CRDL1_MOUSE
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 03-AUG-2022, entry version 135.
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.ENSMUSP00000074230; -.
DR GlyGen; Q920C1; 2 sites.
DR iPTMnet; Q920C1; -.
DR PhosphoSitePlus; Q920C1; -.
DR MaxQB; Q920C1; -.
DR PaxDb; Q920C1; -.
DR PRIDE; Q920C1; -.
DR ProteomicsDB; 283823; -. [Q920C1-1]
DR ProteomicsDB; 283824; -. [Q920C1-2]
DR Antibodypedia; 365; 258 antibodies from 28 providers.
DR DNASU; 83453; -.
DR Ensembl; ENSMUST00000063029; ENSMUSP00000056193; ENSMUSG00000031283. [Q920C1-1]
DR Ensembl; ENSMUST00000074660; ENSMUSP00000074230; ENSMUSG00000031283. [Q920C1-2]
DR Ensembl; ENSMUST00000112878; ENSMUSP00000108499; ENSMUSG00000031283. [Q920C1-1]
DR Ensembl; ENSMUST00000166406; ENSMUSP00000130284; ENSMUSG00000031283. [Q920C1-2]
DR GeneID; 83453; -.
DR KEGG; mmu:83453; -.
DR UCSC; uc009ume.2; mouse. [Q920C1-1]
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; LCGEETI; -.
DR OrthoDB; 454087at2759; -.
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 72 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 226 other tissues.
DR ExpressionAtlas; Q920C1; baseline and differential.
DR Genevisible; Q920C1; MM.
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 InterPro; IPR045717; CHRDL1/2.
DR InterPro; IPR045716; CHRDL_1/2_C.
DR InterPro; IPR001007; VWF_dom.
DR PANTHER; PTHR46303; PTHR46303; 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; 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
