ID   CRDL1_CHICK             Reviewed;         456 AA.
AC   Q90ZD5;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=NRLN1, VOPT;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
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).
CC   -!- FUNCTION: Seems to antagonize the function of BMP4 by binding to it and
CC       preventing its interaction with receptors.
CC       {ECO:0000269|PubMed:11441185}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11441185}.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in the ventral retina.
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DR   EMBL; AF257352; AAK73359.1; -; mRNA.
DR   RefSeq; NP_989502.1; NM_204171.1.
DR   RefSeq; XP_015133640.1; XM_015278154.1.
DR   AlphaFoldDB; Q90ZD5; -.
DR   SMR; Q90ZD5; -.
DR   STRING; 9031.ENSGALP00000013090; -.
DR   PaxDb; Q90ZD5; -.
DR   GeneID; 373985; -.
DR   KEGG; gga:373985; -.
DR   CTD; 91851; -.
DR   VEuPathDB; HostDB:geneid_373985; -.
DR   eggNOG; ENOG502QQFQ; Eukaryota.
DR   InParanoid; Q90ZD5; -.
DR   OrthoDB; 454087at2759; -.
DR   PhylomeDB; Q90ZD5; -.
DR   PRO; PR:Q90ZD5; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Developmental protein; Glycoprotein; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..456
FT                   /note="Chordin-like protein 1"
FT                   /id="PRO_0000005370"
FT   DOMAIN          36..101
FT                   /note="VWFC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          115..181
FT                   /note="VWFC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          262..327
FT                   /note="VWFC 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   MOTIF           181..183
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   456 AA;  52399 MW;  D54F6685F3839BC6 CRC64;
     MRRKWRSEDF HFVFFGVLCL LLIDRGKLEQ VKHSDTYCVF QDKKYRVGER WHPYLEPYGL
     VYCVNCLCSE NGNVLCSRIR CPSLHCPSPV HVPQLCCPRC PEDSLFSVSS KITGKSCEYN
     GTTYHHGEMF VAEGLFQNRQ ANQCAQCSCS EGNVYCGLKT CPKLTCSFPV SVPESCCPVC
     RGDGELSWEQ ADGDIFRQPA NREARHSYHR PHYELSPSST RQVVNVPRFP SARSNRGVLP
     DPQQASGTIV QIVINNKHKH GRVCVSNGKT YSHGESWHPN LRAFGIVECV LCTCNITKQE
     CKKIHCPEQY PCKYPQKVEG KCCKVCPEEV PSQSFDNKDY FCGKETFPVY ESIFTEEGET
     IRKIAVETEK PPQIEIHVWT IRKGILRHFY IEKMSKREFE ELPYFKQITR TTSSQWKIFS
     EGEAQISQMC ESRVCRTELE DLVKVLYLEK SEKGHC