CNMD_MOUSE
ID CNMD_MOUSE Reviewed; 334 AA.
AC Q9Z1F6; Q80UX1; Q9CXU5;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Leukocyte cell-derived chemotaxin 1 {ECO:0000305};
DE AltName: Full=Chondromodulin {ECO:0000312|MGI:MGI:1341171};
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|MGI:MGI:1341171};
GN Synonyms=Chmi {ECO:0000312|MGI:MGI:1341171},
GN Lect1 {ECO:0000312|MGI:MGI:1341171};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hiraki Y., Shukunami C., Inoue H., Suzuki F.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
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 (By similarity). Inhibits in vitro tube formation and
CC mobilization of endothelial cells (By similarity). Plays a role as
CC antiangiogenic factor in cardiac valves to suppress neovascularization.
CC {ECO:0000250, ECO:0000269|PubMed:16980969}.
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:0000305}; Single-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in the four cardiac valves, valvular
CC interstitial cells and extracellular matrix (at protein level).
CC {ECO:0000269|PubMed:16980969}.
CC -!- DEVELOPMENTAL STAGE: Detected from 9.5 dpc in the cardiac valve
CC precursor cells from the atrioventricular cushions and outflow. At 10
CC dpc expressed in the cardiac jelly covering the trabeculating
CC cardiomyocytes of the left ventricle, the outer curvature of the right
CC ventricle and the outflow tract. Expression in the ventricles decreased
CC gradually as development progressed, and disappeared by mid-
CC embryogenesis (at protein level). {ECO:0000269|PubMed:16980969}.
CC -!- PTM: After cleavage, the post-translationally modified ChM-I is
CC secreted as a glycoprotein. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Aged mice show enhanced VEGFA expression,
CC angiogenesis, inflammatory cell infiltration, aortic stenosis, lipid
CC deposition and calcification in the cardiac valves.
CC {ECO:0000269|PubMed:16980969}.
CC -!- SIMILARITY: Belongs to the chondromodulin-1 family. {ECO:0000305}.
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DR EMBL; U43509; AAD00027.1; -; mRNA.
DR EMBL; AK013975; BAB29095.1; -; mRNA.
DR EMBL; CH466535; EDL35758.1; -; Genomic_DNA.
DR EMBL; BC045152; AAH45152.1; -; mRNA.
DR CCDS; CCDS27302.1; -.
DR RefSeq; NP_001297584.1; NM_001310655.1.
DR RefSeq; NP_034831.2; NM_010701.3.
DR AlphaFoldDB; Q9Z1F6; -.
DR SMR; Q9Z1F6; -.
DR STRING; 10090.ENSMUSP00000022603; -.
DR GlyGen; Q9Z1F6; 1 site.
DR PhosphoSitePlus; Q9Z1F6; -.
DR CPTAC; non-CPTAC-3402; -.
DR PaxDb; Q9Z1F6; -.
DR PRIDE; Q9Z1F6; -.
DR ProteomicsDB; 285511; -.
DR Antibodypedia; 24240; 204 antibodies from 28 providers.
DR DNASU; 16840; -.
DR Ensembl; ENSMUST00000022603; ENSMUSP00000022603; ENSMUSG00000022025.
DR GeneID; 16840; -.
DR KEGG; mmu:16840; -.
DR UCSC; uc007utg.2; mouse.
DR CTD; 11061; -.
DR MGI; MGI:1341171; Cnmd.
DR VEuPathDB; HostDB:ENSMUSG00000022025; -.
DR eggNOG; ENOG502QVPC; Eukaryota.
DR GeneTree; ENSGT00480000042679; -.
DR InParanoid; Q9Z1F6; -.
DR OMA; GNLPIFW; -.
DR OrthoDB; 1308600at2759; -.
DR TreeFam; TF329712; -.
DR BioGRID-ORCS; 16840; 2 hits in 69 CRISPR screens.
DR ChiTaRS; Cnmd; mouse.
DR PRO; PR:Q9Z1F6; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9Z1F6; protein.
DR Bgee; ENSMUSG00000022025; Expressed in humerus cartilage element and 132 other tissues.
DR ExpressionAtlas; Q9Z1F6; baseline and differential.
DR Genevisible; Q9Z1F6; MM.
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:0001886; P:endothelial cell morphogenesis; IDA:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:MGI.
DR GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; IMP:MGI.
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; 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_0000005349"
FT PROPEP 211..214
FT /evidence="ECO:0000250"
FT /id="PRO_0000005350"
FT CHAIN 215..334
FT /note="Chondromodulin-1"
FT /evidence="ECO:0000250"
FT /id="PRO_0000005351"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 105..201
FT /note="BRICHOS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00255"
FT REGION 212..270
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 132..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 CONFLICT 108
FT /note="A -> R (in Ref. 2; BAB29095)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="E -> K (in Ref. 1; AAD00027)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="A -> V (in Ref. 1; AAD00027)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="K -> KANFA (in Ref. 2; BAB29095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 37225 MW; BFAAA0B224DC9944 CRC64;
MTENSDKVPI TMVGPEDVEF CSPPAYTTVT VKPSGSPTRL LKVGAVVLIS GAVLLLFGAI
GAFYFWKGND NHIYNVHYSM SINGKLQDGS MEIDAVNNLE TFKMGSGAEE AIEVNDFKNG
ITGIRFAGGE KCYIKAQVKA RIPEVGTVTK QSISELEGKI MPANYEENSL IWVAVDQPVK
DSSFLSSKIL ELCGDLPIFW LKPMYPKEIQ RERREVVRNS APSTTRRPHS EPRGNAGPGR
LSNGTRPNVQ DDAEPFNPDN PYHQQEGESM TFDPRLDHEG ICCIECRRSY THCQKICEPL
GGYYPWPYNY QGCRSACRVV MPCSWWVARI LGMV
