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Database: UniProt
Entry: F6TTK9_MONDO
LinkDB: F6TTK9_MONDO
Original site: F6TTK9_MONDO 
ID   F6TTK9_MONDO            Unreviewed;      1091 AA.
AC   F6TTK9;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=protein kinase C {ECO:0000256|ARBA:ARBA00012429};
DE            EC=2.7.11.13 {ECO:0000256|ARBA:ARBA00012429};
GN   Name=LOC100617582 {ECO:0000313|Ensembl:ENSMODP00000036521.3};
OS   Monodelphis domestica (Gray short-tailed opossum).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX   NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000036521.3, ECO:0000313|Proteomes:UP000002280};
RN   [1] {ECO:0000313|Ensembl:ENSMODP00000036521.3, ECO:0000313|Proteomes:UP000002280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17495919; DOI=10.1038/nature05805;
RA   Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., Duke S.,
RA   Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., Kamal M.,
RA   Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., Benos P.V.,
RA   Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., Deakin J.E.,
RA   Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., Gu W., Hore T.A.,
RA   Huttley G.A., Kleber M., Jirtle R.L., Koina E., Lee J.T., Mahony S.,
RA   Marra M.A., Miller R.D., Nicholls R.D., Oda M., Papenfuss A.T., Parra Z.E.,
RA   Pollock D.D., Ray D.A., Schein J.E., Speed T.P., Thompson K.,
RA   VandeBerg J.L., Wade C.M., Walker J.A., Waters P.D., Webber C.,
RA   Weidman J.R., Xie X., Zody M.C., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Bloom T., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M.,
RA   Samollow P.B., Lander E.S., Lindblad-Toh K.;
RT   "Genome of the marsupial Monodelphis domestica reveals innovation in non-
RT   coding sequences.";
RL   Nature 447:167-177(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMODP00000036521.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily. {ECO:0000256|ARBA:ARBA00005490}.
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DR   AlphaFoldDB; F6TTK9; -.
DR   Ensembl; ENSMODT00000038113.3; ENSMODP00000036521.3; ENSMODG00000024997.3.
DR   eggNOG; KOG0695; Eukaryota.
DR   GeneTree; ENSGT00940000164563; -.
DR   HOGENOM; CLU_000288_63_29_1; -.
DR   TreeFam; TF102004; -.
DR   Proteomes; UP000002280; Chromosome 8.
DR   Bgee; ENSMODG00000024997; Expressed in testis and 16 other cell types or tissues.
DR   ExpressionAtlas; F6TTK9; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 3.30.70.960; SEA domain; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000082; SEA_dom.
DR   InterPro; IPR036364; SEA_dom_sf.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351:SF241; PROTEIN KINASE C; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   Pfam; PF01390; SEA; 2.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF82671; SEA domain; 2.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50024; SEA; 2.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002280};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          26..146
FT                   /note="SEA"
FT                   /evidence="ECO:0000259|PROSITE:PS50024"
FT   DOMAIN          481..602
FT                   /note="SEA"
FT                   /evidence="ECO:0000259|PROSITE:PS50024"
FT   DOMAIN          629..679
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          751..1017
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1018..1089
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          236..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         784
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1091 AA;  121379 MW;  4EF23974CAF96CA9 CRC64;
     MTANNTSGYK HQMSFPCFTN ISWSSCYKTF KLSFTITNMF YTTKMNQKDS RTFKAAEHIL
     QILLKVLFGS SKLGSQYCGC SGLSLRSLKN SIATGVDILC TFKKDSSNLV LDKKVVSWEL
     TEQLCRRELK HLVIDNDSLI VNGYQHKLPG IRSTKRSEVG VGPVTHIPDH GEPGKIMTSL
     TSGLLIRESP VYAIESDIGV GPFTHIPEHG APGDMTSVTS ESTVCAMGFS TETSGTLKNV
     SGSDQGREPT NSTSIPMTDF IGRDSIAYTE TDIRVMETTP RATATQDPLL TVPTGAGDLI
     PGMHRRTVSS PTETSVPSEI SSGVTIAIAR TSLSMTPVEI TASPGSSAPL NISLSRRTAS
     LEPATSLEDP GPAGLTPETE RNPQATPTPA ITLPPASTQE VCTTASPSPP DTTTEGSSVQ
     AGTASVSDQE PSTSSLFPRG DAGVVPDTHA QGHDVPGSTV APIRSPLTPV STIIPIAGRY
     NWKSFILNFT ITNMFYTTKM AQRDSSTFRL PECFLQRLFK VLFERSSLGS QYCGCNVTLL
     RSMKNGAATG VEVICFYKEV FSVPVLDKKK IYQELSQETN GITRLGHYIL DKKSLYVDGY
     NPQMPPPSTK ESVYHHGTRR WRKLYRMNGH LFQSKCFNRR AYCAQCSERI WCLGRQGYKC
     IKCKLLVHKG CHILVPRTCK RHMNLVMPSQ EPQVEDKNDK VDLPSEENDG LAYVPSTWKH
     DSLKDDSGDI KPVIDGMDGI KISQGLGLQD FDLIRVIGRG SYAKVLLVRL KKNDQIYAMK
     VVKKKFVHDH ENTNWVQTEK HVFEQASSNP FLVGLHSCFQ TRSHLFLVIE YVNGGDLLFH
     MQRKNKLPEE HTRFYAAEIC IALNFLHERG IIYRDLKLDN VLLDSEGHIK LTDYGICKEG
     LGPGDTTRTF CGTPNYIAPE ILRGEEYGFS VDWWALGVLM FEMMVGRSPF DIITDKLDMD
     TEDYLFQVIL EKPIQIPRFL SVKASRVLKG FLNKDPKGRL GCQPQTGFSD IKSHTFFRSI
     DWDLLEKKQA LPPFQPQITD DYGLDNFDTQ FTSEPVQLTP DDENVIKRID QSEFEGFEYI
     NPLLLSTEES V
//
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