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Database: UniProt
Entry: A0A452SH59_URSAM
LinkDB: A0A452SH59_URSAM
Original site: A0A452SH59_URSAM 
ID   A0A452SH59_URSAM        Unreviewed;      1307 AA.
AC   A0A452SH59;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000031813.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000031813.1}
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   Ensembl; ENSUAMT00000035473.1; ENSUAMP00000031813.1; ENSUAMG00000024060.1.
DR   GeneTree; ENSGT00940000157091; -.
DR   Proteomes; UP000291022; 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; 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; 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:UP000291022};
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}.
FT   TRANSMEM        377..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        444..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        478..497
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        518..537
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        599..622
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1055..1266
FT                   /note="Alpha-type protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS51158"
FT   REGION          65..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1272..1307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1285..1307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1307 AA;  150161 MW;  0FBB79B26BC68F97 CRC64;
     MHGNIEKYPV YIKLMICFQG NLPPGYKITL IDIGLVIEYL MGGTYRCTYT RKRFRLIYNS
     LGGNNRRSGR NTSSSTPQLR KSHESFGNRA DKKEKMRHNH FIKTAQPYRP KIDTAVEEGK
     KKRAKDEIVD IDDPETKRFP YPLNELLIWA CLMKRQVMAR FLWQHGEESM AKALVACKIY
     RSMAYEAKQS DLVDDTSEEL KQYSNDFGQL AVELLEQSFR QDETMAMKLL TYELKNWSNS
     TCLKLAVSSR LRPFVAHTCT QMLLSDMWMG RLNMRKNSWY KVILSILVPP AILMLEYKTK
     AEMSHIPQSQ DAHQMTMEDS ENNFQNIAEE IPMEVFKEVR ILDSNEGKNE MEIQIKSKKL
     PITRKFYAFY HAPIVKFWFN TLAYLGFLML YTFVVLVQME RLPSVQEWIV IAYIFTYAIE
     KVREIFMSEA GKISQKIKVW FSDYFNISDT IAIISFFVGF GLRFGAKWNF ENAYDNHVFV
     AGRLIYCLNI IFWYVRLLDF LAVNQQAGPY VMMIGKMVAN MFYIVVIMAL VLLSFGVPRK
     AILYPREAPS WTLAKDIVFH PYWMIFGEVY AYEIDVCAND STISQICGPG TWLTPFLQAV
     YLFVQYIIMV NLLIAFFNNV YLQVKAISNI VWKYQRYHFI MAYHEKPVLP PPLIILSHIV
     SLFCCICKRR KKDKTSDGPK LFLTEEDQKK LHDFEEQCVE MYFNEKDDKF HSGSEERIRV
     TFERVEQMCI QIKEVGDRVN YIKRSLQSLD SQIGHLQDLS ALTVDTLKTL TAQKASEASK
     VHNEITRELS ISKHLAQNLI DDGPVRPSVW KKHSVVNTLS SSLPQGGLES TNPFLCNIFM
     KDEKDPPCNI FSQDLPVIPQ RKEFNFPEAG SSCGALFPSA VSPPELRQRI HGVEMLKIFS
     KNQKLGSSSN SIPHLSSPPT KFFVSTPSQP SCKSHLETVT KDQEIVCSKA AEGDNVEFGA
     FVGKFSKPSD APSENTLKHV SSHAGFTECR KTSIPLHSEQ GLASPFKPVL DTNYYYSAVE
     RNNLMRLSQS IPFTPVPPRG EPVTVYRLEE SSPSILNNSM SSWSQLGLCA KIEFLSKEEM
     GGGLRRAVKV QCTWSEHDIL KSGHLYIIKS FLPEVVNAWS RVYKEDTVLH LCLREIQQSF
     GFMFLEVFLL YCHSAGQWFA VEECMTGEFR KYNNNNGDEI IPTNTLEEIM LAFSHWTYEY
     TRGELLVLDL QGVGENLTDP SVIKAEEKRS CDMVFGPANL GEDAIKNFRA KHHCNSCCRK
     LKLPDLKRND YTPDKMLFPQ DEPSDLTLQP GNSTKESEST NSIRLML
//
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