ID A0A091CLT7_FUKDA Unreviewed; 1023 AA.
AC A0A091CLT7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Serine/threonine-protein kinase receptor {ECO:0000256|RuleBase:RU361271};
DE EC=2.7.11.30 {ECO:0000256|RuleBase:RU361271};
GN ORFNames=H920_20295 {ECO:0000313|EMBL:KFO18358.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO18358.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO18358.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO18358.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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: Membrane {ECO:0000256|RuleBase:RU361271}; Single-
CC pass type I membrane protein {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 EMBL; KN125438; KFO18358.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091CLT7; -.
DR STRING; 885580.ENSFDAP00000021375; -.
DR eggNOG; KOG3653; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14054; STKc_BMPR2_AMHR2; 1.
DR Gene3D; 2.10.60.10; CD59; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000472; Activin_recp.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255:SF63; BONE MORPHOGENETIC PROTEIN RECEPTOR TYPE-2; 1.
DR PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR Pfam; PF01064; Activin_recp; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00653; ACTIVIN2R.
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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000256|RuleBase:RU361271};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU361271};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU361271};
KW Membrane {ECO:0000256|RuleBase:RU361271};
KW Metal-binding {ECO:0000256|RuleBase:RU361271};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Receptor {ECO:0000256|RuleBase:RU361271, ECO:0000313|EMBL:KFO18358.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
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|RuleBase:RU361271};
KW Transmembrane helix {ECO:0000256|RuleBase:RU361271}.
FT TRANSMEM 138..162
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361271"
FT DOMAIN 190..491
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 579..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..883
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1023 AA; 113293 MW; B0522D830732199F CRC64;
MLLLNYLYNL SNPSFHLMAP RSSFVQSSTS TPGSQNQERL CAFKDPYQQD LGIGESRISH
ENGTILCSKG CWSHIGDPQE CHYEECVVTT TPSSIQNGTY RFCCCSADLC NVNFTENFPP
PDTTPLSPPQ SFNRDETIII ALASVSVLAV LIVALCFGYR MVAGDHKQGL HSINMMEAAA
SEPSLDLDNL KLLELIGRGR YGAVYKGSLD ERPVAVKVFS FANRQNFINE KNIYRVPLME
HDNIARFIVG DERVTADGRM EYLLVMEYYP NGSLCKYLSL HTSEWVGSCR LAHSVTRGLA
YLHTELPRGD HYKPAISHRD LNSRNVLVKN DGTCVISDFG LSMRLTGNRL VRPGEEDNAA
ISEVGTIRYM APEVLEGAVN LRDCESALKQ VDMYALGLIY WEIFMRCTDL FPGESVPEYQ
MAFQTEVGNH PTFEDMQVLV SREKQRPKFP EAWKENSLAV RSLKETIEDC WDQDAEARLT
AQCAEERMAE LMMIWERNKS VSPTVNPMST AMQNERNLSH NRRVPKIGPY PDYSSSSYIE
DSIHHTDSIV KNISSEHSMS STPLTTGEKN RNSINYERQQ AQARIPSPET SVTSLSTNTT
TTNTTGLTPS TGMTTISELP YPDETNLHAT NVAQSIGPTP VCLQLTEEDL ETNKLDPKEV
DKNLKESSDE NLMEHSLKQF SGPDPLSSTS SSLLYPLIKL AVEVTGQQDF TQATNGQACL
IPDVPPTQIY PLPKQQNLPK RPTSLPLNTK NSTKEPRLKF GSKHKSNLKQ VETGVAKMNT
INTVEPHVVT VTMNGVAGRN HSVNSHAATQ YANGVVPSGQ TANIVAHRAQ EMLQNEFIGE
DTRLNINSSP DEHEPLLRRE QQAGHDEGVL DRLVDRRERP LEGGRTNSNN NNSNPGSEQD
VLTQSISSTV ADPGPSKPRR AQRPNSLDLS ATNVLDGCSI QSESTQDGKS GSGEKIKKRV
KTPYSLKRWR PSTWVISTEP LDCEVNNNGS DQAVPSKSST AVYLAEGGTA TTMVSKDIGM
NCL
//
