CHRD_DANRE
ID CHRD_DANRE Reviewed; 940 AA.
AC O57472; Q9DED8;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Chordin;
DE AltName: Full=Protein chordino;
DE Flags: Precursor;
GN Name=chd; Synonyms=chrd;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Embryo;
RX PubMed=9441687; DOI=10.1006/dbio.1997.8788;
RA Miller-Bertoglio V.E., Fisher S., Sanchez A., Mullins M.C., Halpern M.E.;
RT "Differential regulation of chordin expression domains in mutant
RT zebrafish.";
RL Dev. Biol. 192:537-550(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-42.
RA Fujii R., Hibi M., Hirano T., Shimizu T.;
RT "Regulation of chordino.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Dorsalizing factor. Key developmental protein that dorsalizes
CC early vertebrate embryonic tissues by binding to ventralizing TGF-beta
CC family bone morphogenetic proteins (BMPs) and sequestering them in
CC latent complexes (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:9441687}.
CC -!- SUBUNIT: Interacts with twsg1 and/or bmp4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: During gastrulation, levels are highest in the
CC organizer region. Also present in the developing brain and in paraxial
CC mesoderm and ectoderm. {ECO:0000269|PubMed:9441687}.
CC -!- DEVELOPMENTAL STAGE: First detected shortly after the midbastula
CC transition. Levels increase during gastrulation, persist through early
CC somatogenesis, but then decrease and are gone by 24 hours.
CC {ECO:0000269|PubMed:9441687}.
CC -!- PTM: Cleaved by tolloid proteases; cleavage participates in
CC dorsoventral patterning during early development. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chordin family. {ECO:0000305}.
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DR EMBL; AF034606; AAB93485.1; -; mRNA.
DR EMBL; AB043968; BAB18642.1; -; Genomic_DNA.
DR AlphaFoldDB; O57472; -.
DR SMR; O57472; -.
DR STRING; 7955.ENSDARP00000045109; -.
DR PaxDb; O57472; -.
DR ZFIN; ZDB-GENE-990415-33; chrd.
DR eggNOG; ENOG502QR4J; Eukaryota.
DR InParanoid; O57472; -.
DR PhylomeDB; O57472; -.
DR PRO; PR:O57472; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0036122; F:BMP binding; IBA:GO_Central.
DR GO; GO:0009948; P:anterior/posterior axis specification; IDA:ZFIN.
DR GO; GO:0035143; P:caudal fin morphogenesis; IMP:ZFIN.
DR GO; GO:0061371; P:determination of heart left/right asymmetry; IMP:ZFIN.
DR GO; GO:0007368; P:determination of left/right symmetry; IMP:ZFIN.
DR GO; GO:0048264; P:determination of ventral identity; IMP:ZFIN.
DR GO; GO:0060030; P:dorsal convergence; IGI:ZFIN.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:ZFIN.
DR GO; GO:0003143; P:embryonic heart tube morphogenesis; IMP:ZFIN.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:ZFIN.
DR GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR GO; GO:0070121; P:Kupffer's vesicle development; IMP:ZFIN.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:ZFIN.
DR GO; GO:0043049; P:otic placode formation; IGI:ZFIN.
DR GO; GO:2000223; P:regulation of BMP signaling pathway involved in heart jogging; IMP:ZFIN.
DR GO; GO:0001756; P:somitogenesis; IMP:ZFIN.
DR GO; GO:0010159; P:specification of animal organ position; IMP:ZFIN.
DR InterPro; IPR016353; Chordin.
DR InterPro; IPR010895; CHRD.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF07452; CHRD; 3.
DR Pfam; PF00093; VWC; 4.
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; 3.
DR PROSITE; PS50184; VWFC_2; 4.
PE 2: Evidence at transcript level;
KW Developmental protein; Glycoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..940
FT /note="Chordin"
FT /id="PRO_0000005366"
FT DOMAIN 42..118
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 162..277
FT /note="CHRD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT DOMAIN 279..398
FT /note="CHRD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT DOMAIN 404..519
FT /note="CHRD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT DOMAIN 525..652
FT /note="CHRD 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT DOMAIN 689..748
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 767..836
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 855..919
FT /note="VWFC 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 940 AA; 104999 MW; B855CAF84F4623AC CRC64;
MMEGLLWILL SVIIASVHGS RLKTPALPIQ PEREPMISKG LSGCSFGGRF YSLEDTWHPD
LGEPFGVMHC VMCHCEPQRS RRGKVFGKVS CRNMKQDCPD PTCDDPVLLP GHCCKTCPKG
DSGRKEVESL FDFFQEKDDD LHKSYNDRSY ISSEDTSTRD STTTDFVALL TGVTDSWLPS
SSGVARARFT LSRTSLTFSI TFQRINRPSL IAFLDTDGNT AFEFRVPQAD NDMICGIWKN
VPKPHMRQLE AEQLHVSMTT ADNRKEELQG RIIKHRALFA ETFSAILTSD EVHSGMGGIA
MLTLSDTENN LHFILIMQGL VPPGSSKVPV RVKLQYRQHL LREIRANITA DDSDFAEVLA
DLNSRELFWL SRGQLQISVQ TEGQTLRHIS GFISGRRSCD TLQSVLSSGA ALTAGQTGGV
GSAVFTLHPN GSLDYQLLVA GLSSAVLSVS IEMKPRRRNK RSVLYELSAV FTDQRAAGSC
GRVEARHTHM LLQNELFINI ATALQPDGEL RGQIRLLPYN GLDARRNELP VPLAGVLVSP
PVRTGAAGHA WVSVDPQCHL HYEIIVNGLS KSEDASISAH LHGLAEIGEM DDSSTNHKRL
LTGFYGQQAQ GVLKDISVEL LRHLNEGTAY LQVSTKMNPR GEIRGRIHVP NHCESPAPRA
EFLEEPEFED LLFTREPTEL RKDTHTHVHS CFFEGEQHTH GSQWTPQYNT CFTCTCQKKT
VICDPVMCPT LSCTHTVQPE DQCCPICEEK KESKETAAVE KVEENPEGCY FEGDQKMHAP
GTTWHPFVPP FGYIKCAVCT CKGSTGEVHC EKVTCPPLTC SRPIRRNPSD CCKECPPEET
PPLEDEEMMQ ADGTRLCKFG KNYYQNSEHW HPSVPLVGEM KCITCWCDHG VTKCQRKQCP
LLSCRNPIRT EGKCCPECIE DFMEKEEMAK MAEKKKSWRH
