ID A0A3B4ZKE8_9TELE Unreviewed; 587 AA.
AC A0A3B4ZKE8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=TGF-beta receptor type-2 {ECO:0000256|PIRNR:PIRNR037393};
DE Short=TGFR-2 {ECO:0000256|PIRNR:PIRNR037393};
DE EC=2.7.11.30 {ECO:0000256|PIRNR:PIRNR037393};
DE AltName: Full=TGF-beta type II receptor {ECO:0000256|PIRNR:PIRNR037393};
DE AltName: Full=Transforming growth factor-beta receptor type II {ECO:0000256|PIRNR:PIRNR037393};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000008805.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000008805.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Transmembrane serine/threonine kinase forming with the TGF-
CC beta type I serine/threonine kinase receptor, TGFBR1, the non-
CC promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3.
CC Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to
CC the cytoplasm and is thus regulating a plethora of physiological and
CC pathological processes including cell cycle arrest in epithelial and
CC hematopoietic cells, control of mesenchymal cell proliferation and
CC differentiation, wound healing, extracellular matrix production,
CC immunosuppression and carcinogenesis. The formation of the receptor
CC complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound
CC to the cytokine dimer results in the phosphorylation and the activation
CC of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1
CC phosphorylates SMAD2 which dissociates from the receptor and interacts
CC with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the
CC nucleus where it modulates the transcription of the TGF-beta-regulated
CC genes. This constitutes the canonical SMAD-dependent TGF-beta signaling
CC cascade. Also involved in non-canonical, SMAD-independent TGF-beta
CC signaling pathways. {ECO:0000256|PIRNR:PIRNR037393}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC Evidence={ECO:0000256|PIRNR:PIRNR037393,
CC ECO:0000256|RuleBase:RU361271};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRNR:PIRNR037393,
CC ECO:0000256|RuleBase:RU361271};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRNR:PIRNR037393,
CC ECO:0000256|RuleBase:RU361271};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR037393}.
CC Membrane raft {ECO:0000256|ARBA:ARBA00004285}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479,
CC ECO:0000256|RuleBase:RU361271}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily.
CC {ECO:0000256|ARBA:ARBA00009605, ECO:0000256|PIRNR:PIRNR037393,
CC ECO:0000256|RuleBase:RU361271}.
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DR AlphaFoldDB; A0A3B4ZKE8; -.
DR STRING; 144197.ENSSPAP00000008805; -.
DR Ensembl; ENSSPAT00000008965.1; ENSSPAP00000008805.1; ENSSPAG00000006712.1.
DR GeneTree; ENSGT00940000164835; -.
DR Proteomes; UP000261400; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005026; F:transforming growth factor beta receptor activity, type II; IEA:UniProtKB-UniRule.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14055; STKc_TGFbR2_like; 1.
DR Gene3D; 2.10.60.10; CD59; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR InterPro; IPR017194; Transform_growth_fac-b_typ-2.
DR InterPro; IPR015013; Transforming_GF_b_rcpt_2_ecto.
DR PANTHER; PTHR23255:SF51; TGF-BETA RECEPTOR TYPE-2; 1.
DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR Pfam; PF08917; ecTbetaR2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF037393; TGFRII; 1.
DR PRINTS; PR00653; ACTIVIN2R.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57302; Snake toxin-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Apoptosis {ECO:0000256|PIRNR:PIRNR037393};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR037393};
KW Cell membrane {ECO:0000256|PIRNR:PIRNR037393};
KW Differentiation {ECO:0000256|PIRNR:PIRNR037393};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR037393-3};
KW Growth regulation {ECO:0000256|PIRNR:PIRNR037393};
KW Kinase {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271};
KW Magnesium {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271};
KW Manganese {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271};
KW Membrane {ECO:0000256|PIRNR:PIRNR037393};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR037393,
KW ECO:0000256|RuleBase:RU361271};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR037393};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|PIRNR:PIRNR037393};
KW Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR037393,
KW ECO:0000256|RuleBase:RU361271}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transferase {ECO:0000256|PIRNR:PIRNR037393, ECO:0000256|RuleBase:RU361271}.
FT DOMAIN 247..549
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 207..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..587
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 387
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-1"
FT BINDING 253..261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-2"
FT BINDING 283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
FT DISULFID 32..64
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT DISULFID 35..51
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT DISULFID 42..47
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT DISULFID 57..81
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT DISULFID 104..119
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT DISULFID 121..127
FT /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
SQ SEQUENCE 587 AA; 65495 MW; 71A6F95704D1E5A5 CRC64;
SWTCWSTLLM SIMFICLPVL VQSLSHLSYN FCKWCEDSSP VCEDSVCLTN CSLSSFCNSI
EEICVAVWRK TNDTMTVDTM CHHPALPLEG VDPGLLLNFT TRECHMVKQP AEEGAMMVCG
CHGEHECNDK LIFDKGANGF SRLHSKDVIP VVVVSLVPPV MVALIAIAAF YFYRIRRPDK
PSPPARPDWP TKRTPELYQA LDLPCQGARR EGGDVTGAER DESNAKVPSP HSDTIGSMTN
WQSHLPIKLE VLVGKGRFAE VWRACLLGTE RGGVSSCQTM AVKVFPAVEY ASWRNECAIF
SDPELQHDNV VQFLAAEEKG PPSHALRSYW LVLAYHSLGN LQEFLTANIL SWEELVAMAG
SIAKGLAHLH SDTTPRGASK VPVAHRDLKS SNIVVKSRNE CALCDFGLAL RLDISLTVDD
YANSGQVGTA RYMAPEVLES RVNLEDLEAF KQMDVYSMAL VLWEMASRCH AIGEVKSYEP
AFGSKVCEQP CVDSMRDLVL RDRGRPDIPS TWTQHQGMNV FCSTITECWD HDPEARLTAH
CVVERFNALQ EAEAEEEEEE EEEAQEEEAR EEVEGEEEEE EEAGRQE
//