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 12-OCT-2022, entry version 146. DE RecName: Full=Protein kinase C theta type; DE EC=2.7.11.13 {ECO:0000250|UniProtKB:Q04759}; DE AltName: Full=nPKC-theta; GN Name=Prkcq; Synonyms=Pkcq; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC 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., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., 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., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., 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., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT 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 protein RT kinase C (PKC) isoforms in the brain of developing and mature rats."; RL J. Mol. Neurosci. 15:121-135(2000). RN [3] RP FUNCTION IN PHOSPHORYLATION OF MSN. RX PubMed=9516463; DOI=10.1074/jbc.273.13.7594; RA Pietromonaco S.F., Simons P.C., Altman A., Elias L.; RT "Protein kinase C-theta phosphorylation of moesin in the actin-binding RT sequence."; RL J. Biol. Chem. 273:7594-7603(1998). RN [4] RP INTERACTION WITH GLRX3. RX PubMed=18479680; DOI=10.1016/j.cellimm.2008.04.005; RA Kato N., Motohashi S., Okada T., Ozawa T., Mashima K.; RT "PICOT, protein kinase C theta-interacting protein, is a novel regulator of RT FcepsilonRI-mediated mast cell activation."; RL Cell. Immunol. 251:62-67(2008). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). CC -!- FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)- CC dependent serine/threonine-protein kinase that mediates non-redundant CC functions in T-cell receptor (TCR) signaling, including T-cells CC activation, proliferation, differentiation and survival, by mediating CC activation of multiple transcription factors such as NF-kappa-B, JUN, CC NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells, is required CC for the activation of NF-kappa-B and JUN, which in turn are essential CC for IL2 production, and participates in the calcium-dependent NFATC1 CC and NFATC2 transactivation. Mediates the activation of the canonical CC NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on CC several serine residues, inducing CARD11 association with lipid rafts CC and recruitment of the BCL10-MALT1 complex, which then activates IKK CC complex, resulting in nuclear translocation and activation of NFKB1. CC May also play an indirect role in activation of the non-canonical NF- CC kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN CC activation, acts by phosphorylating the mediator STK39/SPAK and may not CC act through MAP kinases signaling. Plays a critical role in TCR/CD28- CC induced NFATC1 and NFATC2 transactivation by participating in the CC regulation of reduced inositol 1,4,5-trisphosphate generation and CC intracellular calcium mobilization. After costimulation of T-cells CC through CD28 can phosphorylate CBLB and is required for the CC ubiquitination and subsequent degradation of CBLB, which is a CC prerequisite for the activation of TCR. During T-cells differentiation, CC plays an important role in the development of T-helper 2 (Th2) cells CC following immune and inflammatory responses, and, in the development of CC inflammatory autoimmune diseases, is necessary for the activation of CC IL17-producing Th17 cells. May play a minor role in Th1 response. Upon CC TCR stimulation, mediates T-cell protective survival signal by CC phosphorylating BAD, thus protecting T-cells from BAD-induced CC apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF- CC kappa-B and JUN pathways. In platelets, regulates signal transduction CC downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors, CC playing a positive role in 'outside-in' signaling and granule secretion CC signal transduction. May relay signals from the activated ITGA2B CC receptor by regulating the uncoupling of WASP and WIPF1, thereby CC permitting the regulation of actin filament nucleation and branching CC activity of the Arp2/3 complex. May mediate inhibitory effects of free CC fatty acids on insulin signaling by phosphorylating IRS1, which in turn CC blocks IRS1 tyrosine phosphorylation and downstream activation of the CC PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of CC phosphatidylglycerol or phosphatidylinositol (By similarity). CC Phosphorylates PDPK1 at 'Ser-504' and 'Ser-532' and negatively CC regulates its ability to phosphorylate PKB/AKT1 (By similarity). CC Phosphorylates CCDC88A/GIV and inhibits its guanine nucleotide exchange CC factor activity (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:Q04759, ECO:0000269|PubMed:9516463}. 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=2.7.11.13; CC Evidence={ECO:0000250|UniProtKB:Q04759}; 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=2.7.11.13; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- ACTIVITY REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are CC calcium-insensitive, but activated by diacylglycerol (DAG) and CC phosphatidylserine. Three specific sites; Thr-538 (activation loop of CC the kinase domain), Ser-676 (turn motif) and Ser-695 (hydrophobic CC region), need to be phosphorylated for its full activation (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Part of a membrane raft complex composed at least of BCL10, CC CARD11, MALT1 and IKBKB (By similarity). Interacts with GLRX3 (via N- CC terminus) (PubMed:18479680). Interacts with ECT2 (By similarity). CC Interacts with CCDC88A/GIV; the interaction leads to phosphorylation of CC CCDC88A and inhibition of its guanine nucleotide exchange factor CC activity (By similarity). {ECO:0000250|UniProtKB:Q04759, CC ECO:0000269|PubMed:18479680}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane CC {ECO:0000250}; Peripheral membrane protein. Note=In resting T-cells, CC mostly localized in cytoplasm. In response to TCR stimulation, CC associates with lipid rafts and then localizes in the immunological CC synapse (By similarity). {ECO:0000250}. CC -!- DOMAIN: The C1 domain, containing the phorbol ester/DAG-type region 1 CC (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a CC non-calcium binding domain. CC -!- PTM: Autophosphorylation at Thr-219 is required for targeting to the CC TCR and cellular function of PRKCQ upon antigen receptor ligation. CC Following TCR stimulation, phosphorylated at Tyr-90 and Ser-685 (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. PKC subfamily. {ECO:0000305}. 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 AlphaFoldDB; Q9WTQ0; -. DR SMR; Q9WTQ0; -. DR IntAct; Q9WTQ0; 2. DR STRING; 10116.ENSRNOP00000025902; -. DR BindingDB; Q9WTQ0; -. DR ChEMBL; CHEMBL2094266; -. DR DrugCentral; Q9WTQ0; -. DR iPTMnet; Q9WTQ0; -. DR PhosphoSitePlus; Q9WTQ0; -. DR PaxDb; Q9WTQ0; -. DR UCSC; RGD:620968; rat. DR RGD; 620968; Prkcq. DR eggNOG; KOG0694; Eukaryota. DR InParanoid; Q9WTQ0; -. DR PhylomeDB; Q9WTQ0; -. DR Reactome; R-RNO-111465; Apoptotic cleavage of cellular proteins. DR Reactome; R-RNO-114508; Effects of PIP2 hydrolysis. DR Reactome; R-RNO-202424; Downstream TCR signaling. DR Reactome; R-RNO-2871837; FCERI mediated NF-kB activation. DR Reactome; R-RNO-373752; Netrin-1 signaling. DR Reactome; R-RNO-9648002; RAS processing. DR PRO; PR:Q9WTQ0; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005737; C:cytoplasm; IDA:RGD. DR GO; GO:0001772; C:immunological synapse; ISO:RGD. DR GO; GO:0016020; C:membrane; IDA:RGD. DR GO; GO:0031594; C:neuromuscular junction; IDA:RGD. DR GO; GO:0005634; C:nucleus; IDA:RGD. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0042383; C:sarcolemma; IDA:RGD. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein kinase activity; ISO:RGD. DR GO; GO:0004697; F:protein kinase C activity; ISO:RGD. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD. DR GO; GO:0007568; P:aging; IEP:RGD. DR GO; GO:0035739; P:CD4-positive, alpha-beta T cell proliferation; ISO:RGD. DR GO; GO:0060326; P:cell chemotaxis; ISO:RGD. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0035556; P:intracellular signal transduction; IDA:RGD. DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISO:RGD. DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0070233; P:negative regulation of T cell apoptotic process; ISS:UniProtKB. DR GO; GO:0030182; P:neuron differentiation; IEP:RGD. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central. DR GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; ISO:RGD. DR GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:RGD. DR GO; GO:0032740; P:positive regulation of interleukin-17 production; ISS:UniProtKB. DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:RGD. DR GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB. DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:RGD. DR GO; GO:0050714; P:positive regulation of protein secretion; IDA:RGD. DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:RGD. DR GO; GO:0050870; P:positive regulation of T cell activation; ISS:UniProtKB. DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD. DR GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; ISS:UniProtKB. DR GO; GO:2000570; P:positive regulation of T-helper 2 cell activation; ISS:UniProtKB. DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:RGD. DR GO; GO:1904355; P:positive regulation of telomere capping; ISO:RGD. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:RGD. DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD. DR GO; GO:0006355; P:regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:RGD. DR GO; GO:0090330; P:regulation of platelet aggregation; ISS:UniProtKB. DR GO; GO:0019229; P:regulation of vasoconstriction; IEP:RGD. DR GO; GO:0045730; P:respiratory burst; IEP:RGD. DR GO; GO:0009749; P:response to glucose; IEP:RGD. DR GO; GO:0009408; P:response to heat; IEP:RGD. DR GO; GO:0001666; P:response to hypoxia; IEP:RGD. DR GO; GO:0032868; P:response to insulin; IEP:RGD. DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD. DR GO; GO:0042110; P:T cell activation; ISO:RGD. DR GO; GO:0042246; P:tissue regeneration; IEP:RGD. DR CDD; cd00029; C1; 2. DR CDD; cd05619; STKc_nPKC_theta; 1. DR Gene3D; 2.60.40.150; -; 1. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR046349; C1-like_sf. DR InterPro; IPR000008; C2_dom. DR InterPro; IPR035892; C2_domain_sf. DR InterPro; IPR020454; DAG/PE-bd. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR034668; nPKC_theta. DR InterPro; IPR002219; PE/DAG-bd. DR InterPro; IPR027264; PKC_theta. DR InterPro; IPR017892; Pkinase_C. DR InterPro; IPR014376; Prot_kin_PKC_delta. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00130; C1_1; 2. DR Pfam; PF00069; Pkinase; 1. DR Pfam; PF00433; Pkinase_C; 1. DR PIRSF; PIRSF000551; PKC_delta; 1. DR PIRSF; PIRSF501105; Protein_kin_C_theta; 1. DR PRINTS; PR00008; DAGPEDOMAIN. DR SMART; SM00109; C1; 2. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF49562; SSF49562; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR SUPFAM; SSF57889; SSF57889; 2. DR PROSITE; PS51285; AGC_KINASE_CTER; 1. DR PROSITE; PS50004; C2; 1. 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 1: Evidence at protein level; KW ATP-binding; Cell membrane; Cytoplasm; Immunity; Inflammatory response; KW Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Repeat; KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger. FT CHAIN 1..707 FT /note="Protein kinase C theta type" FT /id="PRO_0000270836" FT DOMAIN 1..107 FT /note="C2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041" FT DOMAIN 380..634 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 635..706 FT /note="AGC-kinase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618" FT ZN_FING 159..209 FT /note="Phorbol-ester/DAG-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226" FT ZN_FING 231..281 FT /note="Phorbol-ester/DAG-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226" FT ACT_SITE 504 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 386..394 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 409 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 90 FT /note="Phosphotyrosine; by LCK" FT /evidence="ECO:0000250|UniProtKB:Q04759" FT MOD_RES 219 FT /note="Phosphothreonine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q04759" FT MOD_RES 348 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q04759" FT MOD_RES 538 FT /note="Phosphothreonine; by PDPK1" FT /evidence="ECO:0000250|UniProtKB:Q04759" FT MOD_RES 676 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT MOD_RES 685 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q04759" FT MOD_RES 695 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:Q04759, ECO:0000255" 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 //