TGFB2_XENLA
ID TGFB2_XENLA Reviewed; 413 AA.
AC P17247;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2336403; DOI=10.1093/nar/18.8.2185;
RA Rebbert M.L., Bhatia-Dey N., Dawid I.B.;
RT "The sequence of TGF-beta 2 from Xenopus laevis.";
RL Nucleic Acids Res. 18:2185-2185(1990).
RN [2]
RP PROTEIN SEQUENCE OF 302-319.
RX PubMed=2340184; DOI=10.3109/08977199009071500;
RA Roberts A.B., Rosa F., Roche N.S., Coligan J.E., Garfield M., Rebbert M.L.,
RA Kondaiah P., Danielpour D., Kehrl J.H., Wahl S.M., Dawid I.B., Sporn M.B.;
RT "Isolation and characterization of TGF-beta 2 and TGF-beta 5 from medium
RT conditioned by Xenopus XTC cells.";
RL Growth Factors 2:135-147(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA36117.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X51817; CAA36116.1; -; mRNA.
DR EMBL; X51817; CAA36117.1; ALT_INIT; mRNA.
DR PIR; S09510; WFXLB2.
DR RefSeq; NP_001079195.1; NM_001085726.1.
DR AlphaFoldDB; P17247; -.
DR SMR; P17247; -.
DR GeneID; 373801; -.
DR KEGG; xla:373801; -.
DR CTD; 373801; -.
DR Xenbase; XB-GENE-865387; tgfb2.L.
DR OMA; IDSKVIR; -.
DR OrthoDB; 643840at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 373801; Expressed in internal ear and 13 other tissues.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005160; F:transforming growth factor beta receptor binding; IEA:InterPro.
DR GO; GO:0009790; P:embryo development; IEA:UniProt.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0009888; P:tissue development; IEA:UniProt.
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 1: Evidence at protein level;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Growth factor; Mitogen;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..413
FT /note="Transforming growth factor beta-2 proprotein"
FT /id="PRO_0000456186"
FT CHAIN 20..301
FT /note="Latency-associated peptide"
FT /evidence="ECO:0000305|PubMed:2340184"
FT /id="PRO_0000445554"
FT CHAIN 302..413
FT /note="Transforming growth factor beta-2"
FT /evidence="ECO:0000305|PubMed:2340184"
FT /id="PRO_0000033795"
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 308..317
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 316..379
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 345..410
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 349..412
FT /evidence="ECO:0000250|UniProtKB:P61812"
FT DISULFID 378
FT /note="Interchain"
FT /evidence="ECO:0000250|UniProtKB:P61812"
SQ SEQUENCE 413 AA; 47639 MW; 6127715B38734010 CRC64;
MHYYVLFTFL TLDLAPVALS LSTCSALDMD QFMRKRIEAI RGQILSKLKL NSPPEDYPEP
GEVSQDVISI YNSTRDLLQE KANERATSCE RERSEDEYYA KEVYKIDMLP YYTSENVIPP
SYTTPYFRIV RFDVSSMEKN ASNLVKAEFR VFRLMNTKAR VSEQRIELYQ ILKSKDLASP
TQRYIDSKVV KTRAEGEWLS FDVTEAVNEW LHHKDRNLGF KISLHCPCCT FIPSNNYIIP
NKSEELETRF AGIDDAYMYA GGDSKSKTGR KKHTGRTPHL LLMLLPSYRL ESQQSSRRKK
RALDAAYCFR NVQDNCCLRP LYIDFKKDLG WKWIHEPKGY NANFCAGACP YLWSSDTQHS
RVLSLYNTIN PEASASPCCV SQDLDSLTIL YYIGNKPKIE QLSNMIVKSC KCS
