ID A0A3P8PI60_ASTCA Unreviewed; 1702 AA.
AC A0A3P8PI60;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000016654.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000016654.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000016654.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; 8154.ENSACLP00000016654; -.
DR Ensembl; ENSACLT00000017057.1; ENSACLP00000016654.1; ENSACLG00000011338.1.
DR GeneTree; ENSGT00940000158164; -.
DR Proteomes; UP000265100; Chromosome 12.
DR Bgee; ENSACLG00000011338; Expressed in spleen.
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: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 Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1702
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017924525"
FT TRANSMEM 776..795
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 843..861
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 873..891
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 911..928
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 985..1008
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1457..1691
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 1288..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1339..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1309
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1702 AA; 192912 MW; 3AF525DDE1BF4DF8 CRC64;
MLLPMHLCNV VLFARCCCGH LIGEHSWQDS LPPLSLCPGP GQDVEEEWSM ERHTRASPTN
AYGTVDFEDT ATRVCRAKYV RVAVDSKPEA LLQLMLREWQ MERPKLLLSV HGGSENFTLP
PKVNQAFSKG LITAALSTGA WIFTDGINTG VSKYVGDAVK SFGSHDLRKR NTVGITPWGV
IDNNMDLIGR DVFRPYQPLG NPLSKRACLN GFHSHFLLVD DGTLGKHGCQ QGLRRKLEKH
IQLQKIHPRL NQGVPVVCVV VEGGPSVVST VLDYVSTVPP VPVFVFEGSG RAADLLAFLH
KQTAVDRPLE ADIKENFLTT IGDAFGMERT EATDLYTLLL QCMDHRQSIT IFDSESDDQM
APDAAILTAT LKGTKASPSE QLSMTLAWDR ADIAQKDVLV YGQHWQVGSL EQAMLDALVM
DRVSFVKTLI DNGMTMSRFL TVDRLEEHLL FLICYRLSII DMGLVIEYLI GGAYRSTYTR
KQFRAAYSRL HEKVTTFSKL RHGLMPSSTR NRSLQDLHFF RTAQPYKRKV GLDGDVSSPG
LDDAPLLVPF NFNDLFVWAV LQQRQQMALF LWQHGEEALA RATVACKLYR SMAFEARQSS
LDDNIIERFK TYSLEFGKLA VDVLDCAFRQ NEQMAMKLLT YEMEAWSHFT CLQMAVSSCH
RPFVSHSCTQ TLLTDLWTGP LNMRKNSFLK IILSLLLPPA ILLLEFKSKA EMCHVPQTHE
AMLFGLDSVK PAPEQGLSFQ DKRVGPVSET MSSITVRCVS WITTLYDFYT APVVKFWFHT
MSYLAFLMLF SYVVLVKMED QPSVQEWLVI AYILSTAAEK TREILMSEAT KLSQKLKIWF
SEYWNISDFI AILLFVAGLA MRWHSDPYRT AGRLTYCLDI IFWFIRVMDL LAVNQHAGPY
LTMITKMTRN MFYIVVMMAI VLLTYGVSRK AVLSPDEEPS WSLARDIVFQ PYWMIYGEVY
ASEIDPCQED DSCPPASFLA PFLQAVYMFV QYIIMVNILI AFFNNVYFDM ASTSNKLWKY
NRYRYIMTYQ VRPWLPPPLN LLSHMDLGLR AIYKKFSGDA EREERASGLK LYLGHEDRKK
LHEFEERCVQ AYFHEKSECP LSSQKNRIKV TAERTEEMCM MVGEVSEKVN FIQDSLSDLD
SQLGHLQDLS ALAVDTLTLL SASNNLHQEE TRLAQCRLIT ASQHAIPHSW TLPHRSGADG
DAANIQRLVA KPYKSTPPSL LKGYTLAGNR RESQECHVGV RGRFSSVRDQ TPCESCEPSQ
CGSPLSPRGL ESLHFKFWTC EPYLFTSQEE TSMEEEDEVE EEGEEKEEEK TQEEPPNIDV
HRASSSAFLF DPEDISEGLT NPAFSCDDSQ PTSRSRNSNQ WRKPIKSPRW ACLSRDRPYG
YCRSLSSSME NMTFAGAPLS PTRGSFPSLN ESMNNETVER NNLMRLAQTI PFTPVSIMGG
EEVSVYSLEE VASDADPESS SVSSWSSRGL SAILQPLLSE EGSLDGGLRQ GRRVLCTWAE
QDVLRPGLVY VVKGFRPEVV RVCKKYFHGS TALQLCLREI QQQRAAQKMM QVFNQVKPDD
LHHSPRFLDV SLVLWHSNGQ WLTIERNMSG DFMKYNNNTG EEITPCCSLE EMLLAFSHWT
YEYSRRELLV LDIQGVGEEL TDPTVIMAED QSVSRGEMLF GPDNLGDAGI NGFLQKHSCS
AWCHRLGLKG QKHTKPCLLF FF
//
