TNMD_MOUSE
ID TNMD_MOUSE Reviewed; 317 AA.
AC Q9EP64; Q8CET4;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Tenomodulin;
DE Short=TeM;
DE Short=mTeM;
DE AltName: Full=Chondromodulin-1-like protein;
DE Short=ChM1L;
DE Short=mChM1L;
DE AltName: Full=Chondromodulin-I-like protein;
DE AltName: Full=Myodulin;
DE AltName: Full=Tendin;
GN Name=Tnmd; Synonyms=Chm1l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11162640; DOI=10.1006/bbrc.2000.4245;
RA Yamana K., Wada H., Takahashi Y., Sato H., Kasahara Y., Kiyoki M.;
RT "Molecular cloning and characterization of ChM1L, a novel membrane molecule
RT similar to chondromodulin-I.";
RL Biochem. Biophys. Res. Commun. 280:1101-1106(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11162673; DOI=10.1006/bbrc.2001.4271;
RA Shukunami C., Oshima Y., Hiraki Y.;
RT "Molecular cloning of tenomodulin, a novel chondromodulin-I related gene.";
RL Biochem. Biophys. Res. Commun. 280:1323-1327(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=11357195; DOI=10.1002/dvdy.1126;
RA Brandau O., Meindl A., Faessler R., Aszodi A.;
RT "A novel gene, tendin, is strongly expressed in tendons and ligaments and
RT shows high homology with chondromodulin-I.";
RL Dev. Dyn. 221:72-80(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/10ScSn; TISSUE=Skeletal muscle;
RA Cros N., Tkatchenko A.V., Leclerc L., Leger J.J., Marini J.-F.,
RA Dechesne C.A.;
RT "Gene expression alterations revealed by suppression subtractive
RT hybridization in rat soleus muscle disuse atrophy.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
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).
CC -!- FUNCTION: May be an angiogenesis inhibitor.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression in tendons
CC and ligaments, in the diaphragm, eye and skeletal muscle. Expressed in
CC neuronal cells of all brain regions. Very low expression, if any, in
CC glial cells. {ECO:0000269|PubMed:11357195}.
CC -!- DEVELOPMENTAL STAGE: Expression already detected at 9.5 dpc and
CC maintained throughout embryonic development. At 17.5 dpc, high levels
CC found in tendons and ligaments of the skeletomuscular system, including
CC the knee joint, the upper limb and the intercostal ligaments. At this
CC developmental stage, high expression is also detected in the tendinous
CC part of the diaphragm. By contrast, low levels are observed in resting
CC and proliferative chondrocytes of long bones and vertebral bodies, and
CC in the cartilaginous part of the intervertebral disks. No expression in
CC hypertrophic chondrocytes. Outside the skeletomuscular system,
CC expressed in neuronal cells of all brain regions and the spinal cord,
CC liver, lung, bowels, thymus and eye. {ECO:0000269|PubMed:11357195}.
CC -!- SIMILARITY: Belongs to the chondromodulin-1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC25447.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB055422; BAB21757.1; -; mRNA.
DR EMBL; AF219993; AAG48938.1; -; mRNA.
DR EMBL; AF291655; AAK83108.1; -; mRNA.
DR EMBL; AF191768; AAG28393.1; -; mRNA.
DR EMBL; AK014761; BAC25447.1; ALT_SEQ; mRNA.
DR EMBL; BC006919; AAH06919.1; -; mRNA.
DR EMBL; BC049944; AAH49944.1; -; mRNA.
DR CCDS; CCDS30386.1; -.
DR PIR; JC7603; JC7603.
DR RefSeq; NP_071717.1; NM_022322.2.
DR AlphaFoldDB; Q9EP64; -.
DR STRING; 10090.ENSMUSP00000033602; -.
DR GlyGen; Q9EP64; 2 sites.
DR PhosphoSitePlus; Q9EP64; -.
DR PaxDb; Q9EP64; -.
DR PeptideAtlas; Q9EP64; -.
DR PRIDE; Q9EP64; -.
DR ProteomicsDB; 259279; -.
DR Antibodypedia; 28504; 184 antibodies from 21 providers.
DR DNASU; 64103; -.
DR Ensembl; ENSMUST00000033602; ENSMUSP00000033602; ENSMUSG00000031250.
DR GeneID; 64103; -.
DR KEGG; mmu:64103; -.
DR UCSC; uc009uez.2; mouse.
DR CTD; 64102; -.
DR MGI; MGI:1929885; Tnmd.
DR VEuPathDB; HostDB:ENSMUSG00000031250; -.
DR eggNOG; ENOG502QPTP; Eukaryota.
DR GeneTree; ENSGT00480000042679; -.
DR HOGENOM; CLU_071852_1_0_1; -.
DR InParanoid; Q9EP64; -.
DR OMA; PGEKPIQ; -.
DR OrthoDB; 1308600at2759; -.
DR PhylomeDB; Q9EP64; -.
DR TreeFam; TF329712; -.
DR BioGRID-ORCS; 64103; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q9EP64; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9EP64; protein.
DR Bgee; ENSMUSG00000031250; Expressed in vault of skull and 133 other tissues.
DR Genevisible; Q9EP64; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0001886; P:endothelial cell morphogenesis; IDA:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:MGI.
DR InterPro; IPR007084; BRICHOS_dom.
DR InterPro; IPR043405; Chondromodulin/Tenomodulin.
DR PANTHER; PTHR14064; PTHR14064; 1.
DR Pfam; PF04089; BRICHOS; 1.
DR SMART; SM01039; BRICHOS; 1.
DR PROSITE; PS50869; BRICHOS; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..317
FT /note="Tenomodulin"
FT /id="PRO_0000144309"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..50
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..317
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 93..186
FT /note="BRICHOS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00255"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESC2"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 120..178
FT /evidence="ECO:0000250"
FT CONFLICT 4
FT /note="N -> I (in Ref. 5; BAC25447)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="K -> I (in Ref. 5; BAC25447)"
FT /evidence="ECO:0000305"
FT CONFLICT 24
FT /note="K -> M (in Ref. 5; BAC25447)"
FT /evidence="ECO:0000305"
FT CONFLICT 27..28
FT /note="KS -> L (in Ref. 5; BAC25447)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="E -> D (in Ref. 5; BAC25447)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="K -> I (in Ref. 5; BAC25447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 37047 MW; D7A00952F2E2ED9D CRC64;
MAKNPPENCE GCHILNAEAL KSKKICKSLK ICGLVFGILA LTLIVLFWGS KHFWPEVSKK
TYDMEHTFYS NGEKKKIYME IDPITRTEIF RSGNGTDETL EVHDFKNGYT GIYFVGLQKC
FIKTQIKVIP EFSEPEEEID ENEEITTTFF EQSVIWVPAE KPIENRDFLK NSKILEICDN
VTMYWINPTL IAVSELQDFE EDGEDLHFPT SEKKGIDQNE QWVVPQVKVE KTRHTRQASE
EDLPINDYTE NGIEFDPMLD ERGYCCIYCR RGNRYCRRVC EPLLGYYPYP YCYQGGRVIC
RVIMPCNWWV ARMLGRV
