ID U3FVV0_MICFL Unreviewed; 410 AA.
AC U3FVV0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 08-NOV-2023, entry version 41.
DE RecName: Full=Transforming growth factor beta {ECO:0000256|PIRNR:PIRNR001787};
OS Micrurus fulvius (Eastern coral snake) (Coluber fulvius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Elapidae; Elapinae; Micrurus.
OX NCBI_TaxID=8637 {ECO:0000313|EMBL:JAB53191.1};
RN [1] {ECO:0000313|EMBL:JAB53191.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Venom gland {ECO:0000313|EMBL:JAB53191.1};
RX PubMed=23915248; DOI=10.1186/1471-2164-14-531;
RA Margres M.J., Aronow K., Loyacano J., Rokyta D.R.;
RT "The venom-gland transcriptome of the eastern coral snake (Micrurus
RT fulvius) reveals high venom complexity in the intragenomic evolution of
RT venoms.";
RL BMC Genomics 14:531-531(2013).
CC -!- FUNCTION: Transforming growth factor beta-3 proprotein: Precursor of
CC the Latency-associated peptide (LAP) and Transforming growth factor
CC beta-3 (TGF-beta-3) chains, which constitute the regulatory and active
CC subunit of TGF-beta-3, respectively. {ECO:0000256|ARBA:ARBA00003972}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|PIRNR:PIRNR001787}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the TGF-beta family.
CC {ECO:0000256|ARBA:ARBA00006656, ECO:0000256|PIRNR:PIRNR001787,
CC ECO:0000256|RuleBase:RU000354}.
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DR EMBL; GAEP01001630; JAB53191.1; -; mRNA.
DR AlphaFoldDB; U3FVV0; -.
DR GO; GO:0031012; C:extracellular matrix; ISS:AgBase.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-UniRule.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; ISS:AgBase.
DR GO; GO:0050431; F:transforming growth factor beta binding; ISS:AgBase.
DR GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISS:AgBase.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISS:AgBase.
DR GO; GO:0034714; F:type III transforming growth factor beta receptor binding; ISS:AgBase.
DR GO; GO:0045216; P:cell-cell junction organization; ISS:AgBase.
DR GO; GO:0070483; P:detection of hypoxia; ISS:AgBase.
DR GO; GO:0060325; P:face morphogenesis; ISS:AgBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:AgBase.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISS:AgBase.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:AgBase.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISS:AgBase.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:AgBase.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0001666; P:response to hypoxia; ISS:AgBase.
DR GO; GO:0032570; P:response to progesterone; ISS:AgBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; ISS:AgBase.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:AgBase.
DR CDD; cd19386; TGF_beta_TGFB3; 1.
DR Gene3D; 2.60.120.970; -; 1.
DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR001111; TGF-b_propeptide.
DR InterPro; IPR016319; TGF-beta.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR015618; TGFB3.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; TGF-BETA FAMILY; 1.
DR PANTHER; PTHR11848:SF34; TRANSFORMING GROWTH FACTOR BETA-3 PROPROTEIN; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 1.
DR PIRSF; PIRSF001787; TGF-beta; 1.
DR PRINTS; PR01423; TGFBETA.
DR PRINTS; PR01426; TGFBETA3.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; Cystine-knot cytokines; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001787-1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Growth factor {ECO:0000256|ARBA:ARBA00023030,
KW ECO:0000256|PIRNR:PIRNR001787};
KW Mitogen {ECO:0000256|ARBA:ARBA00023246, ECO:0000256|PIRNR:PIRNR001787};
KW Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PIRNR:PIRNR001787};
KW Signal {ECO:0000256|PIRNR:PIRNR001787}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT CHAIN 22..410
FT /note="Transforming growth factor beta"
FT /evidence="ECO:0000256|PIRNR:PIRNR001787"
FT /id="PRO_5004642529"
FT DOMAIN 295..410
FT /note="TGF-beta family profile"
FT /evidence="ECO:0000259|PROSITE:PS51362"
FT DISULFID 305..314
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 313..376
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 342..407
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 346..409
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
FT DISULFID 375
FT /note="Interchain"
FT /evidence="ECO:0000256|PIRSR:PIRSR001787-1"
SQ SEQUENCE 410 AA; 46936 MW; 1BC415B6568E60A5 CRC64;
MHLRGTLLLL SLLSLATVSL SLSSCTTLDL EHIKKKRIEA IRGQILSKLR LTSPPESVGR
SHVPYQVLAL YNSTRELLEE MEEEKEDSCS QDNSESEYYA KEIHKFDMIQ GFPEHNELPL
CPKGVTSNMF RFNVSSAETN ITNLFRAEFR VLRLPNLSSK RSEQRIELFQ ILKPDEHIAK
QRYLSGRNVL TRGSPEWLSF DVTETVREWL FHRESNLGLE ISVHCPCNTF QSNGDILENL
HEVLEIKFKG IDGEESHGRG DLGSLKKQKD LQNPHLILMM LPPHRLGSSA VRSQRKKRAL
DTNYCFRNLE ENCCVRRLYI DFRQDLGWKW VHEPKGYFAN FCSGPCPYLR SADTTHSTIL
GLYNTLNPEA SASPCCVPQD LDPLTILYYV GRTPKVEQLS NMVVKSCKCS
//
