ID A0A2I3H9F7_NOMLE Unreviewed; 1852 AA.
AC A0A2I3H9F7;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=TRPM7 {ECO:0000313|Ensembl:ENSNLEP00000040130.1};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000040130.1, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000040130.1, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000040130.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR629601-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR629601-3};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the protein kinase
CC superfamily. Alpha-type protein kinase family. ALPK subfamily.
CC {ECO:0000256|ARBA:ARBA00025760}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ADFV01034713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01034714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01034715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01034716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01034717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01034718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01034719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01034720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01034721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADFV01034722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSNLET00000036217.1; ENSNLEP00000040130.1; ENSNLEG00000006292.2.
DR GeneTree; ENSGT00940000157091; -.
DR Proteomes; UP000001073; Chromosome 6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR CDD; cd16971; Alpha_kinase_ChaK1_TRMP7; 1.
DR Gene3D; 3.20.200.10; MHCK/EF2 kinase; 1.
DR Gene3D; 1.20.5.1010; TRPM, tetramerisation domain; 1.
DR InterPro; IPR004166; a-kinase_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029601; TRPM7_a-kinase_dom.
DR InterPro; IPR041491; TRPM_SLOG.
DR InterPro; IPR032415; TRPM_tetra.
DR InterPro; IPR037162; TRPM_tetra_sf.
DR PANTHER; PTHR13800:SF8; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY M MEMBER 7; 1.
DR PANTHER; PTHR13800; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL, SUBFAMILY M, MEMBER 6; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF18139; LSDAT_euk; 1.
DR Pfam; PF16519; TRPM_tetra; 1.
DR SMART; SM00811; Alpha_kinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PIRSR:PIRSR629601-2};
KW Calcium {ECO:0000256|ARBA:ARBA00022568};
KW Calcium channel {ECO:0000256|ARBA:ARBA00022673};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00022568};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR629601-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR629601-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022568};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR629601-3}.
FT TRANSMEM 765..783
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 863..885
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 930..952
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 964..983
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1004..1023
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1085..1108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1581..1811
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 551..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1827..1852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1830..1852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1754
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-1"
FT BINDING 1611
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1635
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1707
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1740
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1756
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1764
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1781..1787
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1797
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1799
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1803
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
SQ SEQUENCE 1852 AA; 211462 MW; 9F6587B341B40113 CRC64;
MKLFSSYLSQ KSWIESTLTK RECVYIIPSS KDPHRCLPGC QICQQLVRCF CGRLVKQHAC
FTASLAMKYS DVKLGDHFNQ AIEEWSVEKH TEQSPTDAYG VINFQGGSHS YRAKYVRLSY
DTKPEVILQL LLKEWQMELP KLVISVHGGM QKFELHPRIK QLLGKGLIKA AVTTGAWILT
GGVNTGVAKH VGDALKEHAS RSSRKICTIG IAPWGVIENR NDLVGRDVVA PYQTLLNPLS
KLNVLNNLHS HFILVDDGTV GKYGAEVRLR RELEKTINQQ RIHARIGQGV PVVALIFEGG
PNVILTVLEY LQESPPVPVV VCEGTGRAAD LLAYVHKQTE EGGNLPDAAE PDIISTIKKT
FNFGQNEAVH LFQTLMECMK RKELITVFHI GSDEHQDIDV AILTALLKGT NASAFDQLIL
TLAWDRVDIA KNHVFVYGQQ WLVGSLEQAM LDALVMDRVA FVKLLIENGV SMHKFLTIPR
LEELYNTKQG PTNPMLFHLV RDVKQGNLPP GYKITLIDIG LVIEYLMGGT YRCTYTRKRF
RLIYNSLGGN NRRSGRNTSS STPQLRKSHE SFGNRADKKE KMRHNHFIKT AQPYRPKIDT
VMEEGKKKRT KDEIVDIDDP ETKRFPYPLN ELLIWACLMK RQVMARFLWQ HGEESMAKAL
VACKIYRSMA YEAKQSDLVD DTSEELKQYS NDFGQLAVEL LEQSFRQDET MAMKLLTYEL
KNWSNSTCLK LAVSSRLRPF VAHTCTQMLL SDMWMGRLNM RKNSWYKVIL SILVPPAILL
LEYKTKAEMS HIPQSQDAHQ MTMDDSENNF QNITEEIPME VFKEVRILDS NEGKNEMEIQ
IKSKKLPITR KFYAFYHAPI VKFWFNTLAY LGFLMLYTFV VLVQMEQLPS VQEWIVIAYI
FTYAIEKVRE IFMSEAGKVN QKIKVWFSDY FNISDTIAIV SFFVGFGLRF GAKWNFANAY
DNHVFVAGRL IYCLNIIFWY VRLLDFLAVN QQAGPYVMMI GKMVANMFYI VVIMALVLLS
FGVPRKAILY PHEAPSWTLA KDIVFHPYWM IFGEVYAYEI DVCANDSVIP QICGPGTWLT
PFLQAVYLFV QYIIMVNLLI AFFNNVYLQV KAISNIVWKY QRYHFIMAYH EKPVLPPPLI
ILSHIVSLFC CICKRRKKDK TSDGPKLFLT EEDQKKLHDF EEQCVEMYFN EKDDKFHSGS
EERIRVTFER VEQMCIQIKE VGDRVNYIKR SLQSLDSQIG HLQDLSALTV DTLKTLTAQK
ASEASKVHNE ITRELSISKH LAQNLIDDGP VRPSVWKKHS VVNTLSSSLP QGDLESNNPF
HCHILMKDDK DPQYNIFGQD LPAIPQRKEF NFPEAGSSSG ALFPSAVSPP ELRQRLHGIE
LLKIFNKNQK LGSSSTSIPH LSSPPTKFFV STPSQPSCKS HLETGTKDQE TVCSKATEGD
NIEFGAFVGH RDSMDLQRFK ETSNKIKEIL SNNNTSENTL KRVSSLAGFT DCHRTSIPLH
SKQAEKISRR PSTEDTHEVD SKAALIPYFE PLQISLFLSH FYAAVERNNL MRLSQSIPFT
PVPPRGEPVT VYRLEESSPN ILNNSMSSWS QLGLCAKIEF LSKEEMGGGL RRAVKVQCTW
SEHDILKSGH LYIIKSFLPE VVNTWSSIYK EDTVLHLCLR EIQQQRAAQK LTFAFNQMKP
KSIPYSPRFL EVFLLYCHSA GQWFAVEECM TGEFRKYNNN NGDEIIPTNT LEEIMLAFSH
WTYEYTRGEL LVLDLQGVGE NLTDPSVIKA EEKRSCDMVF GPANLGEDAI KNFRAKHHCN
SCCRKLKLPD LKRNDYTPDK IIFHQDEPSD LNLQPGNSTK ESESTNSVRL ML
//
