ID   CNMD_HUMAN              Reviewed;         334 AA.
AC   O75829; Q5TAM4; Q8TAY6; Q9UM18;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   24-JAN-2024, entry version 176.
DE   RecName: Full=Leukocyte cell-derived chemotaxin 1 {ECO:0000305};
DE   AltName: Full=Chondromodulin {ECO:0000312|HGNC:HGNC:17005};
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|HGNC:HGNC:17005};
GN   Synonyms=CHMI {ECO:0000312|HGNC:HGNC:17005}, LECT1
GN   {ECO:0000312|HGNC:HGNC:17005}, MYETS1 {ECO:0000312|HGNC:HGNC:17005};
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] (ISOFORM 1).
RC   TISSUE=Chondrosarcoma;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC   TISSUE=Chondrosarcoma;
RX   PubMed=10103018; DOI=10.1046/j.1432-1327.1999.00227.x;
RA   Hiraki Y., Mitsui K., Endo N., Takahashi K., Hayami T., Inoue H.,
RA   Shukunami C., Tokunaga K., Kono T., Yamada M., Takahashi H.E., Kondo J.;
RT   "Molecular cloning of human chondromodulin-I, a cartilage-derived growth
RT   modulating factor, and its expression in Chinese hamster ovary cells.";
RL   Eur. J. Biochem. 260:869-878(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
RA   Ozono K.;
RT   "Human chondromodulin-1 gene promoter.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 215-334 (ISOFORM 1).
RX   PubMed=10570955; DOI=10.1016/s0014-5793(99)01201-6;
RA   Hayami T., Shukunami C., Mitsui K., Endo N., Tokunaga K., Kondo J.,
RA   Takahashi H.E., Hiraki Y.;
RT   "Specific loss of chondromodulin-I gene expression in chondrosarcoma and
RT   the suppression of tumor angiogenesis and growth by its recombinant protein
RT   in vivo.";
RL   FEBS Lett. 458:436-440(1999).
RN   [8]
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).
RN   [9]
RP   FUNCTION, AND TISSUE SPECIFICITY.
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. {ECO:0000269|PubMed:16980969}.
CC   -!- INTERACTION:
CC       O75829-2; Q95HB9: HLA-DPA1; NbExp=3; IntAct=EBI-10696063, EBI-17686856;
CC       O75829-2; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-10696063, EBI-10243654;
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O75829-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O75829-2; Sequence=VSP_038380;
CC   -!- TISSUE SPECIFICITY: Detected in cartilage and cardiac valves (at
CC       protein level). Detected in the laminae fibrosa, spongiosa and
CC       ventricularis layers of normal cardiac valves (at protein level).
CC       Expression is decreased cardiac valves of patients with valvular heart
CC       disease (at protein level). Weakly expressed in chondrosarcoma.
CC       {ECO:0000269|PubMed:16980969}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at 9 weeks in developing cartilagenous
CC       bone rudiments.
CC   -!- PTM: After cleavage, the post-translationally modified ChM-I is
CC       secreted as a glycoprotein.
CC   -!- SIMILARITY: Belongs to the chondromodulin-1 family. {ECO:0000305}.
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DR   EMBL; AB006000; BAA33443.1; -; mRNA.
DR   EMBL; AF050147; AAC98971.1; -; Genomic_DNA.
DR   EMBL; CR541910; CAG46708.1; -; mRNA.
DR   EMBL; AL139085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL139089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC025659; AAH25659.1; -; mRNA.
DR   EMBL; AB021290; BAA77384.1; -; Genomic_DNA.
DR   EMBL; AB005999; BAA86262.1; -; mRNA.
DR   CCDS; CCDS45051.1; -. [O75829-2]
DR   CCDS; CCDS9437.1; -. [O75829-1]
DR   RefSeq; NP_001011705.1; NM_001011705.1. [O75829-2]
DR   RefSeq; NP_008946.1; NM_007015.2. [O75829-1]
DR   AlphaFoldDB; O75829; -.
DR   BioGRID; 116245; 7.
DR   IntAct; O75829; 7.
DR   STRING; 9606.ENSP00000367198; -.
DR   GlyCosmos; O75829; 1 site, No reported glycans.
DR   GlyGen; O75829; 1 site.
DR   iPTMnet; O75829; -.
DR   PhosphoSitePlus; O75829; -.
DR   BioMuta; CNMD; -.
DR   EPD; O75829; -.
DR   jPOST; O75829; -.
DR   MassIVE; O75829; -.
DR   PaxDb; 9606-ENSP00000367198; -.
DR   PeptideAtlas; O75829; -.
DR   ProteomicsDB; 50217; -. [O75829-1]
DR   ProteomicsDB; 50218; -. [O75829-2]
DR   Antibodypedia; 24240; 230 antibodies from 28 providers.
DR   DNASU; 11061; -.
DR   Ensembl; ENST00000377962.8; ENSP00000367198.3; ENSG00000136110.13. [O75829-1]
DR   Ensembl; ENST00000448904.6; ENSP00000388576.2; ENSG00000136110.13. [O75829-2]
DR   GeneID; 11061; -.
DR   KEGG; hsa:11061; -.
DR   MANE-Select; ENST00000377962.8; ENSP00000367198.3; NM_007015.3; NP_008946.1.
DR   UCSC; uc001vhf.4; human. [O75829-1]
DR   AGR; HGNC:17005; -.
DR   CTD; 11061; -.
DR   DisGeNET; 11061; -.
DR   GeneCards; CNMD; -.
DR   HGNC; HGNC:17005; CNMD.
DR   HPA; ENSG00000136110; Group enriched (brain, choroid plexus, retina, salivary gland, thyroid gland).
DR   MIM; 605147; gene.
DR   neXtProt; NX_O75829; -.
DR   OpenTargets; ENSG00000136110; -.
DR   PharmGKB; PA134897668; -.
DR   VEuPathDB; HostDB:ENSG00000136110; -.
DR   eggNOG; ENOG502QVPC; Eukaryota.
DR   GeneTree; ENSGT00480000042679; -.
DR   HOGENOM; CLU_071852_0_0_1; -.
DR   InParanoid; O75829; -.
DR   OMA; LGYYPWP; -.
DR   OrthoDB; 5342368at2759; -.
DR   PhylomeDB; O75829; -.
DR   TreeFam; TF329712; -.
DR   PathwayCommons; O75829; -.
DR   SignaLink; O75829; -.
DR   BioGRID-ORCS; 11061; 9 hits in 1135 CRISPR screens.
DR   ChiTaRS; CNMD; human.
DR   GeneWiki; LECT1; -.
DR   GenomeRNAi; 11061; -.
DR   Pharos; O75829; Tbio.
DR   PRO; PR:O75829; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; O75829; Protein.
DR   Bgee; ENSG00000136110; Expressed in tibia and 63 other cell types or tissues.
DR   ExpressionAtlas; O75829; baseline and differential.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C: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; IDA:UniProtKB.
DR   GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IBA:GO_Central.
DR   GO; GO:0006029; P:proteoglycan metabolic process; TAS:ProtInc.
DR   GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR   Gene3D; 3.30.390.150; -; 1.
DR   InterPro; IPR007084; BRICHOS_dom.
DR   InterPro; IPR043405; Chondromodulin/Tenomodulin.
DR   PANTHER; PTHR14064; CHONDROMODULIN-RELATED; 1.
DR   PANTHER; PTHR14064:SF6; LEUKOCYTE CELL-DERIVED CHEMOTAXIN 1; 1.
DR   Pfam; PF04089; BRICHOS; 1.
DR   SMART; SM01039; BRICHOS; 1.
DR   PROSITE; PS50869; BRICHOS; 1.
DR   Genevisible; O75829; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chondrogenesis; Cleavage on pair of basic residues;
KW   Developmental protein; Differentiation; 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:0000250"
FT                   /id="PRO_0000005346"
FT   PROPEP          211..214
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000005347"
FT   CHAIN           215..334
FT                   /note="Chondromodulin-1"
FT                   /id="PRO_0000005348"
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          218..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..267
FT                   /note="Polar residues"
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        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"
FT   VAR_SEQ         264
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_038380"
FT   VARIANT         116
FT                   /note="F -> L (in dbSNP:rs3742298)"
FT                   /id="VAR_048719"
FT   VARIANT         175
FT                   /note="V -> I (in dbSNP:rs7330220)"
FT                   /id="VAR_024413"
SQ   SEQUENCE   334 AA;  37102 MW;  9E2393111F9D4FE5 CRC64;
     MTENSDKVPI ALVGPDDVEF CSPPAYATLT VKPSSPARLL KVGAVVLISG AVLLLFGAIG
     AFYFWKGSDS HIYNVHYTMS INGKLQDGSM EIDAGNNLET FKMGSGAEEA IAVNDFQNGI
     TGIRFAGGEK CYIKAQVKAR IPEVGAVTKQ SISSKLEGKI MPVKYEENSL IWVAVDQPVK
     DNSFLSSKVL ELCGDLPIFW LKPTYPKEIQ RERREVVRKI VPTTTKRPHS GPRSNPGAGR
     LNNETRPSVQ EDSQAFNPDN PYHQQEGESM TFDPRLDHEG ICCIECRRSY THCQKICEPL
     GGYYPWPYNY QGCRSACRVI MPCSWWVARI LGMV
//