ID KPCT_RAT Reviewed; 707 AA. AC Q9WTQ0; DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 2. DT 13-NOV-2007, entry version 36. DE Protein kinase C theta type (EC 2.7.11.13) (nPKC-theta). GN Name=Prkcq; Synonyms=Pkcq; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway; RX PubMed=15057822; DOI=10.1038/nature02426; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 524-667. RC STRAIN=Wistar; TISSUE=Brain; RX PubMed=11220785; DOI=10.1385/JMN:15:2:121; RA Minami H., Owada Y., Suzuki R., Handa Y., Kondo H.; RT "Localization of mRNAs for novel, atypical as well as conventional RT protein kinase C (PKC) isoforms in the brain of developing and mature RT rats."; RL J. Mol. Neurosci. 15:121-135(2000). CC -!- FUNCTION: This is a calcium-independent, phospholipid-dependent, CC serine- and threonine-specific enzyme. Essential for T-cell CC receptor (TCR)-mediated T-cell activation, but is dispensable CC during TCR-dependent thymocyte development. Links the TCR CC signaling complex to the activation of NF-kappa-B in mature T CC lymphocytes. Required for interleukin-2 (IL2) production (By CC similarity). CC -!- FUNCTION: PKC is activated by diacylglycerol which in turn CC phosphorylates a range of cellular proteins. PKC also serves as CC the receptor for phorbol esters, a class of tumor promoters (By CC similarity). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- COFACTOR: Magnesium (By similarity). CC -!- ENZYME REGULATION: Three specific sites; Thr-538 (activation loop CC of the kinase domain), Ser-676 (turn motif) and Ser-695 CC (hydrophobic region), need to be phosphorylated for its full CC activation (By similarity). CC -!- SUBUNIT: Interacts with TXNL2/PICOT (By similarity). CC -!- DOMAIN: The C1 domain, containing the phorbol ester/DAG-type CC region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the CC C2 domain is a non-calcium binding domain. CC -!- PTM: Autophosphorylation at Thr-219 is required for targeting to CC the TCR and cellular function of PKC upon antigen receptor CC ligation. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. PKC subfamily. CC -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain. CC -!- SIMILARITY: Contains 1 C2 domain. CC -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AABR03106275; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR03107517; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR03106934; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR03106283; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR03107733; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR03106804; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR03108584; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR03106764; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB020614; BAA78371.1; -; mRNA. DR UniGene; Rn.8227; -. DR HSSP; P31751; 1MRY. DR SMR; Q9WTQ0; 232-281, 377-649. DR Ensembl; ENSRNOG00000019057; Rattus norvegicus. DR RGD; 620968; Prkcq. DR InterPro; IPR002219; DAG_PE_bd. DR InterPro; IPR015745; PKC. DR InterPro; IPR000961; Pkinase_C. DR InterPro; IPR014376; Prot_kin_PKC_delta. DR InterPro; IPR000719; Prot_kinase_core. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR PANTHER; PTHR22985:SF86; PKC; 2. DR Pfam; PF00130; C1_1; 2. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00433; Pkinase_C; 1. DR PIRSF; PIRSF000551; PKC_delta; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00109; C1; 2. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS50004; C2; FALSE_NEG. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS00479; ZF_DAG_PE_1; 2. DR PROSITE; PS50081; ZF_DAG_PE_2; 2. PE 2: Evidence at transcript level; KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Phorbol-ester binding; Phosphoprotein; Repeat; KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger. FT CHAIN 1 707 Protein kinase C theta type. FT /FTId=PRO_0000270836. FT DOMAIN 8 123 C2. FT DOMAIN 380 634 Protein kinase. FT DOMAIN 635 706 AGC-kinase C-terminal. FT ZN_FING 159 209 Phorbol-ester/DAG-type 1. FT ZN_FING 231 281 Phorbol-ester/DAG-type 2. FT NP_BIND 386 394 ATP (By similarity). FT ACT_SITE 504 504 Proton acceptor (By similarity). FT BINDING 409 409 ATP (By similarity). FT MOD_RES 219 219 Phosphothreonine; by autocatalysis (By FT similarity). FT MOD_RES 538 538 Phosphothreonine; by PDPK1 (By FT similarity). FT MOD_RES 676 676 Phosphoserine (By similarity). FT MOD_RES 685 685 Phosphoserine (By similarity). FT MOD_RES 695 695 Phosphoserine (By similarity). SQ SEQUENCE 707 AA; 81750 MW; 7F82E35DE0C09DB9 CRC64; MSPFLRIGLS NFDCGTCQAC QGEAVNPYCA VLVKEYVESE NGQMYIQKKP TMYPPWDSTF DAHINKGRVM QIIVKGKNVD LISETTVELY SLAERCRKNN GRTEIWLELK PQGRMLMNAR YFLEMSDTKD MSEFENEGFF ALHHRRGAIK QAKVHHVKCH EFTATFFPQP TFCSVCHEFV WGLNKQGYQC RRCNAAIHKK CIDKVIAKCT GSAINSRETM FHKERFKIDM PHRFKVYNYK SPTFCEHCGT LLWGLARQGL KCDACGMNVH HRCQTKVANL CGINQKLMAE ALAMIESTQQ ARTLRDSEHI FREGPIEISF PRSIKSETRP PCVPTPGKSE PQGICWESPL DGADKTAQPP EPEVNLQRAS LQLKLKIDDF ILHKMLGKGS FGKVFLAEFK RTKQFFAIKA LKKDVVLMDD DVECTMVEKR VLSLAWEHPF LTHMFCTFQT KENLFFVMEY LNGGDLMYHI QSCHKFDLSR ATFYAAEVIL GLQFLHSKGI VYRDLKLDNI LLDRDGHIKI ADFGMCKENM LGDAKTNTFC GTPDYIAPEI LLGQKYNHSV DWWSFGVLLY EMLIGQSPFH GQDEEELFHS IRMDNPFYPR WLEREAKDLL VKLFVREPEK RLGVRGDIRQ HPLFREINWE ELERKEIDPP FRPKVKSPYD CSNFDKEFLS EKPRLSFADR ALINSMDQNM FSNFSFINPG METLICS //