CNMD_RAT
ID CNMD_RAT Reviewed; 334 AA.
AC O70367;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Leukocyte cell-derived chemotaxin 1 {ECO:0000305};
DE AltName: Full=Chondromodulin {ECO:0000312|RGD:620176};
DE Contains:
DE RecName: Full=Chondrosurfactant protein;
DE Short=CH-SP;
DE Contains:
DE RecName: Full=Chondromodulin-1;
DE AltName: Full=Chondromodulin-I;
DE Short=ChM-I;
DE Flags: Precursor;
GN Name=Cnmd {ECO:0000312|RGD:620176};
GN Synonyms=Chmi {ECO:0000312|RGD:620176}, Lect1 {ECO:0000312|RGD:620176};
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=Wistar Kyoto; TISSUE=Cartilage;
RX PubMed=11328727;
RA Funaki H., Sawaguchi S., Yaoeda K., Koyama Y., Yaoita E., Funaki S.,
RA Shirakashi M., Oshima Y., Shukunami C., Hiraki Y., Abe H., Yamamoto T.;
RT "Expression and localization of angiogenic inhibitory factor,
RT chondromodulin-I, in adult rat eye.";
RL Invest. Ophthalmol. Vis. Sci. 42:1193-1200(2001).
RN [2]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16980969; DOI=10.1038/nm1476;
RA Yoshioka M., Yuasa S., Matsumura K., Kimura K., Shiomi T., Kimura N.,
RA Shukunami C., Okada Y., Mukai M., Shin H., Yozu R., Sata M., Ogawa S.,
RA Hiraki Y., Fukuda K.;
RT "Chondromodulin-I maintains cardiac valvular function by preventing
RT angiogenesis.";
RL Nat. Med. 12:1151-1159(2006).
CC -!- FUNCTION: Bifunctional growth regulator that stimulates the growth of
CC cultured chondrocytes in the presence of basic fibroblast growth factor
CC (FGF) but inhibits the growth of cultured vascular endothelial cells.
CC May contribute to the rapid growth of cartilage and vascular invasion
CC prior to the replacement of cartilage by bone during endochondral bone
CC development. Inhibits in vitro tube formation and mobilization of
CC endothelial cells. Plays a role as antiangiogenic factor in cardiac
CC valves to suppress neovascularization (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Chondromodulin-1]: Secreted, extracellular
CC space, extracellular matrix {ECO:0000250}. Note=Accumulated in the
CC inter-territorial matrix of cartilage. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Chondrosurfactant protein]: Endomembrane system
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in cartilage, cardiac valves and valvular
CC interstitial cells (at protein level). Expressed in eye.
CC {ECO:0000269|PubMed:16980969}.
CC -!- DEVELOPMENTAL STAGE: Expression first detected in heart at E9.5 and
CC persisted in the adult. {ECO:0000269|PubMed:16980969}.
CC -!- PTM: After cleavage, the post-translationally modified ChM-I is
CC secreted as a glycoprotein. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chondromodulin-1 family. {ECO:0000305}.
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DR EMBL; AF051425; AAC05574.1; -; mRNA.
DR RefSeq; NP_110481.1; NM_030854.1.
DR AlphaFoldDB; O70367; -.
DR STRING; 10116.ENSRNOP00000017400; -.
DR GlyGen; O70367; 1 site.
DR PaxDb; O70367; -.
DR PRIDE; O70367; -.
DR GeneID; 81512; -.
DR KEGG; rno:81512; -.
DR UCSC; RGD:620176; rat.
DR CTD; 11061; -.
DR RGD; 620176; Cnmd.
DR eggNOG; ENOG502QVPC; Eukaryota.
DR InParanoid; O70367; -.
DR OrthoDB; 1308600at2759; -.
DR PhylomeDB; O70367; -.
DR PRO; PR:O70367; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
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:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; ISO:RGD.
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 Chondrogenesis; Cleavage on pair of basic residues; Developmental protein;
KW Differentiation; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Membrane; Reference proteome; Secreted; Transmembrane; Transmembrane helix.
FT CHAIN 1..210
FT /note="Chondrosurfactant protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005352"
FT PROPEP 211..214
FT /evidence="ECO:0000250"
FT /id="PRO_0000005353"
FT CHAIN 215..334
FT /note="Chondromodulin-1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005354"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 105..201
FT /note="BRICHOS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00255"
FT REGION 212..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 132..193
FT /evidence="ECO:0000250"
FT DISULFID 282..286
FT /evidence="ECO:0000250"
FT DISULFID 283..323
FT /evidence="ECO:0000250"
FT DISULFID 293..317
FT /evidence="ECO:0000250"
FT DISULFID 297..313
FT /evidence="ECO:0000250"
SQ SEQUENCE 334 AA; 37387 MW; DB865E515952A4CD CRC64;
MTENSDKVPI TMVGPEDVEF CSPPAYATVT VKPSGSPTRL LKVGAVVLIS GAVLLLFGAI
GAFYFWKGND NHIYNVHYTM SINGRLQDAS MEIDAANNLE TFKMGSGAEE AIEVNDFQNG
ITGIRFAGGE KCYIKAQVKA RIPEVSTGTK QSISELEGKI MPVKYEENSL IWVAVDQPVK
DNSFLSSKIL EFCGDLPIFW LKPMYPKEIP RERREVVRSS APSTTRRPHS EPRGNAGPGR
LSNRTRPSVQ DDEEPFNPDN PYHQQEGESM TFDPRLDHEG ICCIECRRSY THCQKICEPL
GGYYPWPYNY QGCRSACRVV MPCSWWVARI LGMV
