ID   CHRD_XENLA              Reviewed;         941 AA.
AC   Q91713; Q6DD60;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Chordin;
DE   AltName: Full=Organizer-specific secreted-dorsalizing factor;
DE   Flags: Precursor;
GN   Name=chrd;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC   TISSUE=Dorsal lip;
RX   PubMed=8001117; DOI=10.1016/0092-8674(94)90068-x;
RA   Sasai Y., Lu B., Steinbeisser H., Geissert D., Gont L.K., De Robertis E.M.;
RT   "Xenopus chordin: a novel dorsalizing factor activated by organizer-
RT   specific homeobox genes.";
RL   Cell 79:779-790(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INDUCTION.
RX   PubMed=8626017; DOI=10.1006/dbio.1996.0061;
RA   Gont L.K., Fainsod A., Kim S.-H., De Robertis E.M.;
RT   "Overexpression of the homeobox gene Xnot-2 leads to notochord formation in
RT   Xenopus.";
RL   Dev. Biol. 174:174-178(1996).
RN   [4]
RP   CLEAVAGE.
RX   PubMed=10864466; DOI=10.1006/dbio.2000.9740;
RA   Blitz I.L., Shimmi O., Wuennenberg-Stapleton K., O'Connor M.B., Cho K.W.Y.;
RT   "Is chordin a long-range- or short-range-acting factor? Roles for BMP1-
RT   related metalloproteases in chordin and BMP4 autofeedback loop
RT   regulation.";
RL   Dev. Biol. 223:120-138(2000).
RN   [5]
RP   INTERACTION WITH TWSG1 AND BMP4.
RX   PubMed=10866189; DOI=10.1038/35015500;
RA   Oelgeschlager M., Larrain J., Geissert D., De Robertis E.M.;
RT   "The evolutionarily conserved BMP-binding protein Twisted gastrulation
RT   promotes BMP signalling.";
RL   Nature 405:757-763(2000).
RN   [6]
RP   INTERACTION WITH OLFML3.
RX   PubMed=18775317; DOI=10.1016/j.cell.2008.07.008;
RA   Inomata H., Haraguchi T., Sasai Y.;
RT   "Robust stability of the embryonic axial pattern requires a secreted
RT   scaffold for chordin degradation.";
RL   Cell 134:854-865(2008).
CC   -!- FUNCTION: Potent dorsalizing factor. Has potent axis-forming activities
CC       including the ability to recruit neighboring cells into secondary axes.
CC       Regulates cell-cell interactions in the organizing centers of head,
CC       trunk and tail development. {ECO:0000269|PubMed:8001117}.
CC   -!- SUBUNIT: Interacts with twsg1 and/or bmp4. Interacts with olfml3/ont1.
CC       {ECO:0000269|PubMed:10866189, ECO:0000269|PubMed:18775317}.
CC   -!- INTERACTION:
CC       Q91713; B5MFE9: olfml3; NbExp=6; IntAct=EBI-1997746, EBI-1997734;
CC       Q91713; Q8JI28: tll1; NbExp=2; IntAct=EBI-1997746, EBI-1997794;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: First expressed at stage 9.5 in the dorsal marginal
CC       zone. Localized to the dorsal lip of the blastopore (Spemann organizer)
CC       during early gastrulation, after which expression continues in tissues
CC       derived from the organizer. Expressed in the prechordal plate (head
CC       mesoderm) and notochord during early neurulation (stage 13),
CC       transiently in the forebrain, tailbud hinge and posterior notochord in
CC       the early tailbud (stage 26), the chordoneural hinge in the late
CC       tailbud (stage 33) and finally the tip of the tail in the tadpole
CC       (stage 42). {ECO:0000269|PubMed:8001117}.
CC   -!- INDUCTION: By activin in the presence of de novo protein synthesis, and
CC       by gsc and not2. {ECO:0000269|PubMed:8001117,
CC       ECO:0000269|PubMed:8626017}.
CC   -!- PTM: Cleaved by bmp1; cleavage participates in dorsoventral patterning
CC       during early development. Cleavage by bmp1 is enhanced by the
CC       interaction with olfml3/ont1. {ECO:0000269|PubMed:10864466}.
CC   -!- SIMILARITY: Belongs to the chordin family. {ECO:0000305}.
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DR   EMBL; L35764; AAC42222.1; -; mRNA.
DR   EMBL; BC077767; AAH77767.1; -; mRNA.
DR   PIR; A55195; A55195.
DR   RefSeq; NP_001081778.1; NM_001088309.1.
DR   AlphaFoldDB; Q91713; -.
DR   SMR; Q91713; -.
DR   IntAct; Q91713; 4.
DR   GlyCosmos; Q91713; 4 sites, No reported glycans.
DR   DNASU; 398045; -.
DR   GeneID; 398045; -.
DR   KEGG; xla:398045; -.
DR   AGR; Xenbase:XB-GENE-865395; -.
DR   CTD; 398045; -.
DR   Xenbase; XB-GENE-865395; chrd.1.S.
DR   OrthoDB; 3039493at2759; -.
DR   PRO; PR:Q91713; -.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 398045; Expressed in gastrula and 9 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR   GO; GO:0045545; F:syndecan binding; ISS:UniProtKB.
DR   GO; GO:0009798; P:axis specification; IMP:UniProtKB.
DR   GO; GO:0043009; P:chordate embryonic development; IMP:UniProtKB.
DR   GO; GO:0036342; P:post-anal tail morphogenesis; IMP:UniProtKB.
DR   GO; GO:0048793; P:pronephros development; IMP:UniProtKB.
DR   Gene3D; 6.20.200.20; -; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 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; 3.
PE   1: Evidence at protein level;
KW   Developmental protein; Glycoprotein; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..941
FT                   /note="Chordin"
FT                   /id="PRO_0000005367"
FT   DOMAIN          41..117
FT                   /note="VWFC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          161..279
FT                   /note="CHRD 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT   DOMAIN          281..401
FT                   /note="CHRD 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT   DOMAIN          402..522
FT                   /note="CHRD 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT   DOMAIN          528..655
FT                   /note="CHRD 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT   DOMAIN          691..751
FT                   /note="VWFC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          769..838
FT                   /note="VWFC 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          857..919
FT                   /note="VWFC 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   REGION          922..941
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        244
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        350
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        433
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        735
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        110
FT                   /note="L -> G (in Ref. 2; AAH77767)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        839
FT                   /note="Missing (in Ref. 2; AAH77767)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   941 AA;  104947 MW;  7D1C3262064C7323 CRC64;
     MQCPPILLVW TLWIMAVDCS RPKVFLPIQP EQEPLQSKTP AGCTFGGKFY SLEDSWHPDL
     GEPFGVMHCV LCYCEPQRSR RGKPSGKVSC KNIKHDCPSP SCANPILLPL HCCKTCPKAP
     PPPIKKSDFV FDGFEYFQEK DDDLYNDRSY LSSDDVAVEE SRSEYVALLT APSHVWPPVT
     SGVAKARFNL QRSNLLFSIT YKWIDRLSRI RFSDLDGSVL FEHPVHRMGS PRDDTICGIW
     RSLNRSTLRL LRMGHILVSL VTTTLSEPEI SGKIVKHKAL FSESFSALLT PEDSDETGGG
     GLAMLTLSDV DDNLHFILML RGLSGEEGDQ IPILVQISHQ NHVIRELYAN ISAQEQDFAE
     VLPDLSSREM LWLAQGQLEI SVQTEGRRPQ SMSGIITVRK SCDTLQSVLS GGDALNPTKT
     GAVGSASITL HENGTLEYQI QIAGTMSTVT AVTLETKPRR KTKRNILHDM SKDYHDGRVW
     GYWIDANARD LHMLLQSELF LNVATKDFQE GELRGQITPL LYSGLWARYE KLPVPLAGQF
     VSPPIRTGSA GHAWVSLDEH CHLHYQIVVT GLGKAEDAAL NAHLHGFAEL GEVGESSPGH
     KRLLKGFYGS EAQGSVKDLD LELLGHLSRG TAFIQVSTKL NPRGEIRGQI HIPNSCESGG
     VSLTPEEPEY EYEIYEEGRQ RDPDDLRKDP RACSFEGQLR AHGSRWAPDY DRKCSVCSCQ
     KRTVICDPIV CPPLNCSQPV HLPDQCCPVC EEKKEMREVK KPERARTSEG CFFDGDRSWK
     AAGTRWHPFV PPFGLIKCAI CTCKGSTGEV HCEKVTCPKL SCTNPIRANP SDCCKQCPVE
     ERSPMELADS MQSDGAGSCR FGRHWYPNHE RWHPTVPPFG EMKCVTCTCA EGITQCRRQE
     CTGTTCGTGS KRDRCCTKCK DANQDEDEKV KSDETRTPWS F
//