TGFB2_MUSPF
ID TGFB2_MUSPF Reviewed; 414 AA.
AC Q38L25;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 73.
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 Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; Mustelinae;
OC Mustela.
OX NCBI_TaxID=9669;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Senchak A.J., Sato A., Vazquez R., Cable B.B.;
RT "Mustela putorious furo transforming growth factor beta-2 cDNA.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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: Interacts with the serine proteases, HTRA1 and HTRA3 (By
CC similarity). Interacts with ASPN (By similarity). Interacts with MFAP5
CC (By similarity). {ECO:0000250|UniProtKB:P01137,
CC ECO:0000250|UniProtKB:P27090, 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). Interacts
CC with LRRC32/GARP; leading to regulate activation of TGF-beta-2 (By
CC similarity). Interacts with NREP; the interaction results in a decrease
CC in TGFB2 autoinduction (By similarity). {ECO:0000250|UniProtKB:P01137,
CC ECO:0000250|UniProtKB:P27090, ECO:0000250|UniProtKB:P61812}.
CC -!- SUBUNIT: [Transforming growth factor beta-2]: Transforming growth
CC factor beta-2: Homodimer; disulfide-linked (By similarity).
CC Transforming growth factor beta-2: Interacts with TGF-beta receptors
CC (TGFBR1 and TGFBR2), leading to signal transduction (By similarity).
CC {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P27090,
CC 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; DQ217927; ABA86560.1; -; mRNA.
DR RefSeq; NP_001297116.1; NM_001310187.1.
DR AlphaFoldDB; Q38L25; -.
DR SMR; Q38L25; -.
DR STRING; 9669.ENSMPUP00000004208; -.
DR GeneID; 101677182; -.
DR CTD; 7042; -.
DR eggNOG; KOG3900; Eukaryota.
DR InParanoid; Q38L25; -.
DR Proteomes; UP000000715; Unassembled WGS sequence.
DR GO; GO:0031012; C:extracellular matrix; ISS:AgBase.
DR GO; GO:0005576; C:extracellular region; ISS:AgBase.
DR GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR GO; GO:0001540; F:amyloid-beta binding; ISS:AgBase.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:AgBase.
DR GO; GO:0005102; F:signaling receptor binding; ISS:AgBase.
DR GO; GO:0005160; F: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:0032147; P:activation of protein kinase activity; ISS:AgBase.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0060038; P:cardiac muscle cell proliferation; ISS:AgBase.
DR GO; GO:0010002; P:cardioblast differentiation; ISS:AgBase.
DR GO; GO:0008219; P:cell death; ISS:AgBase.
DR GO; GO:0016477; P:cell migration; ISS:AgBase.
DR GO; GO:0000902; P:cell morphogenesis; ISS:AgBase.
DR GO; GO:0045216; P:cell-cell junction organization; ISS:AgBase.
DR GO; GO:0030199; P:collagen fibril organization; ISS:AgBase.
DR GO; GO:0048566; P:embryonic digestive tract development; ISS:AgBase.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:AgBase.
DR GO; GO:0001654; P:eye development; ISS:AgBase.
DR GO; GO:0008347; P:glial cell migration; ISS:AgBase.
DR GO; GO:0001942; P:hair follicle development; ISS:AgBase.
DR GO; GO:0007507; P:heart development; ISS:AgBase.
DR GO; GO:0003007; P:heart morphogenesis; ISS:AgBase.
DR GO; GO:0010693; P:negative regulation of alkaline phosphatase activity; ISS:AgBase.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:AgBase.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:AgBase.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:AgBase.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISS:AgBase.
DR GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISS:AgBase.
DR GO; GO:0051891; P:positive regulation of cardioblast differentiation; ISS:AgBase.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISS:AgBase.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:AgBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:AgBase.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:AgBase.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:AgBase.
DR GO; GO:0045823; P:positive regulation of heart contraction; ISS:AgBase.
DR GO; GO:0045726; P:positive regulation of integrin biosynthetic process; ISS:AgBase.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:AgBase.
DR GO; GO:0045778; P:positive regulation of ossification; ISS:AgBase.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:AgBase.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISS:AgBase.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:AgBase.
DR GO; GO:0051795; P:positive regulation of timing of catagen; ISS:AgBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:AgBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:AgBase.
DR GO; GO:0032909; P:regulation of transforming growth factor beta2 production; ISS:AgBase.
DR GO; GO:0032570; P:response to progesterone; ISS:AgBase.
DR GO; GO:0009611; P:response to wounding; ISS:AgBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:AgBase.
DR GO; GO:0007435; P:salivary gland morphogenesis; ISS:AgBase.
DR GO; GO:0007165; P:signal transduction; ISS:AgBase.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:AgBase.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:AgBase.
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 2: Evidence at transcript level;
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..414
FT /note="Transforming growth factor beta-2 proprotein"
FT /id="PRO_0000456182"
FT CHAIN 21..302
FT /note="Latency-associated peptide"
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT /id="PRO_0000232492"
FT CHAIN 303..414
FT /note="Transforming growth factor beta-2"
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT /id="PRO_0000232493"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 309..318
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 317..380
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 346..411
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 350..413
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 379
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P61812"
SQ SEQUENCE 414 AA; 47706 MW; C3AB53094D066FB2 CRC64;
MHYCVLSAFL LLHLVTAALS LSTCSTLDMD QFMRKRIEAI RGQILSKLKL TSPPEDYPEP
EEVPPEVISI YNSTRDLLQE KASRRAAACE RERSDEEYYA KEVYKIDMPP FFPSENAIPP
TFYRPYFRIV RFDVSAMEKN ASNLVKAEFR VFRLQNPKAR VPEQRIELYQ ILKSKDLTSP
TQRYIDSKVV KTRAEGEWLS FDVTDAVHEW LHHKDRNLGF KISLHCPCCT FVPSNNYIIP
NKSEELEARF AGIDGTSTYT SGDQKTIKST RKKNSGKTPH LLLMLLPSYR LESQQSNRRK
KRALDAAYCF RNVQDNCCLR PLYIDFKRDL GWKWIHEPKG YNANFCAGAC PYLWSSDTQH
SRVLSLYNTI NPEASASPCC VSQDLEPLTI LYYIGKTPKI EQLSNMIVKS CKCS
