ID   CRDL1_MOUSE             Reviewed;         447 AA.
AC   Q920C1; Q924K0; Q9EPZ9;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 143.
DE   RecName: Full=Chordin-like protein 1;
DE   AltName: Full=Neuralin-1;
DE   AltName: Full=Neurogenesin-1;
DE   AltName: Full=Ventroptin;
DE   Flags: Precursor;
GN   Name=Chrdl1; Synonyms=Ng1, Nrln1;
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] (ISOFORMS ALPHA AND BETA).
RC   STRAIN=C57BL/6J;
RX   PubMed=11441185; DOI=10.1126/science.1058379;
RA   Sakuta H., Suzuki R., Takahashi H., Kato A., Shintani T., Iemura S.,
RA   Yamamoto T.S., Ueno N., Noda M.;
RT   "Ventroptin: a BMP-4 antagonist expressed in a double-gradient pattern in
RT   the retina.";
RL   Science 293:111-115(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
RX   PubMed=11118896; DOI=10.1016/s0925-4773(00)00507-4;
RA   Coffinier C.C., Tran U., Larrain J., De Robertis E.M.;
RT   "Neuralin-1 is a novel chordin-related molecule expressed in the mouse
RT   neural plate.";
RL   Mech. Dev. 100:119-122(2001).
RN   [3]
RP   FUNCTION, GLYCOSYLATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=16630536; DOI=10.1016/j.bbrc.2006.03.195;
RA   Chandra A., Itakura T., Yang Z., Tamakoshi T., Xue X., Wang B., Ueki T.,
RA   Sato K., Uezato T., Miura N.;
RT   "Neurogenesin-1 differentially inhibits the osteoblastic differentiation by
RT   bone morphogenetic proteins in C2C12 cells.";
RL   Biochem. Biophys. Res. Commun. 344:786-791(2006).
CC   -!- FUNCTION: Seems to antagonize the function of BMP4 by binding to it and
CC       preventing its interaction with receptors. Alters the fate commitment
CC       of neural stem cells from gliogenesis to neurogenesis. Contributes to
CC       neuronal differentiation of neural stem cells in the brain by
CC       preventing the adoption of a glial fate. May play a crucial role in
CC       dorsoventral axis formation (By similarity). Antagonizes the function
CC       of BMP7 and may thus play an important role in the embryonic bone
CC       formation. Shows no inhibitory effect on the inducing activity of BMP2.
CC       Plays a role during anterior segment eye development (By similarity).
CC       {ECO:0000250, ECO:0000269|PubMed:16630536}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Alpha;
CC         IsoId=Q920C1-1; Sequence=Displayed;
CC       Name=Beta;
CC         IsoId=Q920C1-2; Sequence=VSP_001076, VSP_001077;
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain, lung, liver, kidney and
CC       testis.
CC   -!- DEVELOPMENTAL STAGE: Expression starts in the neural plate at mid-
CC       gastrulation. Later on its expression becomes restricted to discrete
CC       regions of the central nervous system and to derivatives of the neural
CC       crest cells. Expressed as well in the primordial cells of the skeleton
CC       in mice embryos at 13.5 dpc. {ECO:0000269|PubMed:16630536}.
CC   -!- PTM: May be glycosylated. {ECO:0000269|PubMed:16630536}.
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DR   EMBL; AF321853; AAK95586.1; -; mRNA.
DR   EMBL; AF296451; AAK71523.1; -; mRNA.
DR   EMBL; AF305714; AAG27460.1; -; mRNA.
DR   CCDS; CCDS30453.1; -. [Q920C1-2]
DR   CCDS; CCDS53208.1; -. [Q920C1-1]
DR   RefSeq; NP_001107857.1; NM_001114385.1. [Q920C1-1]
DR   RefSeq; NP_112548.2; NM_031258.3. [Q920C1-2]
DR   AlphaFoldDB; Q920C1; -.
DR   SMR; Q920C1; -.
DR   STRING; 10090.ENSMUSP00000108499; -.
DR   GlyCosmos; Q920C1; 2 sites, No reported glycans.
DR   GlyGen; Q920C1; 2 sites.
DR   iPTMnet; Q920C1; -.
DR   PhosphoSitePlus; Q920C1; -.
DR   MaxQB; Q920C1; -.
DR   PaxDb; 10090-ENSMUSP00000074230; -.
DR   ProteomicsDB; 283823; -. [Q920C1-1]
DR   ProteomicsDB; 283824; -. [Q920C1-2]
DR   Antibodypedia; 365; 307 antibodies from 28 providers.
DR   DNASU; 83453; -.
DR   Ensembl; ENSMUST00000063029.13; ENSMUSP00000056193.7; ENSMUSG00000031283.17. [Q920C1-1]
DR   Ensembl; ENSMUST00000074660.12; ENSMUSP00000074230.6; ENSMUSG00000031283.17. [Q920C1-2]
DR   Ensembl; ENSMUST00000112878.9; ENSMUSP00000108499.3; ENSMUSG00000031283.17. [Q920C1-1]
DR   Ensembl; ENSMUST00000166406.3; ENSMUSP00000130284.3; ENSMUSG00000031283.17. [Q920C1-2]
DR   GeneID; 83453; -.
DR   KEGG; mmu:83453; -.
DR   UCSC; uc009ume.2; mouse. [Q920C1-1]
DR   AGR; MGI:1933172; -.
DR   CTD; 91851; -.
DR   MGI; MGI:1933172; Chrdl1.
DR   VEuPathDB; HostDB:ENSMUSG00000031283; -.
DR   eggNOG; ENOG502QQFQ; Eukaryota.
DR   GeneTree; ENSGT00940000160983; -.
DR   HOGENOM; CLU_048288_0_0_1; -.
DR   InParanoid; Q920C1; -.
DR   OMA; EDFRFIF; -.
DR   OrthoDB; 3670395at2759; -.
DR   PhylomeDB; Q920C1; -.
DR   Reactome; R-MMU-201451; Signaling by BMP.
DR   Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR   Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR   BioGRID-ORCS; 83453; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Chrdl1; mouse.
DR   PRO; PR:Q920C1; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q920C1; Protein.
DR   Bgee; ENSMUSG00000031283; Expressed in sciatic nerve and 227 other cell types or tissues.
DR   ExpressionAtlas; Q920C1; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0036122; F:BMP binding; IDA:MGI.
DR   GO; GO:0050431; F:transforming growth factor beta binding; IDA:MGI.
DR   GO; GO:0097113; P:AMPA glutamate receptor clustering; IMP:MGI.
DR   GO; GO:0030509; P:BMP signaling pathway; IMP:MGI.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0001709; P:cell fate determination; ISO:MGI.
DR   GO; GO:0000578; P:embryonic axis specification; IDA:MGI.
DR   GO; GO:0098976; P:excitatory chemical synaptic transmission; IMP:MGI.
DR   GO; GO:0001654; P:eye development; ISS:UniProtKB.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:MGI.
DR   GO; GO:0030182; P:neuron differentiation; ISO:MGI.
DR   GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR   GO; GO:0060074; P:synapse maturation; IMP:MGI.
DR   Gene3D; 6.20.200.20; -; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
DR   InterPro; IPR045717; CHRDL1/2.
DR   InterPro; IPR045716; CHRDL_1/2_C.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR46303:SF2; CHORDIN-LIKE PROTEIN 1; 1.
DR   PANTHER; PTHR46303; VWFC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF19548; CHRDL_1_2_C; 1.
DR   Pfam; PF00093; VWC; 3.
DR   SMART; SM00214; VWC; 3.
DR   SUPFAM; SSF57603; FnI-like domain; 3.
DR   PROSITE; PS01208; VWFC_1; 3.
DR   PROSITE; PS50184; VWFC_2; 3.
DR   Genevisible; Q920C1; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Developmental protein; Differentiation; Glycoprotein;
KW   Neurogenesis; Osteogenesis; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..447
FT                   /note="Chordin-like protein 1"
FT                   /id="PRO_0000005369"
FT   DOMAIN          30..95
FT                   /note="VWFC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          108..174
FT                   /note="VWFC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          253..318
FT                   /note="VWFC 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   REGION          200..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           174..176
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         319..333
FT                   /note="EEPPSQNFDSKGSFC -> GKKAKGALAGGPAFG (in isoform
FT                   Beta)"
FT                   /evidence="ECO:0000303|PubMed:11118896,
FT                   ECO:0000303|PubMed:11441185"
FT                   /id="VSP_001076"
FT   VAR_SEQ         334..447
FT                   /note="Missing (in isoform Beta)"
FT                   /evidence="ECO:0000303|PubMed:11118896,
FT                   ECO:0000303|PubMed:11441185"
FT                   /id="VSP_001077"
FT   CONFLICT        211
FT                   /note="N -> S (in Ref. 2; AAG27460)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   447 AA;  50732 MW;  94C999025A97545D CRC64;
     MDGMKYIISL FFIFVFLEGS KTEQVKHSDT YCVFQDKKYR VGEKWHPYLE PYGLVYCVNC
     ICSENGNVLC SRVRCPSLHC LSPVHIPHLC CPRCPDSLPP VNNKVTSKSC EYNGTTYQHG
     ELFIAEGLFQ NRQPNQCSQC SCSEGNVYCG LKTCPKLTCA FPVSVPDSCC RVCRGDAELS
     WEHADGDIFR QPANREARHS YLRSPYDPPP NRQAGGLPRF PGSRSHRGAV IDSQQASGTI
     VQIVINNKHK HGQVCVSNGK TYSHGESWHP NLRAFGIVEC VLCTCNVTKQ ECKKIHCPNR
     YPCKYPQKID GKCCKVCPEE PPSQNFDSKG SFCGEETMPV YESVFMEDGE TTRKVALETE
     RPPQVEVHVW TIQKGILQHF HIEKISKRMF GELHHFKLVT RTTLNQWKLF TEGEAQLSQM
     CSSQVCRTEL EDLVQVLYLG RPEKDHC
//