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Database: UniProt
Entry: U3J3A5_ANAPP
LinkDB: U3J3A5_ANAPP
Original site: U3J3A5_ANAPP 
ID   U3J3A5_ANAPP            Unreviewed;      1901 AA.
AC   U3J3A5;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 2.
DT   27-MAR-2024, entry version 57.
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|Ensembl:ENSAPLP00000013982.2};
OS   Anas platyrhynchos platyrhynchos (Northern mallard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000013982.2, ECO:0000313|Proteomes:UP000016666};
RN   [1] {ECO:0000313|Ensembl:ENSAPLP00000013982.2, ECO:0000313|Proteomes:UP000016666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT   "A new Pekin duck reference genome.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPLP00000013982.2}
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; 8840.ENSAPLP00000013982; -.
DR   Ensembl; ENSAPLT00000014750.2; ENSAPLP00000013982.2; ENSAPLG00000014165.2.
DR   GeneTree; ENSGT00940000158164; -.
DR   HOGENOM; CLU_001390_2_0_1; -.
DR   Proteomes; UP000016666; Chromosome Z.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
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   GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
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   Reference proteome {ECO:0000313|Proteomes:UP000016666};
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        679..697
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        774..793
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        841..859
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        871..890
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        910..930
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        983..1005
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1634..1864
FT                   /note="Alpha-type protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS51158"
SQ   SEQUENCE   1901 AA;  218336 MW;  1A3DEEAF060EB4A6 CRC64;
     SWPVYQPALQ RDEEWSVQKH TKMSPTDAFG TIKFQDGDHT YHAKYIRLSY DSNLDQLLHL
     MVKEWQMELP KLVISVHGGI QNFQLPSKIK QVFSKGLVKA AETTGAWIIT EGINSGVSRH
     VGDALKGRTS PYLRKICAVG IPPWGIIENQ RDLIGKDVVC LYQTLGNPLS KLSTLNSMHS
     HFLMADDGTV GKYGNEMMLR RNLEKYLSLQ KIHARMGQGV PIVGLVVEGG PNVILMVWEY
     VRTSPPVPVV VYDGTGRAAD ILAFTHKHTG DTGELRPQVK EEVLVMIQNM FSLGQKQSSH
     LFHILMECME HRESITILDV ESEEQQDIDL AILTALLKGT NMSASDQLDL ALAWNQLDIA
     KKHILVYGQH WKVGALEQAM QDALVMDRVD FVKLLIEHGV NMHHFLTISR LEELYNTKQG
     PSNLLLHHLV RDVKQSTLPS DYRISLIDIG LVVEYLLGGA YRSSYTRKHF RILYNDLYRK
     HKNNQMGSRM ASAENTLHSQ FFRTAQPYKC KERSTGFHKS KKKSKEDGNF AENYESPGFT
     YPYNDLLVWA VLMKRQKMAM FFWQHGEEAM VKAVVACKLY KAMAHEAKQS NMVDDTSEEL
     KKYSKEFGQL ALDVLEKAFK QNEQMAMKLL TYELKNWSNS TCLKLAVSVG MRPFVSHTCT
     QMLLTDMWMG RLKMRKNSWF KVIISILLPP TILMLEFKTK AEMSHVPQSQ DFHQFTWYHG
     DQSPPSTKDV LSLKDCDVEK VTQKSDESQV DGGQRNLPRT RKIYEFYNAP IVKFWFHTMA
     YMAFLMLFTY TVLVKMEPRP SVQEWLVIIY IFSTAIEKVR EVFISEPGKF SQKVKVWINE
     YWNFTDSIAI ILFMIGFGLR WSEPPVQTAG RLLYCLDIIF WYARLLDLFA VNQHAGPYLT
     MIGKMTANMF YIVVMMAIVL LSFGVSRKAI LSPEEPPSWT LARDIVFQPY WMMFGEVYAG
     EIDVCETNQD CPPGSFLTPF LQAVYLFVQY IIMVNLLIAF FNNVYYDLKS ISNKLWKYNR
     YRYIMTYHDK PWLPPPFILL SHIGLLINRI FHHRPTNESD QEEGDVGLKL YLSDEELKKL
     HDFEEQCVEK YFHEKNESLN SSDSERIRLT TERLEEMFLQ LKEVHEKVFY IKESLISLDS
     QLGHLQDLSA LTVDILKVLS AVDTLQVEEA LLADTKCRSY RKLPHSWSNV LYSKTLSSLE
     CLYDKKYHYY SMPPSLLRSL VRSQWSSECK DHKLRTESNK VVEDSSRKIE IESDTLTSGI
     SSETKSTPRY GQFLLVPPDH QGGPFSEDVT LNLSFSSTPT NIAVQQNMQS VSLIDKEPEG
     YQWSQTDFVI HLPSKKTNAV EADHPLSLHP PLDDGENVIP CCDDREETEG GYVNWGFSEG
     DEKGVFSSRK KQKKAPCIQS TYNCDGNCKD SPPRHVQIKE SKSFSYNSRS SQHSIISENK
     LKHTSFWISP LWRNWGVCRS NSLPSSQKEK SGKTCKARGG NKNMLVVLSV SCQVIRVDDC
     PQNTQVSSEP AEINIWDEEE KHSKNWLTVS NFSQYHGHLK ESYWLGRTQT AIRRSDGEPH
     CSLLGFVHYS KTLSDIFESQ LACSSSIAVK SVLFAAVERN NLMRLAQTIP FTPVQLFAGE
     EVTVYRLEES SPMNLDKSMS SWSQRGMAAM IQVLSREEMD GGLRRAMKVV CTWSENDVLK
     LGQVFIVKSF LPEVVQAWQK IFHDGTVLHL CLREIQQQRA AQKLIYTFNQ VKPHTIPYTP
     RFLEVFLIYC HSANQWLTIE KYMTGEFRKY NNNNGDEITP SSLLEELLLA FSHWTYVYTR
     GELLVLDLQG VGENLTDPSV IKPEDKRSGK MVFGPANLGE DAIRNFITKH RCNSCCRRLK
     LPDLRRNDCT MERLRPAFGE VEANARETDD ADEPLEYDTR L
//
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