PGFRB_TAKRU
ID PGFRB_TAKRU Reviewed; 1048 AA.
AC P79749;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Platelet-derived growth factor receptor beta;
DE Short=PDGF-R-beta;
DE Short=PDGFR-beta;
DE EC=2.7.10.1;
DE AltName: Full=Beta platelet-derived growth factor receptor;
DE AltName: Full=Beta-type platelet-derived growth factor receptor;
DE Flags: Precursor;
GN Name=pdgfrb;
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8973913; DOI=10.1101/gr.6.12.1185;
RA How G.F., Venkatesh B., Brenner S.;
RT "Conserved linkage between the puffer fish (Fugu rubripes) and human genes
RT for platelet-derived growth factor receptor and macrophage colony-
RT stimulating factor receptor.";
RL Genome Res. 6:1185-1191(1996).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor
CC for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA
CC and PDGFB, and plays an essential role in the regulation of embryonic
CC development, cell proliferation, survival, differentiation, chemotaxis
CC and migration. Plays an essential role in blood vessel development by
CC promoting proliferation, migration and recruitment of pericytes and
CC smooth muscle cells to endothelial cells. Required for normal
CC development of the cardiovascular system. Required for normal
CC recruitment of pericytes (mesangial cells) in the kidney glomerulus,
CC and for normal formation of a branched network of capillaries in kidney
CC glomeruli. Promotes rearrangement of the actin cytoskeleton and the
CC formation of membrane ruffles. Binding of its cognate ligands
CC - homodimeric PDGFB, heterodimers formed by PDGFA and PDGFB or
CC homodimeric PDGFD -leads to the activation of several signaling
CC cascades; the response depends on the nature of the bound ligand and is
CC modulated by the formation of heterodimers between PDGFRA and PDGFRB.
CC Receptor signaling is down-regulated by protein phosphatases that
CC dephosphorylate the receptor and its down-stream effectors, and by
CC rapid internalization of the activated receptor (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
CC of bound ligand. Binding of PDGFB and/or PDGFD leads to dimerization
CC and activation by autophosphorylation on tyrosine residues (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with homodimeric PDGFB and PDGFD, and with
CC heterodimers formed by PDGFA and PDGFB. Monomer in the absence of bound
CC ligand. Interaction with homodimeric PDGFB, heterodimers formed by
CC PDGFA and PDGFB or homodimeric PDGFD, leads to receptor dimerization,
CC where both PDGFRA homodimers and heterodimers with PDGFRB are observed
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}.
CC Lysosome lumen {ECO:0000250}. Note=After ligand binding, the
CC autophosphorylated receptor is ubiquitinated and internalized, leading
CC to its degradation. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. After autophosphorylation, the receptor is
CC polyubiquitinated, leading to its degradation (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Autophosphorylated on tyrosine residues upon ligand binding.
CC Autophosphorylation occurs in trans, i.e. one subunit of the dimeric
CC receptor phosphorylates tyrosine residues on the other subunit (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. CSF-1/PDGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; U63926; AAC60062.1; -; Genomic_DNA.
DR PIR; T30815; T30815.
DR AlphaFoldDB; P79749; -.
DR SMR; P79749; -.
DR STRING; 31033.ENSTRUP00000018654; -.
DR eggNOG; KOG0200; Eukaryota.
DR InParanoid; P79749; -.
DR Proteomes; UP000005226; Unplaced.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043202; C:lysosomal lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005019; F:platelet-derived growth factor beta-receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027288; PGFRB.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF500948; Beta-PDGF_receptor; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Chemotaxis; Cytoplasmic vesicle;
KW Developmental protein; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Kinase; Lysosome; Membrane; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..1048
FT /note="Platelet-derived growth factor receptor beta"
FT /id="PRO_0000248882"
FT TOPO_DOM 31..528
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..1048
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..124
FT /note="Ig-like C2-type 1"
FT DOMAIN 216..309
FT /note="Ig-like C2-type 2"
FT DOMAIN 319..406
FT /note="Ig-like C2-type 3"
FT DOMAIN 596..957
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 821
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 602..610
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 630
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 558
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 575
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 577
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 735
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 746
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 758
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 766
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 770
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 852
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 1036
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 153..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 240..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 434..503
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1048 AA; 117868 MW; 7363EFD38D9B913C CRC64;
MLRASAMRAA VLHLTVALAA LLSSCTTVSC LKIVPEEKQL ILAEGSSLSL TCAGSSETTW
DLKSDDVPFF QMKAESSDLN YKIVQSNSTA SVLTLWHVDW KNTAVYQCRE QLTGEIKEVA
VFVPDRFSPQ TLRFIESSHG MVTKTSGEST VPCVVTNPNI TVTLYDKDTD LPVNGVYVPS
EGFKAYLDYR TYVCRGELNG EVKESQAFNV YSIHVPEDID AYVNASQTVL KQGEPLTVNC
TVQGVELVLF SWDIPNRDIV KHKPETVVLS ATTMRSCLVF PHATVAHSGT YVCHAHESTQ
DQKAFASVNI TVLERGFVAV KSTRKQNITA ELQENVELRV EIEAYPPPQI RWKKDGAPVR
GDKTIIIRQE HEIRYVTILT LVRVRTEQKG LYTALITNED DVKEVTFALE VQVLARIKDL
TDHHLPGKKQ LVTCVAEGVP TPTIQWYSCD SMLKCNNQTS LWQQLKADPE LLSIHTSVTE
ARQTNQVRSQ VTFFKPQHTT VRCETTNQEG LIDFRDVKLV SSSLFSQVVL LAVVLTLVPI
IIMSIIILIA VWKKKPRYEI RWKVIESVSQ DGHEYIYVDP IHLPYDLAWE MPRDNLVLGR
TLGSGAFGRV VEATAHGLSH SQSSIKVAVK MLKATARRSE TQALMSELKI MSHLGPHLNI
VNLLAACTKH GPLYLVTEYC RYGDLVDYLH RNKHTFLQYY LDKNQDDGSL ISGGSTPLSQ
RKGYVSFGSE SDGGYMDMSK DEPAVYVPMQ EQMDTIKYAD IQPSPYESPY QQDLYQEQGG
GRVDLVISDS PALTYDDLLG FSYQVAKGME FLASKNCVHR DLAARNVLIC EGKLVKICDF
GLARDIMHDS NYISKGSTFL PLKWMAPESI FHNLYTTLSD VWSYGILLWE IFTLGGTPYP
DLPMNELFYS PLKRGYRMAK PAHASDEVYE IMKRCWDETF EKRPDFSFLV HCVGDMLTDS
YKKKYSQVNE TFLKSDHPAV ARTKPRLSSP FPIANPAFGS PSLVGLSDFP DPYNQNTRRF
RNEAEVQEGV TSFNEYIIPI PDPKPEKS
