CNMD_CHICK
ID CNMD_CHICK Reviewed; 347 AA.
AC Q9PUU8; Q9YI63;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10590475;
RX DOI=10.1002/(sici)1097-0177(199911)216:3<233::aid-dvdy2>3.0.co;2-g;
RA Dietz U.H., Ziegelmeier G., Bittner K., Bruckner P., Balling R.;
RT "Spatio-temporal distribution of Chondromodulin-I mRNA in the chicken
RT embryo: expression during cartilage development and formation of the heart
RT and eye.";
RL Dev. Dyn. 216:233-243(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Fetal sternum;
RX PubMed=10452551; DOI=10.1016/s0014-5793(99)00931-x;
RA Shukunami C., Yamamoto S., Tanabe T., Hiraki Y.;
RT "Generation of multiple transcripts from the chicken chondromodulin-I gene
RT and their expression during embryonic development.";
RL FEBS Lett. 456:165-170(1999).
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 -!- TISSUE SPECIFICITY: Expressed in the cartilage and in fetal
CC precartilaginous tissues as well as in heart and eye.
CC -!- DEVELOPMENTAL STAGE: Expression onset occurs between stage 10 and stage
CC 13.
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; AF138280; AAD32212.1; -; mRNA.
DR EMBL; AF027380; AAD08642.1; -; mRNA.
DR RefSeq; NP_990141.1; NM_204810.1.
DR AlphaFoldDB; Q9PUU8; -.
DR SMR; Q9PUU8; -.
DR STRING; 9031.ENSGALP00000027337; -.
DR PaxDb; Q9PUU8; -.
DR GeneID; 395600; -.
DR KEGG; gga:395600; -.
DR CTD; 395600; -.
DR VEuPathDB; HostDB:geneid_395600; -.
DR eggNOG; ENOG502QVPC; Eukaryota.
DR InParanoid; Q9PUU8; -.
DR OrthoDB; 1308600at2759; -.
DR PhylomeDB; Q9PUU8; -.
DR PRO; PR:Q9PUU8; -.
DR Proteomes; UP000000539; 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..209
FT /note="Chondrosurfactant protein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005358"
FT PROPEP 210..213
FT /evidence="ECO:0000255"
FT /id="PRO_0000005359"
FT CHAIN 214..347
FT /note="Chondromodulin-1"
FT /id="PRO_0000005360"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 103..200
FT /note="BRICHOS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 130..192
FT /evidence="ECO:0000250"
FT DISULFID 295..299
FT /evidence="ECO:0000250"
FT DISULFID 296..336
FT /evidence="ECO:0000250"
FT DISULFID 306..330
FT /evidence="ECO:0000250"
FT DISULFID 310..326
FT /evidence="ECO:0000250"
FT CONFLICT 250
FT /note="D -> E (in Ref. 2; AAD08642)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 38636 MW; F3C5FF338E5D4B66 CRC64;
MAEGSEKVPI ARAGPEDVEQ GLPPAYTAAV PPPGPGRLLK AGATVLIAGA LLLLAGAIGA
FYFWKATERQ VYNVHYTMSI NGKVQDGSME IDAGNNLETF KTGSGSEEAV EVHDFQIGIT
GIRFAGGEKC YIKAQPKARV PEVDAMTKAS LSSDLEDEIM PVRFDENSLI WVAADEPIKH
NGFLSPKILE LCGDLPIFWL RPTYPKDKQR ERREMKRNKR QSESNFDAEH RAAAAEEVNT
RSTPTQLTQD LGPQSNETRP MQQESDQTLN PDNPYNQLEG EGMAFDPMLD HLGVCCIECR
RSYTQCQRIC EPLLGYYPWP YNYQGCRTAC RIIMPCSWWV ARIMGVV
