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Database: UniProt
Entry: A0A3B4ZKE8_9TELE
LinkDB: A0A3B4ZKE8_9TELE
Original site: A0A3B4ZKE8_9TELE 
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
//
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