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Database: UniProt
Entry: G3NI08_GASAC
LinkDB: G3NI08_GASAC
Original site: G3NI08_GASAC 
ID   G3NI08_GASAC            Unreviewed;       526 AA.
AC   G3NI08;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271};
DE            EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000004968.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000004968.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000004968.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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|RuleBase:RU361271};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU361271};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU361271};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
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|RuleBase:RU361271}.
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DR   AlphaFoldDB; G3NI08; -.
DR   Ensembl; ENSGACT00000004982.1; ENSGACP00000004968.1; ENSGACG00000003781.1.
DR   GeneTree; ENSGT00940000157527; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000003781; Expressed in muscle tissue and 10 other cell types or tissues.
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:InterPro.
DR   GO; GO:0006915; P:apoptotic process; 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:SF55; 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|ARBA:ARBA00022703};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR037393-
KW   2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR037393-3};
KW   Growth regulation {ECO:0000256|ARBA:ARBA00022604};
KW   Kinase {ECO:0000256|RuleBase:RU361271};
KW   Magnesium {ECO:0000256|RuleBase:RU361271};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU361271};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361271};
KW   Metal-binding {ECO:0000256|RuleBase:RU361271};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRSR:PIRSR037393-2};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU361271};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU361271}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|RuleBase:RU361271};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU361271};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU361271}.
FT   TRANSMEM        120..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU361271"
FT   DOMAIN          204..499
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        337
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037393-1"
FT   BINDING         210..218
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037393-2"
FT   BINDING         237
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037393-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   DISULFID        5..38
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT   DISULFID        8..25
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT   DISULFID        15..21
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT   DISULFID        31..55
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT   DISULFID        75..90
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
FT   DISULFID        92..98
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037393-3"
SQ   SEQUENCE   526 AA;  59421 MW;  2696EFF1A674D268 CRC64;
     MNQLCKFCDV ELTSCSGTGT CVSNCSITSI CTDRVEVCVS IWRKNETDLS LETLCHNPSK
     PLYGVMLDDY NSSTCVMKKK NTTSGMAEIC SCRDVEECND KVLFIPVGPQ KIVDPTPDDA
     LLSVILVSLL PLLTMGVVVA GMFYWYRAYR QRVSQEWERS AKKRKTKAGG LDCDACAIMM
     DDDGSDSSST HANHLNHNTE PLPIELDMLV GKGRFAQVYK AKLKQTTSDQ FETVAVKIFP
     YEEYASWKNE KDIFSYMDLR HENIVHFLTA EERKVEKQYW LITAFHPRGN LQEHLTRHVI
     SWEELQVLGL SLARGVAHLH SDRLLCGRPK VPIVHRDLKS SNILVKNDLT LCLCDFGLGL
     RLDSTLSVDD LANSGQVGTA RYMAPEVLEA RLNLENMESF KQTDIYSMAL VLWEMTSRCE
     AVGEVKEYEP AYGSKVREHP CVESMKDSVL RDRGRPEIPD TWLRHKGLAQ ICGTIMECWD
     HDPEARLTAL CVAERILELE DEMDKLSSRS SSAEKIPAEL KIPMEV
//
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