TNMD_HUMAN
ID TNMD_HUMAN Reviewed; 317 AA.
AC Q9H2S6; Q9HBX0; Q9UJG0;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Tenomodulin;
DE Short=TeM;
DE Short=hTeM;
DE AltName: Full=Chondromodulin-1-like protein;
DE Short=ChM1L;
DE Short=hChM1L;
DE AltName: Full=Chondromodulin-I-like protein;
DE AltName: Full=Myodulin;
DE AltName: Full=Tendin;
GN Name=TNMD; Synonyms=CHM1L; ORFNames=UNQ771/PRO1565;
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].
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].
RC 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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=19602561; DOI=10.1210/jc.2009-0292;
RA Saiki A., Olsson M., Jernas M., Gummesson A., McTernan P.G., Andersson J.,
RA Jacobson P., Sjoholm K., Olsson B., Yamamura S., Walley A., Froguel P.,
RA Carlsson B., Sjostrom L., Svensson P.A., Carlsson L.M.;
RT "Tenomodulin is highly expressed in adipose tissue, increased in obesity,
RT and down-regulated during diet-induced weight loss.";
RL J. Clin. Endocrinol. Metab. 94:3987-3994(2009).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=19780194; DOI=10.1002/jor.20999;
RA Jelinsky S.A., Archambault J., Li L., Seeherman H.;
RT "Tendon-selective genes identified from rat and human musculoskeletal
RT tissues.";
RL J. Orthop. Res. 28:289-297(2010).
RN [9]
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=22700804; DOI=10.1152/japplphysiol.00198.2012;
RA Qi J., Dmochowski J.M., Banes A.N., Tsuzaki M., Bynum D., Patterson M.,
RA Creighton A., Gomez S., Tech K., Cederlund A., Banes A.J.;
RT "Differential expression and cellular localization of novel isoforms of the
RT tendon biomarker tenomodulin.";
RL J. Appl. Physiol. 113:861-871(2012).
CC -!- FUNCTION: May be an angiogenesis inhibitor.
CC -!- INTERACTION:
CC Q9H2S6; Q9BSE2: TMEM79; NbExp=4; IntAct=EBI-10306119, EBI-8649725;
CC Q9H2S6-2; Q86WK6: AMIGO1; NbExp=3; IntAct=EBI-12003398, EBI-19125216;
CC Q9H2S6-2; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-12003398, EBI-11343438;
CC Q9H2S6-2; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-12003398, EBI-747430;
CC Q9H2S6-2; Q12983: BNIP3; NbExp=3; IntAct=EBI-12003398, EBI-749464;
CC Q9H2S6-2; O60238: BNIP3L; NbExp=3; IntAct=EBI-12003398, EBI-849893;
CC Q9H2S6-2; P27797: CALR; NbExp=3; IntAct=EBI-12003398, EBI-1049597;
CC Q9H2S6-2; P20138: CD33; NbExp=3; IntAct=EBI-12003398, EBI-3906571;
CC Q9H2S6-2; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-12003398, EBI-6942903;
CC Q9H2S6-2; P36957: DLST; NbExp=3; IntAct=EBI-12003398, EBI-351007;
CC Q9H2S6-2; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12003398, EBI-18304435;
CC Q9H2S6-2; P12314: FCGR1A; NbExp=3; IntAct=EBI-12003398, EBI-2869867;
CC Q9H2S6-2; Q6P531: GGT6; NbExp=3; IntAct=EBI-12003398, EBI-2868927;
CC Q9H2S6-2; Q9UM44: HHLA2; NbExp=3; IntAct=EBI-12003398, EBI-2867874;
CC Q9H2S6-2; Q8N743: KIR3DL3; NbExp=3; IntAct=EBI-12003398, EBI-17272405;
CC Q9H2S6-2; Q9HB07: MYG1; NbExp=3; IntAct=EBI-12003398, EBI-709754;
CC Q9H2S6-2; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-12003398, EBI-1055945;
CC Q9H2S6-2; Q9NPE6: SPAG4; NbExp=3; IntAct=EBI-12003398, EBI-10819434;
CC Q9H2S6-2; Q96A25: TMEM106A; NbExp=3; IntAct=EBI-12003398, EBI-3915978;
CC Q9H2S6-2; Q9BSE2: TMEM79; NbExp=3; IntAct=EBI-12003398, EBI-8649725;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000305}; Single-pass
CC type II membrane protein {ECO:0000305}. Nucleus envelope.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Membrane {ECO:0000305}; Single-pass
CC type II membrane protein {ECO:0000305}. Nucleus envelope.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=64kDa, I;
CC IsoId=Q9H2S6-1; Sequence=Displayed;
CC Name=2; Synonyms=33 kDa, II;
CC IsoId=Q9H2S6-2; Sequence=VSP_054950, VSP_054951;
CC Name=3; Synonyms=45kDa, III;
CC IsoId=Q9H2S6-3; Sequence=VSP_054949;
CC -!- TISSUE SPECIFICITY: Highly expressed in hypovascular connective tissues
CC such as tendons. Has also strong expression in adipose tissue.
CC {ECO:0000269|PubMed:19602561, ECO:0000269|PubMed:19780194,
CC ECO:0000269|PubMed:22700804}.
CC -!- SIMILARITY: Belongs to the chondromodulin-1 family. {ECO:0000305}.
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DR EMBL; AB055421; BAB21756.1; -; mRNA.
DR EMBL; AF234259; AAG49144.1; -; mRNA.
DR EMBL; AF191770; AAG28395.1; -; mRNA.
DR EMBL; AF291656; AAK83109.1; -; mRNA.
DR EMBL; AY358706; AAQ89069.1; -; mRNA.
DR EMBL; AL035608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS14469.1; -. [Q9H2S6-1]
DR PIR; JC7597; JC7597.
DR RefSeq; NP_071427.2; NM_022144.2. [Q9H2S6-1]
DR AlphaFoldDB; Q9H2S6; -.
DR BioGRID; 122062; 18.
DR IntAct; Q9H2S6; 20.
DR STRING; 9606.ENSP00000362122; -.
DR GlyGen; Q9H2S6; 2 sites.
DR iPTMnet; Q9H2S6; -.
DR PhosphoSitePlus; Q9H2S6; -.
DR BioMuta; TNMD; -.
DR DMDM; 18202941; -.
DR MassIVE; Q9H2S6; -.
DR PaxDb; Q9H2S6; -.
DR PeptideAtlas; Q9H2S6; -.
DR PRIDE; Q9H2S6; -.
DR ProteomicsDB; 80587; -. [Q9H2S6-1]
DR Antibodypedia; 28504; 184 antibodies from 21 providers.
DR DNASU; 64102; -.
DR Ensembl; ENST00000373031.5; ENSP00000362122.4; ENSG00000000005.6. [Q9H2S6-1]
DR GeneID; 64102; -.
DR KEGG; hsa:64102; -.
DR MANE-Select; ENST00000373031.5; ENSP00000362122.4; NM_022144.3; NP_071427.2.
DR UCSC; uc004efy.5; human. [Q9H2S6-1]
DR CTD; 64102; -.
DR DisGeNET; 64102; -.
DR GeneCards; TNMD; -.
DR HGNC; HGNC:17757; TNMD.
DR HPA; ENSG00000000005; Tissue enhanced (adipose tissue, breast, seminal vesicle).
DR MIM; 300459; gene.
DR neXtProt; NX_Q9H2S6; -.
DR OpenTargets; ENSG00000000005; -.
DR PharmGKB; PA134878561; -.
DR VEuPathDB; HostDB:ENSG00000000005; -.
DR eggNOG; ENOG502QPTP; Eukaryota.
DR GeneTree; ENSGT00480000042679; -.
DR HOGENOM; CLU_071852_1_0_1; -.
DR InParanoid; Q9H2S6; -.
DR OMA; PGEKPIQ; -.
DR OrthoDB; 1308600at2759; -.
DR PhylomeDB; Q9H2S6; -.
DR TreeFam; TF329712; -.
DR PathwayCommons; Q9H2S6; -.
DR SignaLink; Q9H2S6; -.
DR BioGRID-ORCS; 64102; 9 hits in 690 CRISPR screens.
DR ChiTaRS; TNMD; human.
DR GeneWiki; TNMD; -.
DR GenomeRNAi; 64102; -.
DR Pharos; Q9H2S6; Tbio.
DR PRO; PR:Q9H2S6; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9H2S6; protein.
DR Bgee; ENSG00000000005; Expressed in calcaneal tendon and 102 other tissues.
DR Genevisible; Q9H2S6; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IBA:GO_Central.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IBA:GO_Central.
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 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disulfide bond; Glycoprotein; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..317
FT /note="Tenomodulin"
FT /id="PRO_0000144308"
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 VAR_SEQ 1..63
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_054949"
FT VAR_SEQ 193..207
FT /note="VSELQDFEEEGEDLH -> GMTFLSSSSSYFLRQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054950"
FT VAR_SEQ 208..317
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_054951"
FT CONFLICT 40
FT /note="A -> T (in Ref. 3; AAG28395)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="N -> S (in Ref. 3; AAG28395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 37130 MW; D17507D7E2EA0C68 CRC64;
MAKNPPENCE DCHILNAEAF KSKKICKSLK ICGLVFGILA LTLIVLFWGS KHFWPEVPKK
AYDMEHTFYS NGEKKKIYME IDPVTRTEIF RSGNGTDETL EVHDFKNGYT GIYFVGLQKC
FIKTQIKVIP EFSEPEEEID ENEEITTTFF EQSVIWVPAE KPIENRDFLK NSKILEICDN
VTMYWINPTL ISVSELQDFE EEGEDLHFPA NEKKGIEQNE QWVVPQVKVE KTRHARQASE
EELPINDYTE NGIEFDPMLD ERGYCCIYCR RGNRYCRRVC EPLLGYYPYP YCYQGGRVIC
RVIMPCNWWV ARMLGRV
