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   24-JAN-2024, entry version 141.
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   GlyCosmos; Q9Z0E2; 3 sites, No reported glycans.
DR   GlyGen; Q9Z0E2; 3 sites.
DR   PhosphoSitePlus; Q9Z0E2; -.
DR   MaxQB; Q9Z0E2; -.
DR   PaxDb; 10090-ENSMUSP00000007171; -.
DR   ProteomicsDB; 279074; -.
DR   Antibodypedia; 33823; 284 antibodies from 27 providers.
DR   DNASU; 12667; -.
DR   Ensembl; ENSMUST00000007171.13; ENSMUSP00000007171.7; ENSMUSG00000006958.15.
DR   GeneID; 12667; -.
DR   KEGG; mmu:12667; -.
DR   UCSC; uc007yre.2; mouse.
DR   AGR; MGI:1313268; -.
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; 3039493at2759; -.
DR   PhylomeDB; Q9Z0E2; -.
DR   TreeFam; TF106451; -.
DR   BioGRID-ORCS; 12667; 0 hits in 76 CRISPR screens.
DR   PRO; PR:Q9Z0E2; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q9Z0E2; Protein.
DR   Bgee; ENSMUSG00000006958; Expressed in interphalangeal joint and 197 other cell types or tissues.
DR   ExpressionAtlas; Q9Z0E2; baseline and differential.
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:0008283; P:cell population proliferation; IGI:MGI.
DR   GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR   GO; GO:0160093; P:chordate pharynx 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:0010467; P:gene expression; 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:0021513; P:spinal cord dorsal/ventral patterning; ISO: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   Gene3D; 6.20.200.20; -; 1.
DR   InterPro; IPR016353; Chordin.
DR   InterPro; IPR010895; CHRD.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR46526; CHORDIN; 1.
DR   PANTHER; PTHR46526:SF1; CHORDIN; 1.
DR   Pfam; PF07452; CHRD; 3.
DR   Pfam; PF00093; VWC; 3.
DR   PIRSF; PIRSF002496; Chordin; 1.
DR   SMART; SM00754; CHRD; 4.
DR   SMART; SM00214; VWC; 4.
DR   SUPFAM; SSF57603; FnI-like domain; 4.
DR   PROSITE; PS50933; CHRD; 4.
DR   PROSITE; PS01208; VWFC_1; 2.
DR   PROSITE; PS50184; VWFC_2; 2.
DR   Genevisible; Q9Z0E2; MM.
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
//