORD*
*FIELD* NO
190930
*FIELD* TI
*190930 TROPOMODULIN; TMOD
;;E-TROPOMODULIN; ETMOD
*FIELD* TX
CLONING
Sung et al. (1991, 1992) cloned the tropomodulin gene from human
read morereticulocyte and fetal liver cDNA libraries.
By Northern blot analysis, Sung et al. (1996) showed that the TMOD gene
is expressed in major human tissues at different levels in the following
order: heart and skeletal muscle much greater than in brain, lung, and
pancreas, which is greater than in placenta, liver, and kidney. They
pointed to structural similarities between tropomodulin and the 64-kD
autoantigen in Graves disease (139080) and suggested that the 2 genes
evolved from a common ancestral gene.
Chu et al. (2000) noted that erythrocyte TMOD is a 359-amino acid
globular protein.
By RNA dot blot analysis, Conley et al. (2001) confirmed expression of
ETMOD in almost every tissue tested, with highest abundance in fetal and
adult heart and skeletal muscle.
GENE FUNCTION
Human erythrocyte tropomodulin is a 43-kD tropomyosin-regulating protein
(Gilligan and Bennett, 1993). It may modulate the association of
tropomyosin with the spectrin-actin complex in the erythrocyte membrane
skeleton, and thus the viscoelastic properties of erythrocytes.
Tropomodulin is associated with the pointed end of the actin filaments
(Fowler et al., 1993). Sung et al. (1996) stated that it binds
specifically to the N terminus of tropomyosin and blocks the elongation
and depolarization of tropomyosin-coated actin filaments.
Conley (2001) found that both Tmod and Smlmod (LMOD1; 602715)
cofractionated with tropomyosin in the Triton-insoluble cytoskeleton
fraction of rabbit stomach smooth muscle, and both were solubilized by
high salt. Immunofluorescent localization found Smlmod present along the
length of actin filaments of rat intestinal smooth muscle, while Tmod
stained in a punctate pattern distinct from that of actin filaments or
the dense body marker, alpha-actinin (see 102575). Hypercontraction of
rat intestinal smooth muscle with 10 mM Ca(2+) caused both Smlmod and
Tmod to associate near alpha-actinin at the periphery of actin-rich
contraction bands.
GENE STRUCTURE
Using PCR methods to obtain TMOD genomic clones, Chu et al. (2000)
determined that the TMOD gene contains 9 exons. Chu et al. (2000)
suggested that the use of alternative promoters may account for
tissue-specific expression and regulation.
MAPPING
Sung et al. (1991) mapped the TMOD gene to 9q22.2-q22.3 by in situ
hybridization. By interspecific backcross linkage analysis, Pilz et al.
(1995) mapped the Tmod gene to mouse chromosome 4, and White et al.
(1995) used recombinant inbred strains to map the gene to a region
within 1.0 cM of Mup1 (major urinary protein-1) on chromosome 4.
Lench et al. (1996) created an EST- and STS-based YAC contig map of
9q22.3 and showed that it contains the following genes in this order
(from centromere to telomere): TMOD, XPA (611153), ALDOB (612724), BAAT
(602938). All 4 of these genes map to a syntenic region of mouse
chromosome 4 and are situated in the same order as their counterparts on
human 9q22.3.
*FIELD* RF
1. Chu, X.; Thompson, D.; Yee, L. J.; Sung, L. A.: Genomic organization
of mouse and human erythrocyte tropomodulin genes encoding the pointed
end capping protein for the actin filaments. Gene 256: 271-281,
2000.
2. Conley, C. A.: Leiomodin and tropomodulin in smooth muscle. Am.
J. Physiol. Cell Physiol. 280: C1645-C1656, 2001.
3. Conley, C. A.; Fritz-Six, K. L.; Almenar-Queralt, A.; Fowler, V.
M.: Leiomodins: larger members of the tropomodulin (Tmod) gene family. Genomics 73:
127-139, 2001.
4. Fowler, V. M.; Sussmann, M. A.; Miller, P. G.; Flucher, B. E.;
Daniels, M. P.: Tropomodulin is associated with the free (pointed)
ends of the thin filaments in rat skeletal muscle. J. Cell Biol. 120:
411-420, 1993.
5. Gilligan, D. M.; Bennett, V.: The junctional complex of the membrane
skeleton. Semin. Hemat. 30: 74-83, 1993.
6. Lench, N. J.; Telford, E. A.; Andersen, S. E.; Moynihan, T. P.;
Robinson, P. A.; Markham, A. F.: An EST and STS-based YAC contig
map of human chromosome 9q22.3 Genomics 38: 199-205, 1996.
7. Pilz, A.; Woodward, K.; Povey, S.; Abbott, C.: Comparative mapping
of 50 human chromosome 9 loci in the laboratory mouse. Genomics 25:
139-149, 1995.
8. Sung, L. A.; Fan, Y.-S.; Lin, C. C.: Gene assignment, expression,
and homology of human tropomodulin. Genomics 34: 92-96, 1996.
9. Sung, L. A.; Fan, Y. S.; Lambert, K.; Fowler, V.; Chien, S.; Lin,
C.: Assignment of human erythrocyte tropomodulin gene to q22 of chromosome
9. (Abstract) Cytogenet. Cell Genet. 58: 1944, 1991.
10. Sung, L. A.; Fowler, V. M.; Lambert, K.; Chien, S.: Molecular
cloning of human erythroid tropomodulin. (Abstract) FASEB J. 5:
A1625, 1991.
11. Sung, L. A.; Fowler, V. M.; Lambert, K.; Sussman, M. A.; Karr,
D.; Chien, S.: Molecular cloning and characterization of human fetal
liver tropomodulin: a tropomyosin-binding protein. J. Biol. Chem. 267:
2616-2621, 1992.
12. White, R. A.; Dowler, L. L.; Woo, M.; Adkison, L. R.; Pal, S.;
Gershon, D.; Fowler, V. M.: The tropomodulin (Tmod) gene maps to
chromosome 4, closely linked to Mup1. Mammalian Genome 6: 332-333,
1995.
*FIELD* CN
Patricia A. Hartz - updated: 8/5/2003
Paul J. Converse - updated: 2/28/2001
Victor A. McKusick - updated: 1/29/1999
*FIELD* CD
Victor A. McKusick: 9/17/1991
*FIELD* ED
carol: 04/14/2009
carol: 7/12/2007
mgross: 8/5/2003
carol: 4/12/2001
mgross: 2/28/2001
carol: 2/2/1999
terry: 1/29/1999
psherman: 8/4/1998
terry: 1/17/1997
terry: 6/21/1996
terry: 6/5/1996
terry: 6/3/1996
mark: 6/15/1995
terry: 2/7/1995
carol: 2/18/1993
supermim: 3/16/1992
carol: 2/20/1992
carol: 9/17/1991