ID H2MAR4_ORYLA Unreviewed; 1973 AA.
AC H2MAR4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 48.
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:ENSORLP00000015624.2};
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000015624.2, ECO:0000313|Proteomes:UP000001038};
RN [1] {ECO:0000313|Ensembl:ENSORLP00000015624.2, ECO:0000313|Proteomes:UP000001038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000015624.2,
RC ECO:0000313|Proteomes:UP000001038};
RX PubMed=17554307; DOI=10.1038/nature05846;
RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT "The medaka draft genome and insights into vertebrate genome evolution.";
RL Nature 447:714-719(2007).
RN [2] {ECO:0000313|Ensembl:ENSORLP00000015624.2}
RP IDENTIFICATION.
RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000015624.2};
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; 8090.ENSORLP00000015624; -.
DR Ensembl; ENSORLT00000015625.2; ENSORLP00000015624.2; ENSORLG00000012478.4.
DR GeneTree; ENSGT00940000158164; -.
DR HOGENOM; CLU_046430_1_0_1; -.
DR InParanoid; H2MAR4; -.
DR OrthoDB; 201873at2759; -.
DR Proteomes; UP000001038; Chromosome 9.
DR Bgee; ENSORLG00000012478; Expressed in intestine and 10 other cell types or tissues.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
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:0005261; F:monoatomic cation channel activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0098655; P:monoatomic cation transmembrane transport; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
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; 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 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:UP000001038};
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 867..887
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 934..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 1003..1023
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1076..1099
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1125..1147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1718..1952
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 560..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1434..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1553..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1453
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1973 AA; 223435 MW; 74986DD90D34053B CRC64;
MRVDGRPQHF CVLHLNDTNM SRKSWIEETL FKRECVRFIP SSWDQHRCVP VCQICQNLIR
CCCGRLVGEH SWQESVPPLS FYAASGQEME EDWSIEVHTR ASPTNAYGTI DFEDTATRVC
RAKYVRVAVD SKPEALLQLM LREWQMERPK LLLTVQGGTE NFVLPPKVMQ AFSKGLITAA
LSTGGWILTD GINTGVSKYV GEAVKVFGGH DLRKRNTVGI TPWGVIDNNM DLIGRDVFKP
YQPLGNPLSK RVCLNGFHSH FLLVDDGTLG KYGCQQGLRR KLEKHIQQQK IHPRLNQRVP
MVCVVVEGGP SIVFTVLDYV SSAPPVPVFV FEGSGRAADL LSFLHKQTAN DRQLDADIIE
DFLTRIGDEF GVERTEAIRL YSVLQQCMEH RESITIFDSE SDDQMAPDAA ILSTTLKGTK
ASPAEQLNMA LAWDQADIAQ KDILVYGQHW PVGSLEKAML DALVLDRVSF VKMLIDNGMT
MSHFLTVERL EELYNTPLGQ TQRFLQHLVE DAKQTSLPAG YRLSLIDVGL VIEYLIGGAY
RSTYTRKHFR AAYSRMQDND RRWDSSGSFS KQRLGLKSNS RRNGSRQDLQ FFRTAQPYKR
KDQDATPGST RDTRLSSSLG DASLQVLFNF NDLFVWAVLQ QRQQMALFLW QHGEEALARA
IVGCKLYRSM AFEARLSSMY DNIAEKFKAD SLEFGKLAVD VLDCAFRQNG QMAMKLLTSE
MEAWSHFTCL QLAVSSCHRP FVSHSCTQTL LTDLWTGPLN MRKNSFMKII LSLLLPPAIL
LLEFKSEAEM CHVPQTHEAM LFGLDSVKST PVPQATADLS HHDAERGLPF YEKCLGPLSR
SVSTITVQWL PWITRIYDFY TAPVVKFWFH TMSYLCFLML FSFVVLVKME NRPSIQEWLV
IFYIVSTAVE KTREVLMSEP RKLRQKLKIW FSEYWNISDF VAILLFLVGF ALRWHPDPYR
TAGRIAYCLD IIFWFIRVLD LLAVNQHAGP YLTIITKMTS NMFFIVVMMA IVLLSFGVSR
KAILSPDEEP SWSLARDIVF QPYWMIFGEV YAGEIDPCAG GNSCPPASFL TSFLQAVYMF
VQYIIMVNVL IAFFNNIYFD MASTSNKLWK YNRYRYIMTY QERPWLPPPL ILLSHMALAL
RCIYWKLLGD TEPGERGSGL KLHLGHEDRK KLHEFEKKCV EVYFHEKDRD VQSNQIKKIR
AIAERAEEMS VMVGEISEKV NCIQHSLSEL DCQMGQLQDL SALAVDTLTL LTASDSLQKE
EARLAQCRIN PTLQHVLPHS WTLPHRSNTD CDVPSFRRLN TKSCKSTPPS LLKGSVAAAS
RVASVERHMG SKGSKEAKHK DTERKEETTT EDSHSGTADY PIEKLLGVPK PSSHASVTLF
NNGKIIHEGE KHQTPSESCG SSRCESPLSP RAVGPPSQRS WACDPYLYPS VADTSMEEQE
ECDSEEQDDT PEHLTDSEGD RLPSFVSKRS SQWRRPSIAP RWLYMPKERF YSFSRSLSSS
MENITFSGAP LSPTRGSFFT LNEAVSKERI RGRRGFRDDT CLPCSRSQEW SKSSDSIQVS
GSREKGQSRK TVKIKESSFD PEGVQPHLPD ASWRRRSKFI GEPTCWSAST SLSQLNFDSP
DLMKQMISHQ EVWSPTHSAW NSRAKSMSRR SSLQSGIPLE VKSPSFQSSE NLYPHYSATE
RNNLMRLAQT IPFTPVSIFG GEEVSIYTLE EAPCDADADS PSASVWSSKG LSAILQPLSS
EEGSLDGGLR QGCRMLCTWA EQDILKPGLI YVAKAFKSEV VHVWQKHFPG STALQLCLRE
IQQQRAAQKM MQVFNQIKPH DMHPTPRFLD VSLVLWHSNG QWLTIERNMT GDFRKYNNNT
GEEITPCSSL EDMLLAFSHW TYEHSCKELL VLDIQGVGEE LTDPTVIMAD DQSGGKGDLL
FGPDNLGVAA INGFLQKHTC NLCCHRLGLK DLRTRPTSSE ISSEAGRISR KEE
//
