CNMD_BOVIN
ID CNMD_BOVIN Reviewed; 335 AA.
AC P17404; P23590;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Leukocyte cell-derived chemotaxin 1 {ECO:0000305};
DE AltName: Full=Chondromodulin {ECO:0000250|UniProtKB:O75829};
DE AltName: Full=Small cartilage-derived glycoprotein;
DE Short=SCGP;
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:0000250|UniProtKB:O75829};
GN Synonyms=CHMI {ECO:0000250|UniProtKB:O75829},
GN LECT1 {ECO:0000250|UniProtKB:O75829};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 215-241 AND 297-317,
RP SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
RC TISSUE=Fetal epiphyseal cartilage;
RX PubMed=1709014; DOI=10.1016/0006-291x(91)91660-5;
RA Hiraki Y., Tanaka H., Inoue H., Kondo J., Kamizono A., Suzuki F.;
RT "Molecular cloning of a new class of cartilage-specific matrix,
RT chondromodulin-I, which stimulates growth of cultured chondrocytes.";
RL Biochem. Biophys. Res. Commun. 175:971-977(1991).
RN [2]
RP PROTEIN SEQUENCE OF 215-335, VARIANTS MET-221 AND 223-ASN-GLU-224,
RP GLYCOSYLATION AT ASN-223 (VARIANT 223-ASN-GLU-224), AND GLYCOSYLATION AT
RP THR-236 AND ASN-244.
RC TISSUE=Nasal cartilage;
RX PubMed=2351661; DOI=10.1016/s0021-9258(19)38715-0;
RA Neame P.J., Treep J.T., Young C.N.;
RT "An 18-kDa glycoprotein from bovine nasal cartilage. Isolation and primary
RT structure of small, cartilage-derived glycoprotein.";
RL J. Biol. Chem. 265:9628-9633(1990).
RN [3]
RP ERRATUM OF PUBMED:2351661.
RA Neame P.J., Treep J.T., Young C.N.;
RL J. Biol. Chem. 265:22056-22056(1990).
RN [4]
RP PROTEOLYTIC PROCESSING.
RX PubMed=11323410; DOI=10.1074/jbc.m009967200;
RA Azizan A., Holaday N., Neame P.J.;
RT "Post-translational processing of bovine chondromodulin-I.";
RL J. Biol. Chem. 276:23632-23638(2001).
RN [5]
RP REVIEW.
RX PubMed=10912526; DOI=10.1007/s004670000339;
RA Hiraki Y., Shukunami C.;
RT "Chondromodulin-I as a novel cartilage-specific growth-modulating factor.";
RL Pediatr. Nephrol. 14:602-605(2000).
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. Note=Accumulated in the inter-territorial
CC matrix of cartilage.
CC -!- SUBCELLULAR LOCATION: [Chondrosurfactant protein]: Endomembrane system
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Nasal and articular cartilage, and fetal epiphysis.
CC -!- PTM: After cleavage, the post-translationally modified ChM-I is
CC secreted as a glycoprotein. {ECO:0000269|PubMed:11323410}.
CC -!- PTM: Two other smaller nonglycosylated chondromodulin forms (9 kDa and
CC 7 kDa) are found either in developing articular cartilage or in
CC chondrocytes. The 9 kDa form could be processed by an extracellular
CC matrix-associated protease as a metalloproteinase and the 7 kDa form
CC could be processed intracellularly. {ECO:0000269|PubMed:11323410}.
CC -!- SIMILARITY: Belongs to the chondromodulin-1 family. {ECO:0000305}.
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DR EMBL; M65081; AAA30445.1; -; mRNA.
DR PIR; JT0569; JT0569.
DR RefSeq; NP_776694.1; NM_174269.2.
DR AlphaFoldDB; P17404; -.
DR STRING; 9913.ENSBTAP00000035726; -.
DR iPTMnet; P17404; -.
DR PaxDb; P17404; -.
DR Ensembl; ENSBTAT00000035859; ENSBTAP00000035726; ENSBTAG00000025502.
DR GeneID; 281683; -.
DR KEGG; bta:281683; -.
DR CTD; 11061; -.
DR VEuPathDB; HostDB:ENSBTAG00000025502; -.
DR VGNC; VGNC:27507; CNMD.
DR eggNOG; ENOG502QVPC; Eukaryota.
DR GeneTree; ENSGT00480000042679; -.
DR HOGENOM; CLU_071852_0_0_1; -.
DR InParanoid; P17404; -.
DR OMA; GNLPIFW; -.
DR OrthoDB; 1308600at2759; -.
DR TreeFam; TF329712; -.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000025502; Expressed in laryngeal cartilage and 85 other tissues.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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 Chondrogenesis; Cleavage on pair of basic residues; Developmental protein;
KW Differentiation; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Membrane; Reference proteome; Secreted;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..210
FT /note="Chondrosurfactant protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000005343"
FT PROPEP 211..214
FT /evidence="ECO:0000255"
FT /id="PRO_0000005344"
FT CHAIN 215..335
FT /note="Chondromodulin-1"
FT /id="PRO_0000005345"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 104..201
FT /note="BRICHOS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00255"
FT REGION 221..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine; in variant 223-N-E-
FT 224"
FT /evidence="ECO:0000269|PubMed:2351661"
FT CARBOHYD 236
FT /note="O-linked (GalNAc...) threonine; partial"
FT /evidence="ECO:0000269|PubMed:2351661"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2351661"
FT DISULFID 131..193
FT /evidence="ECO:0000250"
FT DISULFID 283..287
FT /evidence="ECO:0000269|PubMed:1709014"
FT DISULFID 284..324
FT /evidence="ECO:0000269|PubMed:1709014"
FT DISULFID 294..318
FT /evidence="ECO:0000269|PubMed:1709014"
FT DISULFID 298..314
FT /evidence="ECO:0000269|PubMed:1709014"
FT VARIANT 221
FT /note="V -> M"
FT /evidence="ECO:0000269|PubMed:2351661"
FT VARIANT 223..224
FT /note="TT -> NE"
FT CONFLICT 256
FT /note="P -> PD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 37164 MW; 6D72CA8740448441 CRC64;
MTENSDKVPI ALVGPDDVEF CSPPAYAAVT VKPSSPARLL KVGAVVLISG AVLLLLGAIG
AFYFWKGSDN HIYNVHYTMS INGKLQDGSM EIDAGNNLET FKMGSGAEEA VEVNDFQNGI
TGIRFAGGEK CYIKAQVKAR IPEVGTMTKQ SISSELEGKI MPVKYEENSL IWVAGDQPVK
DNSFLSSKVL ELCGDLPIFW LKPTYPKEIQ RERRELVRKI VTTTTTRRLR SGPQGTPAPG
RPNNGTRPSV QEDAEPFNPD NPYHQQEGES MTFDPRLDHE GICCIECRRS YTHCQKICEP
LGGYHPWPYN YQGCRSACRV IMPCSWWVAR ILGMV
