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Latency-associated peptide (Transforming growth factor beta-2) (Transforming growth factor beta-2 proprotein) (Fragment)

 L0N335_NYMHO            Unreviewed;       366 AA.
L0N335;
06-MAR-2013, integrated into UniProtKB/TrEMBL.
06-MAR-2013, sequence version 1.
02-JUN-2021, entry version 39.
RecName: Full=Latency-associated peptide {ECO:0000256|ARBA:ARBA00018579};
AltName: Full=Transforming growth factor beta-2 {ECO:0000256|ARBA:ARBA00020548};
AltName: Full=Transforming growth factor beta-2 proprotein {ECO:0000256|ARBA:ARBA00018531};
Flags: Fragment;
Name=TGFB2 {ECO:0000313|EMBL:BAM72547.1};
Nymphicus hollandicus (Cockatiel).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Psittaciformes; Cacatuidae; Nymphicus.
NCBI_TaxID=13180 {ECO:0000313|EMBL:BAM72547.1};
[1] {ECO:0000313|EMBL:BAM72547.1}
NUCLEOTIDE SEQUENCE.
TISSUE=Jaw muscle {ECO:0000313|EMBL:BAM72547.1};
PubMed=23235703; DOI=10.1098/rspb.2012.2319;
Tokita M., Nakayama T., Schneider R.A., Agata K.;
"Molecular and cellular changes associated with the evolution of novel jaw
muscles in parrots.";
Proc. R. Soc. B 280:20122319-20122319(2013).
-!- FUNCTION: Transforming growth factor beta-2 proprotein: Precursor of
the Latency-associated peptide (LAP) and Transforming growth factor
beta-2 (TGF-beta-2) chains, which constitute the regulatory and active
subunit of TGF-beta-2, respectively. {ECO:0000256|ARBA:ARBA00002073}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Secreted, extracellular space, extracellular matrix
{ECO:0000256|ARBA:ARBA00004498}.
-!- SIMILARITY: Belongs to the TGF-beta family.
{ECO:0000256|ARBA:ARBA00006656, ECO:0000256|RuleBase:RU000354}.
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EMBL; AB761289; BAM72547.1; -; mRNA.
GO; GO:0031012; C:extracellular matrix; ISS:AgBase.
GO; GO:0005576; C:extracellular region; ISS:AgBase.
GO; GO:0005615; C:extracellular space; ISS:AgBase.
GO; GO:0001540; F:amyloid-beta binding; ISS:AgBase.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; ISS:AgBase.
GO; GO:0005102; F:signaling receptor binding; ISS:AgBase.
GO; GO:0005160; F:transforming growth factor beta receptor binding; ISS:AgBase.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISS:AgBase.
GO; GO:0034714; F:type III transforming growth factor beta receptor binding; ISS:AgBase.
GO; GO:0032147; P:activation of protein kinase activity; ISS:AgBase.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase.
GO; GO:0060038; P:cardiac muscle cell proliferation; ISS:AgBase.
GO; GO:0010002; P:cardioblast differentiation; ISS:AgBase.
GO; GO:0007050; P:cell cycle arrest; ISS:AgBase.
GO; GO:0008219; P:cell death; ISS:AgBase.
GO; GO:0016477; P:cell migration; ISS:AgBase.
GO; GO:0000902; P:cell morphogenesis; ISS:AgBase.
GO; GO:0045216; P:cell-cell junction organization; ISS:AgBase.
GO; GO:0030199; P:collagen fibril organization; ISS:AgBase.
GO; GO:0048566; P:embryonic digestive tract development; ISS:AgBase.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:AgBase.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:AgBase.
GO; GO:0001654; P:eye development; ISS:AgBase.
GO; GO:0008347; P:glial cell migration; ISS:AgBase.
GO; GO:0007507; P:heart development; ISS:AgBase.
GO; GO:0003007; P:heart morphogenesis; ISS:AgBase.
GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; ISS:AgBase.
GO; GO:0030308; P:negative regulation of cell growth; ISS:AgBase.
GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:AgBase.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:AgBase.
GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISS:AgBase.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISS:AgBase.
GO; GO:0051891; P:positive regulation of cardioblast differentiation; ISS:AgBase.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:AgBase.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030307; P:positive regulation of cell growth; ISS:AgBase.
GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:AgBase.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:AgBase.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:AgBase.
GO; GO:0045823; P:positive regulation of heart contraction; ISS:AgBase.
GO; GO:0045726; P:positive regulation of integrin biosynthetic process; ISS:AgBase.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:AgBase.
GO; GO:0045778; P:positive regulation of ossification; ISS:AgBase.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:AgBase.
GO; GO:0050714; P:positive regulation of protein secretion; ISS:AgBase.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:AgBase.
GO; GO:0051795; P:positive regulation of timing of catagen; ISS:AgBase.
GO; GO:0006468; P:protein phosphorylation; ISS:AgBase.
GO; GO:0032909; P:regulation of transforming growth factor beta2 production; ISS:AgBase.
GO; GO:0042493; P:response to drug; ISS:AgBase.
GO; GO:0032570; P:response to progesterone; ISS:AgBase.
GO; GO:0009611; P:response to wounding; ISS:AgBase.
GO; GO:0007435; P:salivary gland morphogenesis; ISS:AgBase.
GO; GO:0007165; P:signal transduction; ISS:AgBase.
GO; GO:0060395; P:SMAD protein signal transduction; ISS:BHF-UCL.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:AgBase.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR001839; TGF-b_C.
InterPro; IPR001111; TGF-b_propeptide.
InterPro; IPR016319; TGF-beta.
InterPro; IPR015615; TGF-beta-rel.
InterPro; IPR003940; TGFb2.
InterPro; IPR017948; TGFb_CS.
PANTHER; PTHR11848; PTHR11848; 1.
Pfam; PF00019; TGF_beta; 1.
Pfam; PF00688; TGFb_propeptide; 1.
PIRSF; PIRSF001787; TGF-beta; 1.
PRINTS; PR01423; TGFBETA.
PRINTS; PR01425; TGFBETA2.
SMART; SM00204; TGFB; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00250; TGF_BETA_1; 1.
PROSITE; PS51362; TGF_BETA_2; 1.
2: Evidence at transcript level;
Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
Coiled coil {ECO:0000256|SAM:Coils};
Disulfide bond {ECO:0000256|PIRSR:PIRSR001787-1};
Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
Growth factor {ECO:0000256|ARBA:ARBA00023030,
ECO:0000256|RuleBase:RU000354}; Mitogen {ECO:0000256|ARBA:ARBA00023246};
Secreted {ECO:0000256|ARBA:ARBA00022530}.
DOMAIN 266..366
/note="TGF_BETA_2"
/evidence="ECO:0000259|PROSITE:PS51362"
COILED 46..66
/evidence="ECO:0000256|SAM:Coils"
DISULFID 276..285
/evidence="ECO:0000256|PIRSR:PIRSR001787-1"
DISULFID 284..347
/evidence="ECO:0000256|PIRSR:PIRSR001787-1"
DISULFID 346
/note="Interchain"
/evidence="ECO:0000256|PIRSR:PIRSR001787-1"
NON_TER 1
/evidence="ECO:0000313|EMBL:BAM72547.1"
NON_TER 366
/evidence="ECO:0000313|EMBL:BAM72547.1"
SEQUENCE 366 AA; 42560 MW; EDDB5100CE5184C3 CRC64;
FMRKRIEAIR GQILSKLKLT SPPDEYPEPE EVPPEVISIY NSTRDLLQEK ANHRAATCER
ERSEEEYYAK EVYKIDMQPF YPENAIPPSY YSLYFRIVRF DVSAMEKNAS NLVKAELRVF
RLQNSKARVS EQRIELYQVL KSKELSSPGQ RYIDSKVVKT RAEGEWLSFD VTEAVHEWLH
HRDRNLGFKI SLHCPCCTFV PSNNYIIPNK SEELXARFAG IDDYTYSSGD VKALKSNRKK
YSGKTPHLLL MLLPSYRLES QQPSRRKKRA LDAAYCFRNV QDNCCLRPLY IDFKRDLGWK
WIHEPKGYHA NFCAGACPYL WSSDTQHSRV LSXYNTINPE ASASPCCVSQ DLEPLTILYY
IGKTPK


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[] Latency-associated peptide (Transforming growth factor beta-2) (Transforming growth factor beta-2 proprotein)
[TGFB1] Latency-associated peptide (Transforming growth factor beta-1) (Transforming growth factor beta-1 proprotein) (Fragment)
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Bibliography :