TNMD_RAT
ID TNMD_RAT Reviewed; 317 AA.
AC Q9ESC2;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Tenomodulin;
DE Short=TeM;
DE Short=rTeM;
DE AltName: Full=Chondromodulin-1-like protein;
DE Short=ChM1L;
DE Short=rChM1L;
DE AltName: Full=Myodulin;
GN Name=Tnmd; Synonyms=Chm1l;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
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].
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 [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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: Highly expressed in tendons.
CC {ECO:0000269|PubMed:19780194}.
CC -!- SIMILARITY: Belongs to the chondromodulin-1 family. {ECO:0000305}.
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DR EMBL; AF191769; AAG28394.1; -; mRNA.
DR EMBL; AB055423; BAB21758.1; -; mRNA.
DR RefSeq; NP_071626.1; NM_022290.1.
DR AlphaFoldDB; Q9ESC2; -.
DR STRING; 10116.ENSRNOP00000005214; -.
DR GlyGen; Q9ESC2; 2 sites.
DR iPTMnet; Q9ESC2; -.
DR PhosphoSitePlus; Q9ESC2; -.
DR PaxDb; Q9ESC2; -.
DR Ensembl; ENSRNOT00000083229; ENSRNOP00000073972; ENSRNOG00000060970.
DR GeneID; 64104; -.
DR KEGG; rno:64104; -.
DR UCSC; RGD:620938; rat.
DR CTD; 64102; -.
DR RGD; 620938; Tnmd.
DR eggNOG; ENOG502QPTP; Eukaryota.
DR GeneTree; ENSGT00480000042679; -.
DR HOGENOM; CLU_071852_1_0_1; -.
DR InParanoid; Q9ESC2; -.
DR OMA; PGEKPIQ; -.
DR OrthoDB; 1308600at2759; -.
DR PhylomeDB; Q9ESC2; -.
DR TreeFam; TF329712; -.
DR PRO; PR:Q9ESC2; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000060970; Expressed in quadriceps femoris and 11 other tissues.
DR Genevisible; Q9ESC2; RN.
DR GO; GO:0009986; C:cell surface; NAS:RGD.
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:0071773; P:cellular response to BMP stimulus; IEP:UniProtKB.
DR GO; GO:0001886; P:endothelial cell morphogenesis; ISO:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:0035990; P:tendon cell differentiation; IEP:UniProtKB.
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 Disulfide bond; Glycoprotein; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..317
FT /note="Tenomodulin"
FT /id="PRO_0000144310"
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:0007744|PubMed:22673903"
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"
SQ SEQUENCE 317 AA; 36971 MW; 8C0328825F915D88 CRC64;
MAKNPPENCE GCHILNAEAL KSKKIRKSLK ICGLVFGILA LTLIVLFWGS KHFWPEVSKK
TYGMEHTFYS NGEKKKISME IDPITRTEIF RSGNGTDETL EVHDFKNGYT GIYFVGLQKC
FIKTQIKVIP EFSEPEEEID ENEEITTTFF EQSVIWVPAE KPIENRDFLK NSKILEICDN
VTMYWINPTL IAVSELQDFE EDGEDLHFPT SEKKGIDQNE QWVVPQVKVE KTRRTRQASE
EDLPVNDYTE NGIEFDPMLD ERGYCCIYCR RGNRYCRRVC EPLLGYYPYP YCYQGGRVIC
RVIMPCNWWV ARMLGRV
