ID   CNMD_RABIT              Reviewed;         333 AA.
AC   O77770;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Leukocyte cell-derived chemotaxin 1 {ECO:0000305};
DE   AltName: Full=Chondromodulin {ECO:0000250|UniProtKB:O75829};
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   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9731231; DOI=10.1006/bbrc.1998.9233;
RA   Shukunami C., Hiraki Y.;
RT   "Expression of cartilage-specific functional matrix chondromodulin-I mRNA
RT   in rabbit growth plate chondrocytes and its responsiveness to growth
RT   stimuli in vitro.";
RL   Biochem. Biophys. Res. Commun. 249:885-890(1998).
RN   [2]
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 {ECO:0000250}. Note=Accumulated in the
CC       inter-territorial matrix of cartilage. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Chondrosurfactant protein]: Endomembrane system
CC       {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
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; AF072129; AAC36470.1; -; mRNA.
DR   RefSeq; NP_001075509.1; NM_001082040.1.
DR   AlphaFoldDB; O77770; -.
DR   SMR; O77770; -.
DR   STRING; 9986.ENSOCUP00000005069; -.
DR   GeneID; 100008692; -.
DR   KEGG; ocu:100008692; -.
DR   CTD; 11061; -.
DR   eggNOG; ENOG502QVPC; Eukaryota.
DR   InParanoid; O77770; -.
DR   OrthoDB; 1308600at2759; -.
DR   Proteomes; UP000001811; 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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
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   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_0000005355"
FT   PROPEP          211..214
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000005356"
FT   CHAIN           215..333
FT                   /note="Chondromodulin-1"
FT                   /id="PRO_0000005357"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          104..201
FT                   /note="BRICHOS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00255"
FT   REGION          212..269
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        131..193
FT                   /evidence="ECO:0000250"
FT   DISULFID        281..285
FT                   /evidence="ECO:0000250"
FT   DISULFID        282..322
FT                   /evidence="ECO:0000250"
FT   DISULFID        292..316
FT                   /evidence="ECO:0000250"
FT   DISULFID        296..312
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   333 AA;  36974 MW;  70B5FFA9613DEA1D CRC64;
     MTENSDKVPI ALVGPDDVEF CGPPAYATVT VKPSGPARLL KVGAVVLISG AVLLLFGAIG
     AFYLWKGSDN HIYNVHYTMS INGKLQDGSM EIDARNNLET FKMGSGAEEA IEVNDFQNGI
     TGIRFAGGEK CYIKAQVKAR VPEVGTVTQQ SISSELEGKI MPVKHEEEAL VWVAVGQPVQ
     DNSFLSARVL ELCGDLPIFW LKPTYPKEIQ RERREVVRKT VPTTTKRPHS GPRGNPGPAR
     MRNDSRPSVQ EDSEPFNPDN PYHQEGESMT FDPRLDHEGI CCIECRRSYT HCQKICEPLG
     GYNPWPYNYQ GCRSACRVVM PCSWWVARIL GMV