ID   UNIV_STRPU              Reviewed;         395 AA.
AC   P48970;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Univin;
DE   Flags: Precursor;
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7958442; DOI=10.1006/dbio.1994.1303;
RA   Stenzel P., Angerer L.M., Smith B.J., Angerer R.C., Vale W.W.;
RT   "The univin gene encodes a member of the transforming growth factor-beta
RT   superfamily with restricted expression in the sea urchin embryo.";
RL   Dev. Biol. 166:149-158(1994).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS.
RA   Angerer L.M., Stenzel P.;
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Could have a critical role in early developmental decisions
CC       in the sea urchin embryo.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Highest levels of expression in the egg and
CC       prehatching blastula. During late cleavage stages, it accumulates
CC       progressively to a circumequatorial band. During gastrulation it is
CC       detected primarily in the presumptive foregut and ciliated band. By
CC       pluteus stage, it is detected only in these cell types.
CC   -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR   EMBL; U10533; AAA57553.2; -; mRNA.
DR   RefSeq; NP_999793.1; NM_214628.1.
DR   AlphaFoldDB; P48970; -.
DR   SMR; P48970; -.
DR   STRING; 7668.SPU_000668-tr; -.
DR   EnsemblMetazoa; NM_214628; NP_999793; LOC373488.
DR   GeneID; 373488; -.
DR   KEGG; spu:373488; -.
DR   eggNOG; KOG3900; Eukaryota.
DR   HOGENOM; CLU_020515_4_0_1; -.
DR   OrthoDB; 919690at2759; -.
DR   PhylomeDB; P48970; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR001839; TGF-b_C.
DR   InterPro; IPR001111; TGF-b_propeptide.
DR   InterPro; IPR015615; TGF-beta-rel.
DR   InterPro; IPR017948; TGFb_CS.
DR   PANTHER; PTHR11848; PTHR11848; 1.
DR   Pfam; PF00019; TGF_beta; 1.
DR   Pfam; PF00688; TGFb_propeptide; 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; Cytokine; Disulfide bond; Glycoprotein;
KW   Growth factor; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..272
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000034002"
FT   CHAIN           273..395
FT                   /note="Univin"
FT                   /id="PRO_0000034003"
FT   REGION          69..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        294..360
FT                   /evidence="ECO:0000250"
FT   DISULFID        323..392
FT                   /evidence="ECO:0000250"
FT   DISULFID        327..394
FT                   /evidence="ECO:0000250"
FT   DISULFID        359
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   395 AA;  43837 MW;  0FA3340DF5A6360E CRC64;
     MDVSKVLILT LIWLLTADSA PPDYVTLTRK MESKILRVMG LSERPRPKPN ATAPQYMWDL
     YRQQMAATEG AAASRGGETE IGKEEEEDGR PCSETKLSSN IIRSVSHTGG DLRASNSTSL
     QQILLFDVAS IPHAETIEAA DLRLEIPALP SATDVPSLAV RIYQLESRTR LNSIVSLKDK
     RLRLLDVVLA DLSQGYAGTI DILSTVNSWR SKKTSNHGLL LHVELMSTSG NNRRGSQVIK
     ELGAISKKCT ANLIVTSSEY RQCSKRNRRN KRQAESEAPA DISSFPTASL TNLCQRHRLF
     VSFRDVGWEN WIIAPMGYQA YYCDGECPFP LGERLNGTNH AIIQTLVNSI DNRAVPKVCC
     APTKLSGISM LYFDNNENVV LRQYEDMVVE ACGCR