CRDL2_MOUSE
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 03-AUG-2022, entry version 114.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP 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., Bolon B.,
RA Yokota T., Zhang K.;
RT "A novel chordin-like BMP inhibitor, CHL2, expressed preferentially in
RT chondrocytes of developing cartilage and osteoarthritic joint 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 project:
RT 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 and
RT complex alternative splicing in human tissues and during myoblast and
RT 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 preventing
CC or reducing the rate of matrix accumulation. May play a role during
CC myoblast and osteoblast differentiation, and maturation. {ECO:0000250,
CC ECO:0000269|PubMed:14660436, 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 expression of
CC isoforms was observed during myoblast and osteoblast differentiation
CC 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 ligaments
CC of the ovary and oviduct in females, and of testis, epididymis and
CC certain male accessory sex glands in males. Expression was high in
CC uterine myometrium. Weakly expressed in cartilage of the femoral head,
CC patella, articular facets of vertebrae, in the annulus fibrosus of
CC intervertebral disks. In normal cartilage, expression was confined to
CC articular chondrocytes especially in the superficial zone.
CC {ECO:0000269|PubMed:14660436}.
CC -!- DEVELOPMENTAL STAGE: In embryo expressed to the surface chondrocytes of
CC developing joint cartilage and to the connective tissue of reproductive
CC organs. {ECO:0000269|PubMed:14660436}.
CC -!- CAUTION: According to PubMed:14660436 interacts with human BMP2, BMP4,
CC BMP5, BMP6, BMP7 but not human INHBA. According to PubMed:15094188
CC interacts with human INHBA but not human BMP2, BMP4 and BMP6.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK50575.1; Type=Frameshift; Evidence={ECO:0000305};
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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 AlphaFoldDB; Q8VEA6; -.
DR SMR; Q8VEA6; -.
DR BioGRID; 213242; 6.
DR STRING; 10090.ENSMUSP00000032977; -.
DR GlyGen; Q8VEA6; 2 sites.
DR PhosphoSitePlus; Q8VEA6; -.
DR PaxDb; Q8VEA6; -.
DR PRIDE; Q8VEA6; -.
DR ProteomicsDB; 284167; -. [Q8VEA6-1]
DR DNASU; 69121; -.
DR GeneID; 69121; -.
DR KEGG; mmu:69121; -.
DR CTD; 25884; -.
DR MGI; MGI:1916371; Chrdl2.
DR eggNOG; ENOG502QQFQ; Eukaryota.
DR InParanoid; Q8VEA6; -.
DR OrthoDB; 454087at2759; -.
DR PhylomeDB; Q8VEA6; -.
DR BioGRID-ORCS; 69121; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Chrdl2; mouse.
DR PRO; PR:Q8VEA6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8VEA6; protein.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0036122; F:BMP binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0002062; P:chondrocyte 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; IPR030117; Chordin-like_2.
DR InterPro; IPR045717; CHRDL1/2.
DR InterPro; IPR045716; CHRDL_1/2_C.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR46303; PTHR46303; 1.
DR PANTHER; PTHR46303:SF3; PTHR46303:SF3; 1.
DR Pfam; PF19548; CHRDL_1_2_C; 1.
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; Developmental protein;
KW Differentiation; Glycoprotein; Osteogenesis; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..426
FT /note="Chordin-like protein 2"
FT /id="PRO_0000005372"
FT DOMAIN 31..96
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 109..175
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 246..311
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT REGION 182..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WN34"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 26
FT /note="R -> L (in Ref. 2; AAK50575)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="H -> Q (in Ref. 2; AAK50575)"
FT /evidence="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
