TGFB2_CHICK
ID TGFB2_CHICK Reviewed; 412 AA.
AC P30371;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Transforming growth factor beta-2 proprotein;
DE Contains:
DE RecName: Full=Latency-associated peptide;
DE Short=LAP;
DE Contains:
DE RecName: Full=Transforming growth factor beta-2;
DE Short=TGF-beta-2;
DE Flags: Precursor;
GN Name=TGFB2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=White leghorn; TISSUE=Blood;
RX PubMed=1683775; DOI=10.1089/dna.1991.10.723;
RA Burt D.W., Paton I.R.;
RT "Molecular cloning and primary structure of the chicken transforming growth
RT factor-beta 2 gene.";
RL DNA Cell Biol. 10:723-734(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Chondrocyte;
RX PubMed=2340183; DOI=10.3109/08977199009071499;
RA Jakowlew S.B., Dillard P.J., Sporn M.B., Roberts A.B.;
RT "Complementary deoxyribonucleic acid cloning of an mRNA encoding
RT transforming growth factor-beta 2 from chicken embryo chondrocytes.";
RL Growth Factors 2:123-133(1990).
CC -!- FUNCTION: [Transforming growth factor beta-2 proprotein]: Precursor of
CC the Latency-associated peptide (LAP) and Transforming growth factor
CC beta-2 (TGF-beta-2) chains, which constitute the regulatory and active
CC subunit of TGF-beta-2, respectively. {ECO:0000250|UniProtKB:P01137,
CC ECO:0000250|UniProtKB:P04202}.
CC -!- FUNCTION: [Latency-associated peptide]: Required to maintain the
CC Transforming growth factor beta-2 (TGF-beta-2) chain in a latent state
CC during storage in extracellular matrix. Associates non-covalently with
CC TGF-beta-2 and regulates its activation via interaction with 'milieu
CC molecules', such as LTBP1 and LRRC32/GARP, that control activation of
CC TGF-beta-2. {ECO:0000250|UniProtKB:P01137,
CC ECO:0000250|UniProtKB:P04202}.
CC -!- FUNCTION: [Transforming growth factor beta-2]: Multifunctional protein
CC that regulates various processes such as angiogenesis and heart
CC development (By similarity). Activation into mature form follows
CC different steps: following cleavage of the proprotein in the Golgi
CC apparatus, Latency-associated peptide (LAP) and Transforming growth
CC factor beta-2 (TGF-beta-2) chains remain non-covalently linked
CC rendering TGF-beta-2 inactive during storage in extracellular matrix
CC (By similarity). At the same time, LAP chain interacts with 'milieu
CC molecules', such as LTBP1 and LRRC32/GARP, that control activation of
CC TGF-beta-2 and maintain it in a latent state during storage in
CC extracellular milieus (By similarity). Once activated following release
CC of LAP, TGF-beta-2 acts by binding to TGF-beta receptors (TGFBR1 and
CC TGFBR2), which transduce signal (By similarity).
CC {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202,
CC ECO:0000250|UniProtKB:P61812}.
CC -!- SUBUNIT: [Latency-associated peptide]: Interacts with Transforming
CC growth factor beta-2 (TGF-beta-2) chain; interaction is non-covalent
CC and maintains (TGF-beta-2) in a latent state (By similarity).
CC {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P61812}.
CC -!- SUBUNIT: [Transforming growth factor beta-2]: Homodimer; disulfide-
CC linked (By similarity). Interacts with TGF-beta receptors (TGFBR1 and
CC TGFBR2), leading to signal transduction (By similarity).
CC {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P61812}.
CC -!- SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted,
CC extracellular space, extracellular matrix
CC {ECO:0000250|UniProtKB:P01137}.
CC -!- SUBCELLULAR LOCATION: [Transforming growth factor beta-2]: Secreted
CC {ECO:0000250|UniProtKB:P01137}.
CC -!- PTM: [Transforming growth factor beta-2]: The precursor proprotein is
CC cleaved in the Golgi apparatus to form Transforming growth factor beta-
CC 2 (TGF-beta-2) and Latency-associated peptide (LAP) chains, which
CC remain non-covalently linked, rendering TGF-beta-2 inactive.
CC {ECO:0000250|UniProtKB:P01137}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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DR EMBL; X58071; CAA41101.1; -; Genomic_DNA.
DR EMBL; X59082; CAA41101.1; JOINED; Genomic_DNA.
DR EMBL; X59081; CAA41101.1; JOINED; Genomic_DNA.
DR EMBL; X59080; CAA41101.1; JOINED; Genomic_DNA.
DR PIR; A39489; A39489.
DR AlphaFoldDB; P30371; -.
DR SMR; P30371; -.
DR STRING; 9031.ENSGALP00000031309; -.
DR PaxDb; P30371; -.
DR VEuPathDB; HostDB:geneid_421352; -.
DR eggNOG; KOG3900; Eukaryota.
DR InParanoid; P30371; -.
DR PhylomeDB; P30371; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; ISS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; ISS:UniProtKB.
DR GO; GO:0005160; F:transforming growth factor beta receptor binding; ISS:UniProtKB.
DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISS:UniProtKB.
DR GO; GO:0034714; F:type III transforming growth factor beta receptor binding; ISA:AgBase.
DR GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0048513; P:animal organ development; TAS:AgBase.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; ISS:UniProtKB.
DR GO; GO:0010002; P:cardioblast differentiation; ISS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; TAS:AgBase.
DR GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0000902; P:cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
DR GO; GO:0030199; P:collagen fibril organization; ISS:UniProtKB.
DR GO; GO:0042416; P:dopamine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEP:AgBase.
DR GO; GO:0048566; P:embryonic digestive tract development; IEP:AgBase.
DR GO; GO:0048568; P:embryonic organ development; IEP:AgBase.
DR GO; GO:0042118; P:endothelial cell activation; NAS:AgBase.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0003198; P:epithelial to mesenchymal transition involved in endocardial cushion formation; TAS:DFLAT.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0001654; P:eye development; IEP:AgBase.
DR GO; GO:0008585; P:female gonad development; IEP:AgBase.
DR GO; GO:0008347; P:glial cell migration; ISS:UniProtKB.
DR GO; GO:0008406; P:gonad development; TAS:AgBase.
DR GO; GO:0007507; P:heart development; IEP:AgBase.
DR GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; ISS:UniProtKB.
DR GO; GO:0030324; P:lung development; IEP:AgBase.
DR GO; GO:0008584; P:male gonad development; IEP:AgBase.
DR GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; ISS:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; TAS:AgBase.
DR GO; GO:0030308; P:negative regulation of cell growth; ISA:AgBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; TAS:AgBase.
DR GO; GO:0021915; P:neural tube development; IEP:AgBase.
DR GO; GO:0048666; P:neuron development; ISS:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISS:UniProtKB.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0051891; P:positive regulation of cardioblast differentiation; ISS:UniProtKB.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0045823; P:positive regulation of heart contraction; ISS:UniProtKB.
DR GO; GO:0050778; P:positive regulation of immune response; ISS:UniProtKB.
DR GO; GO:0045726; P:positive regulation of integrin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0045778; P:positive regulation of ossification; ISA:AgBase.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISS:UniProtKB.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:UniProtKB.
DR GO; GO:0051795; P:positive regulation of timing of catagen; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISA:AgBase.
DR GO; GO:0045595; P:regulation of cell differentiation; NAS:AgBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:1903659; P:regulation of complement-dependent cytotoxicity; ISA:AgBase.
DR GO; GO:0040008; P:regulation of growth; NAS:AgBase.
DR GO; GO:0060390; P:regulation of SMAD protein signal transduction; ISA:AgBase.
DR GO; GO:0032909; P:regulation of transforming growth factor beta2 production; ISS:UniProtKB.
DR GO; GO:0060416; P:response to growth hormone; IEP:AgBase.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR GO; GO:0032570; P:response to progesterone; ISS:UniProtKB.
DR GO; GO:0009615; P:response to virus; IDA:AgBase.
DR GO; GO:0009611; P:response to wounding; ISA:AgBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0007435; P:salivary gland morphogenesis; ISA:AgBase.
DR GO; GO:0007165; P:signal transduction; ISA:AgBase.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEP:AgBase.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
DR GO; GO:0048103; P:somatic stem cell division; ISS:UniProtKB.
DR GO; GO:0001756; P:somitogenesis; IEP:AgBase.
DR GO; GO:0048536; P:spleen development; IEP:AgBase.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0042060; P:wound healing; ISS:UniProtKB.
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; IPR016319; TGF-beta.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR003940; TGFb2.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 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; PR01425; TGFBETA2.
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 3: Inferred from homology;
KW Cleavage on pair of basic residues; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Growth factor; Mitogen; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..412
FT /note="Transforming growth factor beta-2 proprotein"
FT /id="PRO_0000456185"
FT CHAIN 21..300
FT /note="Latency-associated peptide"
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT /id="PRO_0000033792"
FT CHAIN 301..412
FT /note="Transforming growth factor beta-2"
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT /id="PRO_0000033793"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 307..316
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 315..378
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 344..409
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 348..411
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 377
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P61812"
SQ SEQUENCE 412 AA; 47606 MW; 93E759BF1BD958DC CRC64;
MHCYLLSVFL TLDLAAVALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL TSPPDEYPEP
EEVPPEVISI YNSTRDLLQE KANHRAATCE RERSDEEYYA KEVYKIDMQP FYPENAIPPS
YYSLYFRIVR FDVSAMEKNA SNLVKAEFRV FRLQNSKARV SEQRIELYQV LKSKELSSPG
QRYIDSKVVK TRAEGEWLSF DVTEAVHEWL HHRDRNLGFK ISLHCPCCTF VPSNNYIIPN
KSEEPEARFA GIDDYTYSSG DVKALKSNRK KYSGKTPHLL LMLLPSYRLE SQQPSRRKKR
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYH ANFCAGACPY LWSSDTQHSR
VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS
