ID A0A2U4AVH0_TURTR Unreviewed; 1824 AA.
AC A0A2U4AVH0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 2.
DT 27-MAR-2024, entry version 29.
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=TRPM7 {ECO:0000313|RefSeq:XP_019784970.2};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019784970.2};
RN [1] {ECO:0000313|RefSeq:XP_019784970.2}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019784970.2};
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR629601-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR629601-3};
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_019784970.2; XM_019929411.2.
DR Proteomes; UP000245320; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd16971; Alpha_kinase_ChaK1_TRMP7; 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; IPR029601; TRPM7_a-kinase_dom.
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 ATP-binding {ECO:0000256|PIRSR:PIRSR629601-2};
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 ECO:0000256|PIRSR:PIRSR629601-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR629601-2};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000313|RefSeq:XP_019784970.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
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, ECO:0000256|PIRSR:PIRSR629601-3}.
FT TRANSMEM 758..776
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 856..878
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 923..945
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 957..976
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 997..1016
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1078..1101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1595..1824
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 544..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1379..1405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1492..1543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1500..1515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1768
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-1"
FT BINDING 1625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1649
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1754
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1770
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1778
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1795..1801
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-2"
FT BINDING 1811
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1813
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
FT BINDING 1817
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR629601-3"
SQ SEQUENCE 1824 AA; 208127 MW; 544F14A486F8A6B6 CRC64;
MSQKSWIEST LTKRECVYII PSSKDPHRCL PGCQICQQLV RCFCGRLVKQ HACFTASLAM
KYSDVKLGDH FNQTLEEWSV EKHTEQSPTD AYGVINFQGG SHSYRAKYVR LSYDTKPEVI
LQLLLKEWQM ELPKLVISVH GGMQKFELHP RIKQLLGKGL IKAAVTTGAW ILTGGVNTGV
AKHVGDALKE HTSRSSRKIC TIGIAPWGVI ENRNDLVGRD VVAPYQTLLN PLSKLNVLNN
LHSHFILVDD GTVGKYGAEV RLRRELEKTI NQQRIHARIG QGVPVVALIF EGGPNVILTV
LEYLQESPPV PVVVCEGTGR AADLLAYIHK QTEEGGNLHD AAEPDIISTI KKTFNFGQSE
AVHLFQTLME CMKRKELITV FHIGSEEHQD IDVAILTALL KGTNASAFDQ LILTLAWDRV
DIAKNHVFVY GQQWLVGSLE QAMLDALVMD RVAFVKLLIE NGVSMHKFLT IPRLEELYNT
KQGPTNPMLF HLVRDVKQGN LPPGYKITLI DIGLVIEYLM GGTYRCTYTR KRFRLIYNSL
GGNNRRSGRN TSSSTPQLRK SQESFGNRAD KKEKMRHNHF IKTAQPYRPK IDTAVEEGKK
KRTKDEIVDI DDPETKRFPY PLNELLIWAC LMKRQVMARF LWQHGEESMA KALVACKIYR
SMAYEAKQSD LVDDTSEELK QYSNDFGQLA VELLEQSFRQ DETMAMKLLT YELKNWSNST
CLKLAVSSRL RPFVAHTCTQ MLLSDMWMGR LNMRKNSWYK VILSILVPPA ILMLEYKTKA
EMSHIPQSQD AHQMTMEDSE NNFQNITEEI PMEVFKEVRI LDRNEGKNEL EIQIKSKKLP
ITRKFYAFYH APIVKFWFNT LAYLGFLMLY TFVVLVQMEQ LPSVQEWIVI AYIFTYAIEK
VREIFMSEAG KISQKIKVWF SDYFNISDTI AIISFFIGFG LRFGAKWNFE NAYDNHVFVA
GRLIYCLNII FWYVRLLDFL AVNQQAGPYV MMIGKMVANM FYIVVIMALV LLSFGVPRKA
ILYPREAPSW TLAKDIVFHP YWMIFGEVYA YEIDVCAKDS TITEICGPGT WLTPFLQAVY
LFVQYIIMVN LLIAFFNNVY LQVKAISNIV WKYQRYHFIM AYHEKPVLPP PLIILSHIVS
LFCCICKRRK KDKTSDGPKL FLTEEDQKKL HDFEEQCVEM YFNEKDDKFH SGSEERIRVT
FERVEQMSIQ IKEVGDRVNY IKRSLQSLDS QIGHLQDLSA LTVDTLKTLT AQKASEASKV
HNEITRELSI SKHLAQNLID DGSVRPSVWK KHSVVNTLSS SLPQGGLESN NPFLCNIFMK
DEKDSQFNIS GQDLPVIPQR KEFNFPEAGS SCGALFPSAV SPPELRQRQH GVETLKMFSK
NQKSGSSSNS IPHLSSPPTK FFVSTPSQPS CKSHLETITK DQETVCSKAA EGDNVEFGAF
VGHRDSMDLQ RFKETSNKIK EILSNDIPSE NTLKHVSSHA GFTECHKTSV PLHSEQVESN
SRRPSIEDSH EVDSKAALLP DWLQDRPSNR EMPSEEGTLN GLASPFKPVM DTNYYYSAVE
RNNLMRLSQS IPFTPVPPRG EPVTVYRLEE SSPNILNNSM SSWSQLGLCA KIEFLSKEEM
GGGLRRAVKV QCTWSEHDIL KSGHLYIIKS FLPEVVNTWS SIYKEDTVLH LCLREIQQQR
AAQKLTFAFN QMKPKSIPYS PRFLEVFLLY CHSAGQWFAV EECMTGEFRK YNNNNGDEII
PTNTLEEIML AFSHWTYEYT RGELLVLDLQ GVGENLTDPS VIKAEEKRSC DMVFGPANLG
EDAIKNFRAK HHCNSCCRKL KLPG
//
