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CHRD_RAT
ID   CHRD_RAT                Reviewed;         951 AA.
AC   Q63148;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Chordin;
DE   Flags: Precursor;
GN   Name=Chrd;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 653-828.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Kuroda S., Tokunaga C., Konishi H., Kikkawa U.;
RL   Submitted (JUL-1996) 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   -!- SUBUNIT: Interacts with TWSG1 and/or BMP4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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; AABR03079283; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; D86581; BAA13128.1; -; mRNA.
DR   AlphaFoldDB; Q63148; -.
DR   SMR; Q63148; -.
DR   STRING; 10116.ENSRNOP00000002394; -.
DR   GlyGen; Q63148; 3 sites.
DR   PaxDb; Q63148; -.
DR   PRIDE; Q63148; -.
DR   RGD; 620181; Chrd.
DR   eggNOG; ENOG502QR4J; Eukaryota.
DR   HOGENOM; CLU_008477_0_0_1; -.
DR   InParanoid; Q63148; -.
DR   PhylomeDB; Q63148; -.
DR   PRO; PR:Q63148; -.
DR   Proteomes; UP000002494; Unplaced.
DR   Genevisible; Q63148; RN.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0005576; C:extracellular region; ISO:RGD.
DR   GO; GO:0005615; C:extracellular space; ISO:RGD.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0036122; F:BMP binding; ISO:RGD.
DR   GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISO:RGD.
DR   GO; GO:0008201; F:heparin binding; ISO:RGD.
DR   GO; GO:0045545; F:syndecan binding; ISO:RGD.
DR   GO; GO:0048844; P:artery morphogenesis; ISO:RGD.
DR   GO; GO:0030509; P:BMP signaling pathway; ISO:RGD.
DR   GO; GO:0061312; P:BMP signaling pathway involved in heart development; ISO:RGD.
DR   GO; GO:0021919; P:BMP signaling pathway involved in spinal cord dorsal/ventral patterning; ISO:RGD.
DR   GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR   GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR   GO; GO:1904888; P:cranial skeletal system development; ISO:RGD.
DR   GO; GO:0035906; P:descending aorta development; ISO:RGD.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; ISO:RGD.
DR   GO; GO:0000578; P:embryonic axis specification; ISO:RGD.
DR   GO; GO:0035050; P:embryonic heart tube development; ISO:RGD.
DR   GO; GO:0072148; P:epithelial cell fate commitment; ISO:RGD.
DR   GO; GO:0035640; P:exploration behavior; ISO:RGD.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR   GO; GO:0030900; P:forebrain development; ISO:RGD.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; ISO:RGD.
DR   GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR   GO; GO:0060291; P:long-term synaptic potentiation; ISO:RGD.
DR   GO; GO:0045185; P:maintenance of protein location; ISO:RGD.
DR   GO; GO:0014030; P:mesenchymal cell fate commitment; ISO:RGD.
DR   GO; GO:0001707; P:mesoderm formation; ISO:RGD.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:RGD.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:RGD.
DR   GO; GO:0014029; P:neural crest formation; ISO:RGD.
DR   GO; GO:0048663; P:neuron fate commitment; ISO:RGD.
DR   GO; GO:0001649; P:osteoblast differentiation; ISO:RGD.
DR   GO; GO:0007389; P:pattern specification process; ISO:RGD.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; ISO:RGD.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISO:RGD.
DR   GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0017038; P:protein import; ISO:RGD.
DR   GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISO:RGD.
DR   GO; GO:1990926; P:short-term synaptic potentiation; ISO:RGD.
DR   GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR   GO; GO:0007224; P:smoothened signaling pathway; ISO:RGD.
DR   GO; GO:0050808; P:synapse organization; ISO:RGD.
DR   GO; GO:0048845; P:venous blood vessel morphogenesis; ISO:RGD.
DR   GO; GO:0008542; P:visual learning; ISO:RGD.
DR   InterPro; IPR016353; Chordin.
DR   InterPro; IPR010895; CHRD.
DR   InterPro; IPR001007; VWF_dom.
DR   Pfam; PF07452; CHRD; 2.
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; 2.
PE   2: Evidence at transcript level;
KW   Developmental protein; Glycoprotein; Reference proteome; Repeat; Secreted;
KW   Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..951
FT                   /note="Chordin"
FT                   /id="PRO_0000219088"
FT   DOMAIN          49..126
FT                   /note="VWFC 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          171..280
FT                   /note="CHRD 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT   DOMAIN          282..401
FT                   /note="CHRD 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT   DOMAIN          402..523
FT                   /note="CHRD 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT   DOMAIN          529..649
FT                   /note="CHRD 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00230"
FT   DOMAIN          702..762
FT                   /note="VWFC 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          782..848
FT                   /note="VWFC 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   DOMAIN          870..930
FT                   /note="VWFC 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT   REGION          144..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          669..701
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          932..951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        145..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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        880
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        746..749
FT                   /note="SCPH -> RCSQ (in Ref. 2; BAA13128)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        757
FT                   /note="C -> W (in Ref. 2; BAA13128)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        762
FT                   /note="P -> S (in Ref. 2; BAA13128)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        771
FT                   /note="P -> S (in Ref. 2; BAA13128)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        810
FT                   /note="A -> G (in Ref. 2; BAA13128)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        817..818
FT                   /note="AT -> VN (in Ref. 2; BAA13128)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        823
FT                   /note="C -> S (in Ref. 2; BAA13128)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   951 AA;  102007 MW;  F7E2F509718C0EBE CRC64;
     MPSLPAPPAP RLLLGLLLLG SRPAGGTGPE APALPIRSEK EPLPVRGAAG CSFGGKVYAL
     DETWHPDLGE PFGVMRCVLC ACEAPQWARR GRGPGRVSCK NIKPQCPTLA CRQPRQLPGH
     CCQTCPQDAE RSNLDPQPAG LVFEYPRDPE HRSYSDRGEP GTGERTRGDG HTEDFVALLT
     GPRTQAVARA RVSLLRSSLR FSISYQRLDR PSRVRFTDPT GNILFEHPAA PTQDGLVCGV
     WRAVPRLSVR LLRAEQLRVA LVTPTHPSEE VWGPLIWQGA LTAETFSAIL TLEDPLQRGV
     GGIALLTLSD TEDALHFLLL FRGLLGGLAH VPLKLQILHQ GQLLRELQAN ASAQEPGFAE
     VLPSLTDQEM DWLVLGELQM VLEKMGGPEL RISGYITTRQ SCDVLQSVLC GADALIPVQT
     GAAGSASFIL LGNGSLIYQV QVIGTGSEVV AMTLETKPQR KNQRTVLCHM AGLQLGGHMA
     VGVCSGLGAR GAHMLLQNEL FLNIGTKDFP DGELRGHVTA LCYSGHSAHY DRLPVPLAGA
     LVLPPVRSQA AGHAWLSLDT HCHLHYEVLL AGLGGSEQGT VTAHLLGPPG MPGPQRLLKG
     FYGSEAQGVV KDLEPVLLRH LTQGTASLLI TTKSNPRGEL RGQVHIASQC EVGGLRLASE
     GVRMSLAPNG EAATSPMLPA GPGPEAPVPA KHGSSGRPRD PNTCFFEGQQ RPHGARWAPN
     YDPLCSLCTC QRRTVICDPV VCPPPSCPHP VQALDQCCPV CPEKQRSRDL PSLPNLEPGE
     GCYFDGDRSW RAAGTRWHPV VPPFGLIKCA VCTCKGATGE VHCEKVQCPR LACAQPVRAN
     PTDCCKQCPV GSGTHAKLGD PMQADGPRGC RFAGQWFPEN QSWHPSVPPF GEMSCITCRC
     GAGVPHCERD DCSPPLSCGS GKESRCCSHC TAQRSSETRT LPELEKEAQR S
 
 
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