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NOD4A_XENLA
ID   NOD4A_XENLA             Reviewed;         402 AA.
AC   O13048;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Nodal homolog 4-A;
DE   AltName: Full=Nodal-related protein 4-A;
DE   AltName: Full=Xnr-4;
DE   AltName: Full=Xnr4;
DE   Flags: Precursor;
GN   Name=nodal4-a; Synonyms=nr4 {ECO:0000312|EMBL:AAC60127.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAC60127.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Gastrula {ECO:0000269|PubMed:9133442};
RX   PubMed=9133442; DOI=10.1006/dbio.1997.8510;
RA   Joseph E.M., Melton D.A.;
RT   "Xnr4: a Xenopus nodal-related gene expressed in the Spemann organizer.";
RL   Dev. Biol. 184:367-372(1997).
RN   [2] {ECO:0000305}
RP   FUNCTION, AND INDUCTION.
RX   PubMed=10375512; DOI=10.1242/dev.126.14.3229;
RA   Osada S., Wright C.V.E.;
RT   "Xenopus nodal-related signaling is essential for mesendodermal patterning
RT   during early embryogenesis.";
RL   Development 126:3229-3240(1999).
RN   [3] {ECO:0000305}
RP   FUNCTION, AND INDUCTION.
RX   PubMed=10572051; DOI=10.1242/dev.126.24.5759;
RA   Kofron M., Demel T., Xanthos J., Lohr J., Sun B., Sive H., Osada S.,
RA   Wright C.V.E., Wylie C., Heasman J.;
RT   "Mesoderm induction in Xenopus is a zygotic event regulated by maternal
RT   VegT via TGFbeta growth factors.";
RL   Development 126:5759-5770(1999).
RN   [4] {ECO:0000305}
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=10683171; DOI=10.1242/dev.127.6.1173;
RA   Agius E., Oelgeschlaeger M., Wessely O., Kemp C., De Robertis E.M.;
RT   "Endodermal Nodal-related signals and mesoderm induction in Xenopus.";
RL   Development 127:1173-1183(2000).
RN   [5] {ECO:0000305}
RP   FUNCTION, AND INDUCTION.
RX   PubMed=11784097; DOI=10.1006/dbio.2001.0493;
RA   Onuma Y., Takahashi S., Yokota C., Asashima M.;
RT   "Multiple nodal-related genes act coordinately in Xenopus embryogenesis.";
RL   Dev. Biol. 241:94-105(2002).
RN   [6] {ECO:0000305}
RP   FUNCTION, AND INDUCTION.
RX   PubMed=16651540; DOI=10.1242/dev.02358;
RA   Sinner D., Kirilenko P., Rankin S., Wei E., Howard L., Kofron M.,
RA   Heasman J., Woodland H.R., Zorn A.M.;
RT   "Global analysis of the transcriptional network controlling Xenopus
RT   endoderm formation.";
RL   Development 133:1955-1966(2006).
CC   -!- FUNCTION: Cooperation and regulatory loops of multiple nodals are
CC       essential for mesendoderm patterning in early embryos. Plays a role in
CC       mesoderm formation and may be required for neural development.
CC       {ECO:0000269|PubMed:10375512, ECO:0000269|PubMed:10572051,
CC       ECO:0000269|PubMed:11784097, ECO:0000269|PubMed:16651540,
CC       ECO:0000269|PubMed:9133442}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P43021}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q91620}.
CC   -!- TISSUE SPECIFICITY: During blastula stages, expressed in the endoderm
CC       at a higher level dorsally than ventrally. Expressed in the deep cells
CC       of the Spemann organizer at the gastrula stage. Expressed in the
CC       notochord (a derivative of the organizer) and neural tube during the
CC       neural stages. {ECO:0000269|PubMed:10683171,
CC       ECO:0000269|PubMed:9133442}.
CC   -!- DEVELOPMENTAL STAGE: Expressed zygotically. First expressed at the
CC       midblastula transition (MBT). {ECO:0000269|PubMed:10683171,
CC       ECO:0000269|PubMed:9133442}.
CC   -!- INDUCTION: By dorsal-mesoderm inducing signals including vegt and other
CC       nodal-related proteins. By sox17. {ECO:0000269|PubMed:10375512,
CC       ECO:0000269|PubMed:10572051, ECO:0000269|PubMed:10683171,
CC       ECO:0000269|PubMed:11784097, ECO:0000269|PubMed:16651540}.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000255}.
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DR   EMBL; U79162; AAC60127.1; -; mRNA.
DR   RefSeq; NP_001081816.1; NM_001088347.1.
DR   AlphaFoldDB; O13048; -.
DR   GeneID; 398068; -.
DR   KEGG; xla:398068; -.
DR   CTD; 398068; -.
DR   Xenbase; XB-GENE-864954; nodal.L.
DR   OrthoDB; 1518399at2759; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR001839; TGF-b_C.
DR   InterPro; IPR015615; TGF-beta-rel.
DR   InterPro; IPR017948; TGFb_CS.
DR   PANTHER; PTHR11848; PTHR11848; 1.
DR   Pfam; PF00019; TGF_beta; 1.
DR   SMART; SM00204; TGFB; 1.
DR   SUPFAM; SSF57501; SSF57501; 1.
DR   PROSITE; PS00250; TGF_BETA_1; 1.
DR   PROSITE; PS51362; TGF_BETA_2; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Developmental protein; Disulfide bond;
KW   Glycoprotein; Growth factor; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..278
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000334505"
FT   CHAIN           279..402
FT                   /note="Nodal homolog 4-A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000334506"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        238
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        302..368
FT                   /evidence="ECO:0000250|UniProtKB:P43021"
FT   DISULFID        331..399
FT                   /evidence="ECO:0000250|UniProtKB:P43021"
FT   DISULFID        335..401
FT                   /evidence="ECO:0000250|UniProtKB:P43021"
FT   DISULFID        367
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P43021"
SQ   SEQUENCE   402 AA;  46271 MW;  928B46B550443288 CRC64;
     MHLYFYCLIL LFVPGGNSLG INSYLKHMSN KPQDHVNRTK TVDSKDLAAL PLSSYMLNLY
     QSFHHSELNH GTEGAPSLPS NHRADIIRSL AAKSFDHGGS RWTLVFDFSS LSQEEEHQLA
     EVRFDFRAFE GAISAEMEVM VDFLHQSSSC QSISGWCQSY LYVGSLTGTL RSRSSDTWVT
     FEATDIIHKW FERNEKGKSR YEDREKQLKK LPRAKSAERR YQQQNTEDQQ IVMMVYSNIS
     KKERLSGTAT LLQDAAHSKY LVVMPGIQTI AHTRRHRRSH IFKEHVMGMK HVPPADSSRT
     LCRRVDFFVD FKQIGWDSWI IHPMKYNAYR CEGECPSPVN ESVKPNNHAY MQSLLNYYVK
     GKAPEVCCVP IRMSSLSMVY YDHDDIAFQN HEGMIVEECG CQ
 
 
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