ID A0A340WQG1_LIPVE Unreviewed; 2021 AA.
AC A0A340WQG1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
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_007451056.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007451056.1};
RN [1] {ECO:0000313|RefSeq:XP_007451056.1}
RP IDENTIFICATION.
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_007451056.1; XM_007450994.1.
DR STRING; 118797.A0A340WQG1; -.
DR GeneID; 103087343; -.
DR KEGG; lve:103087343; -.
DR CTD; 140803; -.
DR InParanoid; A0A340WQG1; -.
DR OrthoDB; 201873at2759; -.
DR Proteomes; UP000265300; 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_007451056.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000265300};
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 743..761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 841..860
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 908..926
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 938..957
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 977..997
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1050..1073
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1749..1979
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 800..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1670..1706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1999..2021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1670..1705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2021 AA; 231588 MW; DDB1BA96301F189C CRC64;
MLLLNKSQKS WIEGVFDKRE CNKIIPSSKD PHRCTAGCQV CQNLIRCYCG RLIRDHYGID
EAWTISAANG SENEQWSVEK 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
TNMLLHHLVQ DVKQHALLSG YRITLIDIGL VIEYLIGRAY RSSYTRKNFR ALYSNLYRKH
KPPLHRRCRS GNRNESAEST LHYQFIRTAQ PYKVKEKSVA LHKSRKKSKE EQNISDDPDS
TGFIYPYNDL LVWAVLMKRQ KMAMFFWQHG EEATVKAVIA CILYRAMARE AKESNMVDDA
SEELKNYSKQ FGRLALDVLE KAFKQNERMA MKLLTYELKN WSNSTCLKLA VSGGLRPFVS
HTCTQMLLTD MWMGRLKMRK NSWLKIIISI LFPPTILTLE FKSKAEMSHV PQSQDSQFTW
YNGDQNASAP KESACLKDYD LESGPDEKPD ENQHFDLKSG PQSLPWTRKV YEFYSAPIVK
FWFYTMVYLA FLMLFTYTVL VEMQPQPTVQ EWLVIIYIFT NAIEKVREVY ISEPGKFTQK
VKVWISEYWN LMETVATGLF LVGFGLRWGD PPFYTAGRLI YCIDIIFWFS RLLDFFAVNQ
HAGPYVTMIA KMTANMFYIV IIMAIVLLSF GVARKAILSP KETPSWRLAR DIVFEPYWMI
YGEVYASEID VCSSQPSCPP GSFLTPFLQA VYLFVQYIIM VNLLIAFFNN VYIDLKSISN
NLWKYNRYRY IMTYHEKPWL PPPFILLSHI GLLLRRLCHH QAPNDQEEGD VGLKLYLSKE
DLKKLHNFEE QCVEKYFHEK MEGLNCSCEE RIRVTSERVT EMCFQLKEMN EKVSFIRDSL
LSLDSQVGHL QDLSALTVDT LKVLSAVDTL QEDEALLANR KHSTCRKLPH SWSNVICAEV
LGSLEISGKK KYQCYSMPPS LLRSLARGWH PPRVQTGPFL EITDRKFSNV RDDQEEQETE
NSIVASGVSL NRQAHPKYGQ FLLVPSHLEQ VPYSAGTNLP LSRPSLEAGT DVLATEHVTQ
SAVPVHLTWQ TPVVSAQGSV VETKEQYESL AQLPARQDKG EQVLPTLICA PAPIKVTSLP
SQVKSMQTGG GYVNWAFSEG DETGVFSTEK QWQTCLASAC NCDSKQSEQC QRQIRDRSLS
DNSTRLAQRD CSEVGPWLQQ NTSLRISPLR RDRPFIRSQS LRLHKEEKLK ICKIKNLSKS
SEIGQSKWIK AKMLTKDRKL SKKKKKTQGL QVPVITVNTC SQSDQLNPEP GENKISEEQN
CSKNWIPVSK FSQISLESYI YQKMKSRETE RHSVRVSDYV RQSQEDLSKN SLWNSRSTKV
NRNSQLRSSN GVNKISTSLK SPQESHHHYS AIERNNLMRL SQTIPFTPIQ LFAGEEVTVY
RLEESSPLNL DKSMSSWSQR GTSAMIQVLS QEEMDGGLRK AMKVISTWSE DGVLKPGHVF
IVKSFLPEVV QAWRKIFQES TVLHLCLREI QQQRAAQKLI YTFNQVKPQT IHYTPRFLEV
FLIYCHSAKQ WLTIEKYMTG EFRKYNNNNG DEIAPSNTLE ELMLAFSHWT YEYTRGELLV
LDLQGVGENL TDPSVIKPEE KQSRGMVFGP ANLGEDAIRN FIAKHRCNSC CRKLKLPDLK
RNDYSPGRIN YAFGLEIKTE PAEETPAEEE GNNSPEDLTR L
//
