ID CRDL2_MOUSE Reviewed; 426 AA. AC Q8VEA6; Q925I3; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 13-FEB-2019, entry version 100. DE RecName: Full=Chordin-like protein 2; DE Flags: Precursor; GN Name=Chrdl2; Synonyms=Chl2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, AND INTERACTION WITH BMPS; GDF5 AND INHBA. RX PubMed=14660436; DOI=10.1242/dev.00901; RA Nakayama N., Han C.-Y.E., Cam L., Lee J.I., Pretorius J., Fisher S., RA Rosenfeld R., Scully S., Nishinakamura R., Duryea D., Van G., RA Bolon B., Yokota T., Zhang K.; RT "A novel chordin-like BMP inhibitor, CHL2, expressed preferentially in RT chondrocytes of developing cartilage and osteoarthritic joint RT cartilage."; RL Development 131:229-240(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; RA Coffinier C.C., De Robertis E.M.; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, AND ALTERNATIVE SPLICING. RX PubMed=15094188; DOI=10.1016/j.gene.2004.01.029; RA Oren A., Toporik A., Biton S., Almogy N., Eshel D., Bernstein J., RA Savitsky K., Rotman G.; RT "hCHL2, a novel chordin-related gene, displays differential expression RT and complex alternative splicing in human tissues and during myoblast RT and osteoblast maturation."; RL Gene 331:17-31(2004). CC -!- FUNCTION: Implicated in tumor angiogenesis (By similarity). May CC inhibits BMPs activity by blocking their interaction with their CC receptors. Has a negative regulator effect on the cartilage CC formation/regeneration from immature mesenchymal cells, by CC preventing or reducing the rate of matrix accumulation. May play a CC role during myoblast and osteoblast differentiation, and CC maturation. {ECO:0000250, ECO:0000269|PubMed:14660436, CC ECO:0000269|PubMed:15094188}. CC -!- SUBUNIT: Interacts with GDF5. May interact with INHBA, BMP2, BMP4, CC BMP5, BMP6, and BMP7. {ECO:0000269|PubMed:14660436}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=Additional isoforms seem to exist. Differential CC expression of isoforms was observed during myoblast and CC osteoblast differentiation and maturation.; CC Name=1; CC IsoId=Q8VEA6-1; Sequence=Displayed; CC -!- TISSUE SPECIFICITY: Weakly expressed in the liver and kidney. In CC reproductive organs expressed in connective tissues such as CC ligaments of the ovary and oviduct in females, and of testis, CC epididymis and certain male accessory sex glands in males. CC Expression was high in uterine myometrium. Weakly expressed in CC cartilage of the femoral head, patella, articular facets of CC vertebrae, in the annulus fibrosus of intervertebral disks. In CC normal cartilage, expression was confined to articular CC chondrocytes especially in the superficial zone. CC {ECO:0000269|PubMed:14660436}. CC -!- DEVELOPMENTAL STAGE: In embryo expressed to the surface CC chondrocytes of developing joint cartilage and to the connective CC tissue of reproductive organs. {ECO:0000269|PubMed:14660436}. CC -!- CAUTION: According to PubMed:14660436 interacts with human BMP2, CC BMP4, BMP5, BMP6, BMP7 but not human INHBA. According to CC PubMed:15094188 interacts with human INHBA but not human BMP2, CC BMP4 and BMP6. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAK50575.1; Type=Frameshift; Positions=388; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF338222; AAK50575.1; ALT_FRAME; mRNA. DR EMBL; BC019399; AAH19399.1; -; mRNA. DR CCDS; CCDS21492.1; -. [Q8VEA6-1] DR RefSeq; NP_001278249.1; NM_001291320.1. DR RefSeq; NP_598470.3; NM_133709.3. DR UniGene; Mm.285295; -. DR ProteinModelPortal; Q8VEA6; -. DR SMR; Q8VEA6; -. DR BioGrid; 213242; 6. DR STRING; 10090.ENSMUSP00000032977; -. DR PhosphoSitePlus; Q8VEA6; -. DR PaxDb; Q8VEA6; -. DR PRIDE; Q8VEA6; -. DR GeneID; 69121; -. DR KEGG; mmu:69121; -. DR CTD; 25884; -. DR MGI; MGI:1916371; Chrdl2. DR eggNOG; ENOG410IF8R; Eukaryota. DR eggNOG; ENOG410YI5E; LUCA. DR HOGENOM; HOG000049211; -. DR HOVERGEN; HBG051113; -. DR InParanoid; Q8VEA6; -. DR KO; K17280; -. DR OrthoDB; 454087at2759; -. DR PhylomeDB; Q8VEA6; -. DR PRO; PR:Q8VEA6; -. DR Proteomes; UP000000589; Unplaced. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW. DR GO; GO:0030154; P:cell differentiation; IDA:MGI. DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:MGI. DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW. DR InterPro; IPR001007; VWF_dom. DR Pfam; PF00093; VWC; 3. DR SMART; SM00214; VWC; 3. DR PROSITE; PS01208; VWFC_1; 3. DR PROSITE; PS50184; VWFC_2; 3. PE 1: Evidence at protein level; KW Alternative splicing; Chondrogenesis; Complete proteome; KW Developmental protein; Differentiation; Glycoprotein; Osteogenesis; KW Phosphoprotein; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1 25 {ECO:0000250}. FT CHAIN 26 426 Chordin-like protein 2. FT /FTId=PRO_0000005372. FT DOMAIN 31 96 VWFC 1. {ECO:0000255|PROSITE- FT ProRule:PRU00220}. FT DOMAIN 109 175 VWFC 2. {ECO:0000255|PROSITE- FT ProRule:PRU00220}. FT DOMAIN 246 311 VWFC 3. {ECO:0000255|PROSITE- FT ProRule:PRU00220}. FT MOD_RES 182 182 Phosphoserine. FT {ECO:0000250|UniProtKB:Q6WN34}. FT CARBOHYD 114 114 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 186 186 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CONFLICT 26 26 R -> L (in Ref. 2; AAK50575). FT {ECO:0000305}. FT CONFLICT 335 335 H -> Q (in Ref. 2; AAK50575). FT {ECO:0000305}. SQ SEQUENCE 426 AA; 47765 MW; 45BAB7BEE09AFE04 CRC64; MVPGVRIIPS LLGLVMFWLP LDSQARSRSG KVCLFGEKIY TPGQSWHPYL EPQGTIYCVR CTCSENGHVN CYRLRCPPLH CSQPVMEPQQ CCPRCVDPHV PSGLRVPLKS CQLNETTYQH GEIFSAQELF PARLSNQCVL CSCIEGHTYC GLMTCPEPSC PTTLPLPDSC CQTCKDRTTE SSTEENLTQL QHGERHSQDP CSERRGPSTP APTSLSSPLG FIPRHFQSVG MGSTTIKIIL KEKHKKACTH NGKTYSHGEV WHPTVLSFGP MPCILCTCID GYQDCHRVTC PTQYPCSQPK KVAGKCCKIC PEDEAEDDHS EVISTRCPKV PGQFHVYTLA SPSPDSLHRF VLEHEASDQV EMYIWKLVKG IYHLVQIKRV RKQDFQKEAQ NFRLLTGTHE GYWTVFLAQT PELKVTASPD KVTKTL //