CHRD_MOUSE
ID CHRD_MOUSE Reviewed; 948 AA.
AC Q9Z0E2;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Chordin;
DE Flags: Precursor;
GN Name=Chrd;
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].
RC STRAIN=B6SJL/F1;
RA Lu B., Bachiller D., Agius E., Piccolo S., De Robertis E.M.;
RT "BMP-binding domains in the chordin secreted protein.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=9782094; DOI=10.1006/geno.1998.5474;
RA Pappano W.N., Scott I.C., Clark T.G., Eddy R.L., Shows T.B.,
RA Greenspan D.S.;
RT "Coding sequence and expression patterns of mouse chordin and mapping of
RT the cognate mouse chrd and human CHRD genes.";
RL Genomics 52:236-239(1998).
RN [3]
RP INTERACTION WITH TWSG1 AND BMP4.
RX PubMed=11260715; DOI=10.1038/35068572;
RA Scott I.C., Blitz I.L., Pappano W.N., Maas S.A., Cho K.W.Y.,
RA Greenspan D.S.;
RT "Homologues of Twisted gastrulation are extracellular cofactors in
RT antagonism of BMP signalling.";
RL Nature 410:475-478(2001).
CC -!- FUNCTION: Dorsalizing factor. Key developmental protein that dorsalizes
CC early vertebrate embryonic tissues by binding to ventralizing TGF-beta
CC family bone morphogenetic proteins (BMPs) and sequestering them in
CC latent complexes.
CC -!- SUBUNIT: Interacts with TWSG1 and/or BMP4.
CC {ECO:0000269|PubMed:11260715}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Detected at high levels in 7 dpc mouse embryos;
CC its level decreases at later developmental stages and in adult tissues.
CC {ECO:0000269|PubMed:9782094}.
CC -!- PTM: Cleaved by tolloid proteases; cleavage participates in
CC dorsoventral patterning during early development. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chordin family. {ECO:0000305}.
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DR EMBL; AF096276; AAD19895.1; -; mRNA.
DR EMBL; AF069501; AAC68867.1; -; mRNA.
DR CCDS; CCDS28059.1; -.
DR RefSeq; NP_001264970.1; NM_001278041.1.
DR RefSeq; NP_034023.1; NM_009893.2.
DR AlphaFoldDB; Q9Z0E2; -.
DR STRING; 10090.ENSMUSP00000007171; -.
DR GlyGen; Q9Z0E2; 3 sites.
DR PhosphoSitePlus; Q9Z0E2; -.
DR MaxQB; Q9Z0E2; -.
DR PaxDb; Q9Z0E2; -.
DR PRIDE; Q9Z0E2; -.
DR ProteomicsDB; 279074; -.
DR Antibodypedia; 33823; 258 antibodies from 27 providers.
DR DNASU; 12667; -.
DR Ensembl; ENSMUST00000007171; ENSMUSP00000007171; ENSMUSG00000006958.
DR GeneID; 12667; -.
DR KEGG; mmu:12667; -.
DR UCSC; uc007yre.2; mouse.
DR CTD; 8646; -.
DR MGI; MGI:1313268; Chrd.
DR VEuPathDB; HostDB:ENSMUSG00000006958; -.
DR eggNOG; ENOG502QR4J; Eukaryota.
DR GeneTree; ENSGT00940000161767; -.
DR HOGENOM; CLU_008477_0_0_1; -.
DR InParanoid; Q9Z0E2; -.
DR OrthoDB; 647180at2759; -.
DR PhylomeDB; Q9Z0E2; -.
DR TreeFam; TF106451; -.
DR BioGRID-ORCS; 12667; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q9Z0E2; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9Z0E2; protein.
DR Bgee; ENSMUSG00000006958; Expressed in interphalangeal joint and 195 other tissues.
DR ExpressionAtlas; Q9Z0E2; baseline and differential.
DR Genevisible; Q9Z0E2; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0036122; F:BMP binding; IDA:MGI.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:MGI.
DR GO; GO:0008201; F:heparin binding; IDA:MGI.
DR GO; GO:0045545; F:syndecan binding; IDA:MGI.
DR GO; GO:0048844; P:artery morphogenesis; IMP:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR GO; GO:0061312; P:BMP signaling pathway involved in heart development; IMP:MGI.
DR GO; GO:0021919; P:BMP signaling pathway involved in spinal cord dorsal/ventral patterning; ISO:MGI.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR GO; GO:1904888; P:cranial skeletal system development; IGI:MGI.
DR GO; GO:0035906; P:descending aorta development; IMP:MGI.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR GO; GO:0000578; P:embryonic axis specification; IDA:MGI.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
DR GO; GO:0072148; P:epithelial cell fate commitment; IDA:MGI.
DR GO; GO:0035640; P:exploration behavior; IMP:MGI.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:MGI.
DR GO; GO:0030900; P:forebrain development; IMP:MGI.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR GO; GO:0045185; P:maintenance of protein location; IDA:MGI.
DR GO; GO:0014030; P:mesenchymal cell fate commitment; IDA:MGI.
DR GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:MGI.
DR GO; GO:0014029; P:neural crest formation; IMP:MGI.
DR GO; GO:0048663; P:neuron fate commitment; IDA:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IDA:MGI.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISO:MGI.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IMP:MGI.
DR GO; GO:0017038; P:protein import; IDA:MGI.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
DR GO; GO:1990926; P:short-term synaptic potentiation; IMP:MGI.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IGI:MGI.
DR GO; GO:0042305; P:specification of segmental identity, mandibular segment; IGI:MGI.
DR GO; GO:0050808; P:synapse organization; IMP:MGI.
DR GO; GO:0048845; P:venous blood vessel morphogenesis; IMP:MGI.
DR GO; GO:0008542; P:visual learning; IMP:MGI.
DR InterPro; IPR016353; Chordin.
DR InterPro; IPR010895; CHRD.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF07452; CHRD; 2.
DR Pfam; PF00093; VWC; 3.
DR PIRSF; PIRSF002496; Chordin; 1.
DR SMART; SM00754; CHRD; 4.
DR SMART; SM00214; VWC; 4.
DR PROSITE; PS50933; CHRD; 4.
DR PROSITE; PS01208; VWFC_1; 2.
DR PROSITE; PS50184; VWFC_2; 2.
PE 1: Evidence at protein level;
KW Developmental protein; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..948
FT /note="Chordin"
FT /id="PRO_0000005365"
FT DOMAIN 49..126
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 168..277
FT /note="CHRD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT DOMAIN 279..398
FT /note="CHRD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT DOMAIN 399..520
FT /note="CHRD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT DOMAIN 526..646
FT /note="CHRD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT DOMAIN 699..759
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 779..845
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 867..927
FT /note="VWFC 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT REGION 143..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 665..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 877
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 948 AA; 101513 MW; 4DC2DA01D9BD2147 CRC64;
MPSLPAPPAP RLLLGLLLLG SRPASGTGPE PPALPIRSEK EPLPVRGAAG CSFGGKVYAL
DETWHPDLGE PFGVMRCVLC ACEAPQWARR GRGPGRVSCK NIKPQCPTLA CRQPRQLPGH
CCQTCPQERS NLDPQPAGLV FEYPRDPEHR SYSDRGEPGV GERTRADGHT DFVALLTGPR
SQAVARARVS LLRSSLRFSV SYQRLDRPSR VRFTDPTGNI LFEHPATPTQ DGLVCGVWRA
VPRLSVRLLR AEQLRVALVT STHPSGEVWG PLIWQGALAA ETFSAILTLE DPLQRGVGGI
ALLTLSDTED SLHFLLLFRG LLGGLAQAPL KLQILHQGQL LRELQANTSA QEPGFAEVLP
SLTDQEMDWL ELGELQMVLE KAGGPELRIS GYITTRQSCD VLQSVLCGAD ALIPVQTGAA
GSASFILLGN GSLIYQVQVV GTGSEVVAMT LETKPQRKNQ RTVLCHMAGL QPGGHMAVGM
CSGLGARGAH MLLQNELFLN VGTKDFPDGE LRGHVTALCY SGHSARYDRL PVPLAGALVL
PPVRSQAAGH AWLSLDTHCH LHYEVLLAGL GGSEQGTVTA HLLGPPGMPG PQRLLKGFYG
SEAQGVVKDL EPVLLRHLAQ GTASLLITTK SSPRGELRGQ VHIASQCEAG GLRLASEGVQ
MPLAPNGEAA TSPMLPAGPG PEAPVPAKHG SPGRPRDPNT CFFEGQQRPH GARWAPNYDP
LCSLCICQRR TVICDPVVCP PPSCPHPVQA LDQCCPVCPE KQRSRDLPSL PNLEPGEGCY
FDGDRSWRAA GTRWHPVVPP FGLIKCAVCT CKGATGEVHC EKVQCPRLAC AQPVRANPTD
CCKQCPVGSG TNAKLGDPMQ ADGPRGCRFA GQWFPENQSW HPSVPPFGEM SCITCRCGAG
VPHCERDDCS PPLSCGSGKE SRCCSHCTAQ RSSETRTLPE LEKEAEHS
