ID   CNMD_DANRE              Reviewed;         286 AA.
AC   P58239;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 1.
DT   03-AUG-2022, entry version 95.
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}; Synonyms=chm1, chmi, lect1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11429291; DOI=10.1016/s0925-4773(01)00417-8;
RA   Sachdev S.W., Dietz U.H., Oshima Y., Lang M.R., Knapik E.W., Hiraki Y.,
RA   Shukunami C.;
RT   "Sequence analysis of zebrafish chondromodulin-1 and expression profile in
RT   the notochord and chondrogenic regions during cartilage morphogenesis.";
RL   Mech. Dev. 105:157-162(2001).
CC   -!- FUNCTION: Bifunctional growth regulator. May contribute to the rapid
CC       growth of cartilage and vascular invasion prior to the replacement of
CC       cartilage by bone during endochondral bone development. Plays a role as
CC       antiangiogenic factor in cardiac valves to suppress neovascularization
CC       (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; AF322374; AAK77023.1; -; mRNA.
DR   AlphaFoldDB; P58239; -.
DR   STRING; 7955.ENSDARP00000022495; -.
DR   PaxDb; P58239; -.
DR   ZFIN; ZDB-GENE-010713-1; cnmd.
DR   eggNOG; ENOG502QVPC; Eukaryota.
DR   InParanoid; P58239; -.
DR   PRO; PR:P58239; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; 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   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   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..165
FT                   /note="Chondrosurfactant protein"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000005361"
FT   PROPEP          166..169
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000005362"
FT   CHAIN           170..286
FT                   /note="Chondromodulin-1"
FT                   /id="PRO_0000005363"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          75..157
FT                   /note="BRICHOS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00255"
FT   REGION          166..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..190
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        102..149
FT                   /evidence="ECO:0000250"
FT   DISULFID        234..238
FT                   /evidence="ECO:0000250"
FT   DISULFID        235..275
FT                   /evidence="ECO:0000250"
FT   DISULFID        245..269
FT                   /evidence="ECO:0000250"
FT   DISULFID        249..265
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  32235 MW;  21B377E0348EDDB3 CRC64;
     MEETAEKTPV EAYSTLKPKG LMKMKKTALV AFIAGAALLL FGGVGAFYLW KVTEKEAISA
     HLGRNIDIKI ENDSDSAEGT IVEVQDFKAG ITAVKFPGKE KCFIKSQART ELSEDEAGVK
     AEVASLVWIT SEEPLKDSSF LSPEILRFCA DLPIYWHHPA NSRALRKRRS ATRMRRQTSA
     GVNRQPARRR NSTASARDER PTGPEYNPEN PYHQNQGSEG TMVFDPMLDH RGICCTECHR
     SYTHCERVCE PLGGYWPWPY NYHGCRPVCR LIMPCRWWAA RVLGLV