ID   DVR1_XENLA              Reviewed;         360 AA.
AC   P09534;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Protein DVR-1;
DE   AltName: Full=Vegetal hemisphere VG1 protein;
DE            Short=VG-1;
DE   Flags: Precursor;
GN   Name=dvr1; Synonyms=vg1;
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 [GENOMIC DNA].
RX   PubMed=3479264; DOI=10.1016/0092-8674(87)90109-7;
RA   Weeks D.L., Melton D.A.;
RT   "A maternal mRNA localized to the vegetal hemisphere in Xenopus eggs codes
RT   for a growth factor related to TGF-beta.";
RL   Cell 51:861-867(1987).
RN   [2]
RP   GLYCOSYLATION AT ASN-113; ASN-181 AND ASN-301.
RX   PubMed=2519512; DOI=10.1002/j.1460-2075.1989.tb03473.x;
RA   Dale L., Matthews G., Tabe L., Colman A.;
RT   "Developmental expression of the protein product of Vg1, a localized
RT   maternal mRNA in the frog Xenopus laevis.";
RL   EMBO J. 8:1057-1065(1989).
CC   -!- FUNCTION: Serves to facilitate the differentiation of either mesoderm
CC       or endoderm either as a cofactor in an instructive signal or by
CC       providing permissive environment.
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Vegetal region of the egg.
CC   -!- DEVELOPMENTAL STAGE: Abundant in oocytes and present throughout
CC       cleavage and gastrula stage. Not readily detected at a stage when
CC       somitogenesis is nearly complete in 24 hours embryos. Steady state
CC       level decreases in a continuous fashion with developmental age.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR   EMBL; M18055; AAA49727.1; -; Genomic_DNA.
DR   PIR; A29619; A29619.
DR   AlphaFoldDB; P09534; -.
DR   SMR; P09534; -.
DR   iPTMnet; P09534; -.
DR   PRIDE; P09534; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0051781; P:positive regulation of cell division; 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   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW   Growth factor; Mitogen; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..246
FT                   /id="PRO_0000033814"
FT   CHAIN           247..360
FT                   /note="Protein DVR-1"
FT                   /id="PRO_0000033815"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:2519512"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:2519512"
FT   CARBOHYD        301
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305|PubMed:2519512"
FT   DISULFID        259..325
FT                   /evidence="ECO:0000250"
FT   DISULFID        288..357
FT                   /evidence="ECO:0000250"
FT   DISULFID        292..359
FT                   /evidence="ECO:0000250"
FT   DISULFID        324
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   360 AA;  41773 MW;  E444A18AA2750984 CRC64;
     MVWLRLWAFL HILAIVTLDP ELKRREELFL RSLGFSSKPN PVSPPPVPSI LWRIFNQRMG
     SSIQKKKPDL CFVEEFNVPG SVIRVFPDQG RFIIPYSDDI HPTQCLEKRL FFNISAIEKE
     ERVTMGSGIE VQPEHLLRKG IDLRLYRTLQ ITLKGMGRSK TSRKLLVAQT FRLLHKSLFF
     NLTEICQSWQ DPLKNLGLVL EIFPKKESSW MSTANDECKD IQTFLYTSLL TVTLNPLRCK
     RPRRKRSYSK LPFTASNICK KRHLYVEFKD VGWQNWVIAP QGYMANYCYG ECPYPLTEIL
     NGSNHAILQT LVHSIEPEDI PLPCCVPTKM SPISMLFYDN NDNVVLRHYE NMAVDECGCR