TGFBR3

TGFBR3
Identifikatori
Aliasi	TGFBR3
Vanjski ID-jevi	OMIM: 600742 MGI: 104637 HomoloGene: 2436 GeneCards: TGFBR3
Lokacija gena (čovjek)
Hrom.	Hromosom 1 (čovjek)
Kraj	91,906,335 bp
Lokacija gena (miš)
Hrom.	Hromosom 5 (miš)
Kraj	107,437,495 bp
Obrazac RNK ekspresije
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• transforming growth factor beta receptor binding; • heparin binding; • activin binding; • transforming growth factor beta receptor activity, type III; • transforming growth factor beta-activated receptor activity; • SMAD binding; • PDZ domain binding; • coreceptor activity; • fibroblast growth factor binding; • type II transforming growth factor beta receptor binding; • GO:0001948, GO:0016582 vezivanje za proteine; • glycosaminoglycan binding; • transforming growth factor beta binding;
Ćelijska komponenta	• Egzosom; • extracellular region; • citoplazma; • integral component of membrane; • inhibin-betaglycan-ActRII complex; • integral component of plasma membrane; • membrana; • cell surface; • receptor complex; • ćelijska membrana; • external side of plasma membrane; • Vanćelijsko; • GO:0005578 Vanćelijski matriks;
Biološki proces	• response to hypoxia; • heart trabecula formation; • GO:0007243 intracellular signal transduction; • liver development; • animal organ regeneration; • definitive erythrocyte differentiation; • BMP signaling pathway; • positive regulation of transforming growth factor beta receptor signaling pathway; • regulation of protein binding; • heart morphogenesis; • transforming growth factor beta receptor complex assembly; • cardiac epithelial to mesenchymal transition; • pathway-restricted SMAD protein phosphorylation; • response to follicle-stimulating hormone; • ventricular cardiac muscle tissue morphogenesis; • roof of mouth development; • cardiac muscle cell proliferation; • response to prostaglandin E; • negative regulation of transforming growth factor beta receptor signaling pathway; • negative regulation of epithelial cell proliferation; • Ćelijska migracija; • definitive hemopoiesis; • epithelial to mesenchymal transition; • response to luteinizing hormone; • GO:0046730, GO:0046737, GO:0046738, GO:0046736 Imuni odgovor; • transforming growth factor beta receptor signaling pathway; • epicardium-derived cardiac fibroblast cell development; • ventricular septum morphogenesis; • regulation of ERK1 and ERK2 cascade; • ventricular compact myocardium morphogenesis; • heart trabecula morphogenesis; • positive regulation of cardiac muscle cell proliferation; • regulation of JNK cascade; • muscular septum morphogenesis; • vasculogenesis involved in coronary vascular morphogenesis; • outflow tract morphogenesis; • secondary palate development; • GO:0034622 protein-containing complex assembly;
	Izvori:Amigo / QuickGO
Ortolozi
	7049
	21814
	ENSG00000069702
	ENSMUSG00000029287
	Q03167
	O88393
	NM_001195683; NM_001195684; NM_003243
	NM_011578
	NP_001182612; NP_001182613; NP_003234
	NP_035708
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Betaglikan, znan i kao receptor III transformirajućeg faktora rasta, jest površinskoćelijski hondroitin-sulfatni/heparan-sulfateni proteoglikan. To je protein koji je kod ljudi kodiran genom TGFBR3 sa hromosoma 1.

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 851 aminokiselina, a molekulska težina 93.499 Da.^[5]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MTSHYVIAIF	ALMSSCLATA	GPEPGALCEL	SPVSASHPVQ	ALMESFTVLS
GCASRGTTGL	PQEVHVLNLR	TAGQGPGQLQ	REVTLHLNPI	SSVHIHHKSV
VFLLNSPHPL	VWHLKTERLA	TGVSRLFLVS	EGSVVQFSSA	NFSLTAETEE
RNFPHGNEHL	LNWARKEYGA	VTSFTELKIA	RNIYIKVGED	QVFPPKCNIG
KNFLSLNYLA	EYLQPKAAEG	CVMSSQPQNE	EVHIIELITP	NSNPYSAFQV
DITIDIRPSQ	EDLEVVKNLI	LILKCKKSVN	WVIKSFDVKG	SLKIIAPNSI
GFGKESERSM	TMTKSIRDDI	PSTQGNLVKW	ALDNGYSPIT	SYTMAPVANR
FHLRLENNAE	EMGDEEVHTI	PPELRILLDP	GALPALQNPP	IRGGEGQNGG
LPFPFPDISR	RVWNEEGEDG	LPRPKDPVIP	SIQLFPGLRE	PEEVQGSVDI
ALSVKCDNEK	MIVAVEKDSF	QASGYSGMDV	TLLDPTCKAK	MNGTHFVLES
PLNGCGTRPR	WSALDGVVYY	NSIVIQVPAL	GDSSGWPDGY	EDLESGDNGF
PGDMDEGDAS	LFTRPEIVVF	NCSLQQVRNP	SSFQEQPHGN	ITFNMELYNT
DLFLVPSQGV	FSVPENGHVY	VEVSVTKAEQ	ELGFAIQTCF	ISPYSNPDRM
SHYTIIENIC	PKDESVKFYS	PKRVHFPIPQ	ADMDKKRFSF	VFKPVFNTSL
LFLQCELTLC	TKMEKHPQKL	PKCVPPDEAC	TSLDASIIWA	MMQNKKTFTK
PLAVIHHEAE	SKEKGPSMKE	PNPISPPIFH	GLDTLTVMGI	AFAAFVIGAL
LTGALWYIYS	HTGETAGRQQ	VPTSPPASEN	SSAAHSIGST	QSTPCSSSST
A

Funkcija

Betaglikan se vezuje za različite članove natporodice TGF-beta liganda preko svog jezgarnog proteina i bFGF preko svojih heparan-sulfatnih lanaca. Nije uključen direktno u TGF-beta transdukciju signala, ali vezivanjem za različite članove natporodice TGF-beta na površini ćelije djeluje kao rezervoar liganda za receptore TGF-beta.^[6]^[7]

Također pogledajte

TGF-beta receptori

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000069702 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000029287 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "UniProt, Q03167" (jezik: en.). Pristupljeno 5. 12. 2021.CS1 održavanje: nepoznati jezik (link)
^ Andres JL, Stanley K, et al. (1989). "Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-beta". J. Cell Biol. 109 (6 (Pt 1)): 3137–3145. doi:10.1083/jcb.109.6.3137. PMC 2115961. PMID 2592419.
^ Andres JL, DeFalcis D, et al. (1992). "Binding of two growth factor families to separate domains of the proteoglycan betaglycan". J. Biol. Chem. 267 (9): 5927–5930. doi:10.1016/S0021-9258(18)42643-9. PMID 1556106.

Dopunska literatura

Massagué J (1992). "Receptors for the TGF-beta family". Cell. 69 (7): 1067–70. doi:10.1016/0092-8674(92)90627-O. PMID 1319842. S2CID 54268875.
Border WA, Noble NA (1994). "Transforming growth factor beta in tissue fibrosis". N. Engl. J. Med. 331 (19): 1286–92. doi:10.1056/NEJM199411103311907. PMID 7935686.
Morén A, Ichijo H, Miyazono K (1992). "Molecular cloning and characterization of the human and porcine transforming growth factor-beta type III receptors". Biochem. Biophys. Res. Commun. 189 (1): 356–62. doi:10.1016/0006-291X(92)91566-9. PMID 1333192.
López-Casillas F, Cheifetz S, Doody J, et al. (1991). "Structure and expression of the membrane proteoglycan betaglycan, a component of the TGF-beta receptor system". Cell. 67 (4): 785–95. doi:10.1016/0092-8674(91)90073-8. PMID 1657406. S2CID 54304782.
Wang XF, Lin HY, Ng-Eaton E, et al. (1991). "Expression cloning and characterization of the TGF-beta type III receptor". Cell. 67 (4): 797–805. doi:10.1016/0092-8674(91)90074-9. PMID 1657407. S2CID 54258148.
Lin HY, Moustakas A, Knaus P, et al. (1995). "The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands". J. Biol. Chem. 270 (6): 2747–54. doi:10.1074/jbc.270.6.2747. PMID 7852346.
López-Casillas F, Payne HM, Andres JL, Massagué J (1994). "Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: mapping of ligand binding and GAG attachment sites". J. Cell Biol. 124 (4): 557–68. doi:10.1083/jcb.124.4.557. PMC 2119924. PMID 8106553.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Johnson DW, Qumsiyeh M, Benkhalifa M, Marchuk DA (1996). "Assignment of human transforming growth factor-beta type I and type III receptor genes (TGFBR1 and TGFBR3) to 9q33-q34 and 1p32-p33, respectively". Genomics. 28 (2): 356–7. doi:10.1006/geno.1995.1157. PMID 8530052.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Brown CB, Boyer AS, Runyan RB, Barnett JV (1999). "Requirement of type III TGF-beta receptor for endocardial cell transformation in the heart". Science. 283 (5410): 2080–2. doi:10.1126/science.283.5410.2080. PMID 10092230.
Gao J, Symons AL, Bartold PM (1999). "Expression of transforming growth factor-beta receptors types II and III within various cells in the rat periodontium". Journal of Periodontal Research. 34 (2): 113–22. doi:10.1111/j.1600-0765.1999.tb02230.x. PMID 10207840.
Lewis KA, Gray PC, Blount AL, et al. (2000). "Betaglycan binds inhibin and can mediate functional antagonism of activin signalling". Nature. 404 (6776): 411–4. Bibcode:2000Natur.404..411L. doi:10.1038/35006129. PMID 10746731. S2CID 4393629.
Zippert R, Bässler A, Holmer SR, et al. (2000). "Eleven single nucleotide polymorphisms and one triple nucleotide insertion of the human TGF-beta III receptor gene". J. Hum. Genet. 45 (4): 250–3. doi:10.1007/s100380070035. PMID 10944857.
Rotzer D, Roth M, Lutz M, et al. (2001). "Type III TGF-β receptor-independent signalling of TGF-β2 via TβRII-B, an alternatively spliced TGF-β type II receptor". EMBO J. 20 (3): 480–90. doi:10.1093/emboj/20.3.480. PMC 133482. PMID 11157754.
Blobe GC, Schiemann WP, Pepin MC, et al. (2001). "Functional roles for the cytoplasmic domain of the type III transforming growth factor beta receptor in regulating transforming growth factor beta signaling". J. Biol. Chem. 276 (27): 24627–37. doi:10.1074/jbc.M100188200. PMID 11323414.
De Crescenzo G, Grothe S, Zwaagstra J, et al. (2001). "Real-time monitoring of the interactions of transforming growth factor-beta (TGF-beta ) isoforms with latency-associated protein and the ectodomains of the TGF-beta type II and III receptors reveals different kinetic models and stoichiometries of binding". J. Biol. Chem. 276 (32): 29632–43. doi:10.1074/jbc.M009765200. PMID 11382746.
Blobe GC, Liu X, Fang SJ, et al. (2001). "A novel mechanism for regulating transforming growth factor beta (TGF-beta) signaling. Functional modulation of type III TGF-beta receptor expression through interaction with the PDZ domain protein, GIPC". J. Biol. Chem. 276 (43): 39608–17. doi:10.1074/jbc.M106831200. PMID 11546783.

Vanjski linkovi

betaglycan na US National Library of Medicine Medical Subject Headings (MeSH)

Šablon:Natporodica TGFβ receptorskih modulatora

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000069702 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000029287 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[UniProt-5] "UniProt, Q03167" (jezik: en.). Pristupljeno 5. 12. 2021.CS1 održavanje: nepoznati jezik (link)

[6] Andres JL, Stanley K, et al. (1989). "Membrane-anchored and soluble forms of betaglycan, a polymorphic proteoglycan that binds transforming growth factor-beta". J. Cell Biol. 109 (6 (Pt 1)): 3137–3145. doi:10.1083/jcb.109.6.3137. PMC 2115961. PMID 2592419.

[7] Andres JL, DeFalcis D, et al. (1992). "Binding of two growth factor families to separate domains of the proteoglycan betaglycan". J. Biol. Chem. 267 (9): 5927–5930. doi:10.1016/S0021-9258(18)42643-9. PMID 1556106.

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