CHRD_XENLA
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 03-AUG-2022, entry version 93.
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 PRIDE; Q91713; -.
DR DNASU; 398045; -.
DR GeneID; 398045; -.
DR KEGG; xla:398045; -.
DR CTD; 398045; -.
DR Xenbase; XB-GENE-865395; chrd.1.S.
DR OrthoDB; 647180at2759; -.
DR PRO; PR:Q91713; -.
DR Proteomes; UP000186698; Chromosome 5S.
DR Bgee; 398045; Expressed in gastrula and 9 other 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 InterPro; IPR016353; Chordin.
DR InterPro; IPR010895; CHRD.
DR InterPro; IPR001007; VWF_dom.
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 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
