ID H3BVY3_TETNG Unreviewed; 1842 AA.
AC H3BVY3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000000145.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000000145.1}
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 -!- 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; 99883.ENSTNIP00000000145; -.
DR Ensembl; ENSTNIT00000004201.1; ENSTNIP00000000145.1; ENSTNIG00000010230.1.
DR GeneTree; ENSGT00940000157091; -.
DR InParanoid; H3BVY3; -.
DR OMA; SSKDPHX; -.
DR TreeFam; TF314204; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
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 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: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 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:UP000007303};
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 759..777
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 854..874
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 924..942
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 954..973
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 985..1008
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1578..1809
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 547..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..1406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1815..1842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1815..1832
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1842 AA; 207846 MW; A1B5657FB417FBE2 CRC64;
QSKKPWIEST FSKRECVYIL PVSKDPHRCL PGCQICQQLV RCCCGRLVRQ HVGFTASLAS
KYSDVKLGEN VGLPTPAAEE WSVEKHTEAS PTDAYGVINF QGGSHSYRAK YARLSYDTRP
ECILRLMLKE WQMELPKILI SVHGGVQNFE LHPRIKQVVG KGLINAAVTT GAWILTGGVN
TGVAKHVGDA LKEHFSRSSK KICTIGIAPW GVIENRNDLL GRDIIAPYQT LLNPLSKLNA
LNSLHSHFLL VDDGTVGRYG AEVNLRRQLE KHINLQRIHA RIGQGVPVVA LIFEGGPNVI
LTVLEYLQES PPVPVVVCEG TGRAADILAY VHKQTEERGR LPDGVEADII ATIKKTFNFS
QSDAIHLFQT LMECMKSKEL ITVFHISSEE HQDIDVAILR ALLKGTNASA FDQLVLTLAW
DRVDIAKNHV FVYGQQLLVS SLEQAMLDAL VMDRVDFVKL LIENGVSMHR FLTISRLEEL
YNTKQPGNNP NLLHLVRDVK QSHLPPNYKI TLIDIGLVIE YLMGGTYRCN YTRKRFRIIY
NNLRGNSRRS GRHSAPGSHL RRNHETFSME ADKKEKTRHN QFIKTAQPYK PKLESSSEQK
TKRSKEEIVD IDDPETRRFP YPFNELLVWA VLMKRQKMSL FFWQHGEENM AKALVACKLY
RSMGYEAKKS DVVDDASEEL KEYSNEFGTL AVDLLEQSFR QDETMAMKLL TYELKNWSNS
TCLKLAVSSH LRPFVAHTCT QMLLSDMWMG RLNMRKNSWY KVILSILVPP AILLLEYKSK
AEMAHIPQSQ DDHQMTMEDS ENNFQSGADD IQMDVFKESR SHDHMEAKNE AETQFRSRKL
PLTRKIYAFY RAPIVKFWSN TLFYLGFLML YSYVVLVKMP EQPSPQEWVV ILYIFTSAIE
KIREMFMSEA GKISQKIKVW FSEYFNICDF LAIITFFIGF GLRLAGGEVF TPGRLVYCLN
IIFWYVRLMD ILAVNQQAGP YVMMIAKMVA NMFYIVVIMA IVLLSFGVPR KAILYPDEEP
SWTLAKDVIF QPYWMMYGEV YAYEIDVCAN NTEPLSKQLC ATGVFLTPLL QAVYLFVQYI
LMVNLLIAFF NNVYLQVKSI SNLVWKYQRY HFIMVYHEKP VLPPPVILLC HVYSLFCMCR
KRKKESTYGP KLFLTEEDRK KLHDFEEQCV EAYFHEKDDQ FHSGSEERIR VTSERVESMC
MQLREVGNKV TFIKRSLHAL DSQIGHLQDL SVLTVDTLKT LTAQRASEAS KVHTQITREL
SLSKNVVPSI GPVAPDAAPH SKSSVIGKRS AGAFFGSSFP QPGTTMADSL FGTGVGSGAG
AEGLGLPSAG ASSGSSAFGL PPPELHLRGP SLSQNKLSRP HEPGLSDSPS SLPNVPSPGT
HFHISSSHLQ PSGSSHPQLS LAGLHPLLPP AGGGSAEFGA FVGHKDIVEL QDSAPEEASS
GQPSPATRPR SQIPPESRGL IRAVNSYAGF TEFGRSPALL HPDSCERAPS RLMTCRRSSK
SPTLPDLASL LPFAVRLLKT LLTVRPIGSP FKPVENYHYS AVERNNLMRL SQSIPFTPVP
PRGEPVTVYR LEESSPNTIN NSMSSWTQKG LCAKIEFLSK EEMGGGLRRA LKVLCTWSEY
DILKPGHLYI VKSFLPEVVQ TWQSIYKEDT VLHLCLREIQ QQRAAQKLTF AFNQLRPKTI
PYSPRFLEVF LLYCHSAGQW FAIEECITGE FRKFNNNNGE EISPTNLLEE TMLAFSHWTY
EYTRGELLVL DLQGGVGEIL TDPSVIKSGE KGSCDMIFGP ANLGDDAIRN FRAKHNCNSC
CRKLKLPDLR RNDYTPDKMT FPHEDPAHPG SKESHQSVRL ML
//
