ID F6S796_ORNAN Unreviewed; 2043 AA.
AC F6S796;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 63.
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=TRPM6 {ECO:0000313|Ensembl:ENSOANP00000018460.3};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000018460.3, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000018460.3, ECO:0000313|Proteomes:UP000002279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000018460.3,
RC ECO:0000313|Proteomes:UP000002279};
RX PubMed=18464734; DOI=10.1038/nature06936;
RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT "Genome analysis of the platypus reveals unique signatures of evolution.";
RL Nature 453:175-183(2008).
RN [2] {ECO:0000313|Ensembl:ENSOANP00000018460.3}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000018460.3};
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 -!- 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}.
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DR STRING; 9258.ENSOANP00000018460; -.
DR Ensembl; ENSOANT00000018463.4; ENSOANP00000018460.3; ENSOANG00000011650.4.
DR eggNOG; KOG3614; Eukaryota.
DR GeneTree; ENSGT00940000158164; -.
DR HOGENOM; CLU_001390_2_0_1; -.
DR TreeFam; TF314204; -.
DR Proteomes; UP000002279; Chromosome X5.
DR Bgee; ENSOANG00000011650; Expressed in adult mammalian kidney and 7 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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; cd16972; Alpha_kinase_ChaK2_TRPM6; 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; IPR029597; TRPM6_a-kinase_dom.
DR InterPro; IPR041491; TRPM_SLOG.
DR InterPro; IPR032415; TRPM_tetra.
DR InterPro; IPR037162; TRPM_tetra_sf.
DR PANTHER; PTHR13800:SF15; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY M MEMBER 6; 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 Calcium {ECO:0000256|ARBA:ARBA00022568};
KW Calcium channel {ECO:0000256|ARBA:ARBA00022673};
KW Calcium transport {ECO:0000256|ARBA:ARBA00022568};
KW Coiled coil {ECO:0000256|SAM:Coils};
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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
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}.
FT TRANSMEM 756..773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 855..875
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 922..940
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 952..971
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 991..1011
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1064..1087
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1773..2003
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 802..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1591..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2014..2043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 664..691
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 810..825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2043 AA; 234158 MW; EEFC27224016A24A CRC64;
MRRSQKSWIE GVFDKRECTK VIPSSKDPHR CTAGCQVCQN LIRCYCGRLI GDHYGMDYSW
SAVSLAAKGQ REEEEEWSVE KHTKKSPTDS FGTINFQDGD HSYHAKYIRT SYDTKLDQLS
HLMLKEWKME LPKLVISVHG GIQNFKMSSK FKKIFSNGLL KAAETTGAWI ITEGINTGVS
KHVGDALKTF SSPCLRKIWA VGIPPWGVIE NRRDLVGKDV VCLYQTLGNP LSKLTTLNSM
HSHFILSDDG TVGKYGNEMK LRRNLERYLS LQKIHTRMGQ GVPVVGLVVE GGPNVILMVW
EYVRDQSPVP VVVCEGTGRA ADLLAFTHKH TADEGQLRPQ VKEEIIHMIQ NTFNFSPNQS
NHLFQILMEC MEHRESITIF DADSEEHQDL DLAILTALLK GTSLSASDQL SLALAWNRVD
IAKKHILVYG QHWKVGSLEQ SMLDALVMDR VDFVKLLIEH GVNLHRFLTI SRLEELYNIK
QGPTNLLLHH LVRDVKQSTL PLDYKISLID IGLVIEYLIG GAYRSSYTRK HFRVLYNSLY
RKHKRVSSFT RNFSHPSLHL NVHSGSRNGS AESTLHSQFI RTAQPYKSKE KLVTLHKSRK
KLKEEPSFPE EPECAGFIYP YNDLLVWAVL MKRQKMAMFF WQHGEEAMVK AVIACKLYRA
MAREAKESNM VDDASEELKN YSKEFGQLAL DVLEKAFKQN EQMAMKLLTY ELKNWSNSTC
LKLAVSVGLR PFVSHTCTQM LLTDMWMGRL KMRKNSWLKV IISILIPPTI LMLEFKSKAE
MSHIPQPQDF HQFTWYYGEP SPSSTKESLS PKDYDMEKGQ EKPDESHTFA PSTGPQSLPG
TRKVYEFYNA PLVKFWFYTM AYLAFLMLFT FTVLVEMQPL PTVQEWLVII YIFTTAIEKV
REIFISEPGK FSQKVKVWIH EYWNLTDTIA IILFTIGFSL RWSDPPVQTA GRLIYCIDII
FWYSRLLDFL AVNQHAGPYL TMIGKMTANM FYIVIMMAIV LLSFGVARKA ILSPKEHPSW
SLARDIVFEP YWMMFGEVYA GEIDACSNRE NCPPGSFLTP FLQAVYLFVQ YIIMVNLLIA
FFNNVYFDMK SISNNLWKYN RYRYIMTYHE KPWLPPPFIL LSHIGLLVRR ICHHRRPHEQ
DQEEGDVGLK LYLSEEDLKK LHDFEERCVE EYFHEKTESL HSSNEERIRV TTERVAEMCF
QMKEVHERVF YIKDSLVSLD SHLGHLQDLS ALTVDTLKVI SAVDTLQVEE ARLATAKHSA
CRKLPHSWNN IIYSESLGSL EGSGDKKYQY YSMPPSLLRS MARSQCPSES QKSPLRGIMD
PQKENANTMG SWEQLEAESG VIPSEVSQDC PDLPKFGQFL LVPPYRKGAF SEETGSAVSP
TSPADKSQVG LLAAKLQVNP QDVPFQLIVQ DSVLEPRPAR EQENDNSVIH LPSEQESGEV
FSPTLNSAPA VARTVSFPSK TNSMEIGGGY VNWAFSEGDE MGVFNNPKKW QVIGPTSCHS
DYNSTNNGSY PIQIWESKSF SYNSERSRQS SDSSESGLLL HRSSSFWINP LRRDWTVCRG
GSLRSQKEEG LVKTCKSKEF SRTSEKYQSA WAKTKLRNRD KKSQKEKKKR QTLQVPVITV
DGCTQNAPMN SEPAENHLSG EEMEHAKKWL TASKFSQISL EAYMHQKVKS QEIERHTVQL
SDYLRQSQED LSNISLWTTK SNNPSRNSSL RSSKGVDKIS ASLKTPQDLH HHYSAVERNN
LMRLSQTIPF TPIKLFAGEE VTIYRLEESS PLNLDKSMSS WSQHGTAALI QVLSREEMDG
GLRKAMKVVC TWSENDVLKP GQVFIVKSFL PEVVRTWHKI FRDSTVLHLC LREIQQQRAA
QKLIYTFNQV KPHTIPYTPR FLEVFLIYCH SANQWLTIEK YMTGEFHKYN NNNGDEICPS
NILEELMLAF SHWTYEYTRG ELLVLDLQGV GENLTDPSVI KPEDKRSSRM VFGPANLGED
AIRNFIAKHR CNSCCRKLKL PDLRRNDYTP ERVNSVFETE TKEPAARAED EDSNECPEYH
TRL
//
