ID A0A2Y9NCN5_DELLE Unreviewed; 2031 AA.
AC A0A2Y9NCN5;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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|RefSeq:XP_022429202.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022429202.1};
RN [1] {ECO:0000313|RefSeq:XP_022429202.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022429202.1};
RG RefSeq;
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 RefSeq; XP_022429202.1; XM_022573494.1.
DR STRING; 9749.A0A2Y9NCN5; -.
DR KEGG; dle:111174589; -.
DR InParanoid; A0A2Y9NCN5; -.
DR OrthoDB; 201873at2759; -.
DR Proteomes; UP000248483; Unplaced.
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 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 Receptor {ECO:0000313|RefSeq:XP_022429202.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
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 754..772
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 852..871
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 919..937
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 949..968
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 988..1008
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1061..1084
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1759..1989
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 811..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1661..1717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2002..2031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1661..1676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1677..1716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2031 AA; 232817 MW; 4338D84B889F7EEB CRC64;
MRVQVKSQKS WIEGVFDKRE CNKIIPSSKD PHRCTAGCQV CQNLIRCYCG RLIRDHYGID
EAWTISAANG SENEQWCVEK HTMKSSTDTF GTINFQDGEH THHSKYIRTS YDTKLDHLLH
LMLKEWKMEL PKLVISVHGG IQNFKMPSKL KEIFSQGLVK AAETTGAWII TEGINTGVSK
HVGDALKAHS SQSLRKIWTV GIPPWGVIEN RKDLIGRDVV CLYQTLGNPL SKLTTLNCMH
SHFILSDDGT VGKYGNEMKL RRNLEKYLSL QKIHSRSRQG VPVVGLVVEG GPNVILSVWE
TVKDKDPVVV CEGTGRAADL LAFTHKHFAD EGTLRPQVKE EIICMIQNTF NFSLKQSKHL
FQILMECMVH RDSITIFDAD SEESQDLDLA ILTALLKGTN LSASEQLNLA MAWDRMDIAK
KHILIYGQHW KPGSLEQAML DALVMDRVDF VKLLIEYGMN LHRFLTISRL EELYNTKQGP
TNMLLHHLVR DVKQHAVLSS YRITLIDIGL VIEYLIGRAY RSSYTRKNFR ALYSNLYRKH
KQVTTFAQSL PQPPLHRRCR SGNRNESAES TLHYQFIRTA QPYKVKEKSV ALHKSRKKSK
EEQNISDDPD STGFIYPYND LLVWAVLMKR QKMAMFFWQH GEEATVKAVI ACILYRAMAR
EAKESNMVDD ASEELKNYSK QFGRLALDVL EKAFKQNERM AMKLLTYELK NWSNSTCLKL
AVSGGLRPFV SHTCTQMLLT DMWMGRLKMR KNSWLKIIIS ILFPPTILTL EFKSKAEMSH
VPQSQDSQFT WYNGDQNASA PKESACLKDY DLESGPDEKP DENQHFDLKS GPQSLPWTRK
VYEFYSAPIV KFWFYTMVYL AFLMLFTYTV LVEMQPQPTV QEWLVIIYIF TNAIEKVREV
YISEPGKFTQ KVKVWISEYW NLMETVATGL FLVGFGLRWG DPPFYTAGRL IYCIDIIFWF
SRLLDFFAVN QHAGPYVTMI AKMTANMFYI VIIMAIVLLS FGVARKAILS PKEPPSWSLA
RDIVFEPYWM IYGEVYASEI DVCSSQPSCP PGSFLTPFLQ AVYLFVQYII MVNLLIAFFN
NVYIDLKSIS NNLWKYNRYR YIMTYHEKPW LPPPFILLSH IGLLLRRLCH HQAPNDQEEG
DVGLKLYLSK EDLKKLHSFE EQCVEKYFHE KMEGLNCSCE ERIRVTSERV TEMCFQLKEM
NEKVSFIRDS LLSLDSQVGH LQDLSALTVD TLKVLSAVDS LQEDEALLAN RKHSTCRKLP
HSWSNVICAE VLGSLEISGK KKYQCYSMPP SLLRSLARGW HPPRVQTGPF LEITDRKFSN
VRDDQEEQET ENSVVASGVS LNRQAHPKYG QFLLVPSHLE QVPYSAETNL PLSRPSLEAG
TDVLATEHVT QSAVPVHLTW QTPVVSAQGS VVETKEQYES LAQLPARQDK EEQVLPTLIC
TPAPIKVTSL PSHVKSMQTG GGYVNWAFSE GDETGVFSTE KQWQTCLAST CNCDSKQSEQ
CQRQIRDRSL SDNSTRLAQR DCSEVGPWLQ QNTSLRISPL RRDRPFIRSQ SLRLHKEEKL
KICKIKNLSK SSEIGQSKWI KAKMLTKDRK LSKKKKKTQG LQVPVITVNT CSQSDQLNPE
PGENKISEEQ NCSKNWIPVS KFSQISLESY IYQKMKSRET ERHSVHVSDH VRQSQEDLSK
NSLWNSRSTK VNRNSQLRSS NGVNKISTSL KSPQESHHHY SAIERNNLMR LSQTIPFTPI
QLFGEEVTVY RLEESSPLNL DKSMSSWSQR GRSAMIQVLS QEEMDGGLRK AMKVISTWSE
DDVLKPGHVF IVKSFLPEVV QAWRKIFQES TVLHLCLREI QQQRAAQKLI YTFNQVKPQT
IPYTPRFLEV FLIYCHSAKQ WLTIEKYMTG EFRKYNNNNG DEIAPSSTLE ELMLAFSHWT
YEYTRGELLV LDLQGVGENL TDPSVIKPEE KQSRGMVFGP ANLGEDAIRN FIAKHRCNSC
CRKLKLPDLK RNDYSPGRIN SAFGLEIKTE PAEETPAEEE GNNSPEDLTR L
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