RIPK3_RAT
ID RIPK3_RAT Reviewed; 478 AA.
AC Q9Z2P5; B0BMV6;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Receptor-interacting serine/threonine-protein kinase 3 {ECO:0000305};
DE EC=2.7.11.1;
DE AltName: Full=Homocysteine respondent protein HCYP2 {ECO:0000303|PubMed:15057822};
DE AltName: Full=RIP-like protein kinase 3 {ECO:0000250|UniProtKB:Q9QZL0};
DE AltName: Full=Receptor-interacting protein 3 {ECO:0000250|UniProtKB:Q9QZL0};
DE Short=RIP-3 {ECO:0000250|UniProtKB:Q9QZL0};
GN Name=Ripk3 {ECO:0000312|RGD:628899};
GN Synonyms=Rip3 {ECO:0000250|UniProtKB:Q9QZL0};
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 [MRNA].
RC STRAIN=Wistar Kyoto;
RA Chen K.H., Tang J.;
RT "A homocysteine-respondent gene cloned from WKY VSMCs by differential
RT display.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY 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: Serine/threonine-protein kinase that activates necroptosis
CC and apoptosis, two parallel forms of cell death. Necroptosis, a
CC programmed cell death process in response to death-inducing TNF-alpha
CC family members, is triggered by RIPK3 following activation by ZBP1.
CC Activated RIPK3 forms a necrosis-inducing complex and mediates
CC phosphorylation of MLKL, promoting MLKL localization to the plasma
CC membrane and execution of programmed necrosis characterized by calcium
CC influx and plasma membrane damage. In addition to TNF-induced
CC necroptosis, necroptosis can also take place in the nucleus in response
CC to orthomyxoviruses infection: following ZBP1 activation, which senses
CC double-stranded Z-RNA structures, nuclear RIPK3 catalyzes
CC phosphorylation and activation of MLKL, promoting disruption of the
CC nuclear envelope and leakage of cellular DNA into the cytosol. Also
CC regulates apoptosis: apoptosis depends on RIPK1, FADD and CASP8, and is
CC independent of MLKL and RIPK3 kinase activity (By similarity).
CC Phosphorylates RIPK1: RIPK1 and RIPK3 undergo reciprocal auto- and
CC trans-phosphorylation (By similarity). In some cell types, also able to
CC restrict viral replication by promoting cell death-independent
CC responses. In response to flavivirus infection in neurons, promotes a
CC cell death-independent pathway that restricts viral replication:
CC together with ZBP1, promotes a death-independent transcriptional
CC program that modifies the cellular metabolism via up-regulation
CC expression of the enzyme ACOD1/IRG1 and production of the metabolite
CC itaconate. Itaconate inhibits the activity of succinate dehydrogenase,
CC generating a metabolic state in neurons that suppresses replication of
CC viral genomes (By similarity). RIPK3 binds to and enhances the activity
CC of three metabolic enzymes: GLUL, GLUD1, and PYGL. These metabolic
CC enzymes may eventually stimulate the tricarboxylic acid cycle and
CC oxidative phosphorylation, which could result in enhanced ROS
CC production (By similarity). {ECO:0000250|UniProtKB:Q9QZL0,
CC ECO:0000250|UniProtKB:Q9Y572}.
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:0000250|UniProtKB:Q9QZL0};
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:0000250|UniProtKB:Q9QZL0};
CC -!- ACTIVITY REGULATION: Activity is stimulated by ZBP1, which senses
CC double-stranded Z-RNA structures. RIPK3-dependent necroptosis is
CC inhibited by RIPK1: RIPK1 prevents the ZBP1-induced activation of RIPK3
CC via FADD-mediated recruitment of CASP8, which cleaves RIPK1 and limits
CC TNF-induced necroptosis. {ECO:0000250|UniProtKB:Q9QZL0}.
CC -!- SUBUNIT: Interacts (via RIP homotypic interaction motif) with RIPK1
CC (via RIP homotypic interaction motif); this interaction induces RIPK1
CC phosphorylation and formation of a RIPK1-RIPK3 necrosis-inducing
CC complex. Interacts with MLKL; the interaction is direct and triggers
CC necroptosis. Interacts with ZBP1 (via RIP homotypic interaction motif);
CC interaction with ZBP1 activates RIPK3, triggering necroptosis (By
CC similarity). Upon TNF-induced necrosis, the RIPK1-RIPK3 dimer further
CC interacts with PGAM5 and MLKL; the formation of this complex leads to
CC PGAM5 phosphorylation and increase in PGAM5 phosphatase activity. Binds
CC TRAF2 and is recruited to the TNFR-1 signaling complex. Interacts with
CC PYGL, GLUL and GLUD1; these interactions result in activation of these
CC metabolic enzymes. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and
CC XIAP/BIRC4. Interacts with ARHGEF2 (By similarity). Interacts with
CC PELI1 (via atypical FHA domain); the phosphorylated form at Thr-185
CC binds preferentially to PELI1 (By similarity). Interacts with BUB1B,
CC TRAF2 and STUB1 (By similarity). Interacts with CASP6 (By similarity).
CC Component of the AIM2 PANoptosome complex, a multiprotein complex that
CC drives inflammatory cell death (PANoptosis) (By similarity).
CC {ECO:0000250|UniProtKB:Q9QZL0, ECO:0000250|UniProtKB:Q9Y572}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9QZL0}. Nucleus {ECO:0000250|UniProtKB:Q9QZL0}.
CC Note=Mainly cytoplasmic. Present in the nucleus in response to
CC influenza A virus (IAV) infection. {ECO:0000250|UniProtKB:Q9QZL0}.
CC -!- DOMAIN: The RIP homotypic interaction motif (RHIM) mediates interaction
CC with the RHIM motif of RIPK1. Both motifs form a hetero-amyloid
CC serpentine fold, stabilized by hydrophobic packing and featuring an
CC unusual Cys-Ser ladder of alternating Ser (from RIPK1) and Cys (from
CC RIPK3). {ECO:0000250|UniProtKB:Q9Y572}.
CC -!- PTM: RIPK1 and RIPK3 undergo reciprocal auto- and trans-
CC phosphorylation. Autophosphorylated following interaction with ZBP1.
CC Phosphorylation of Ser-201 plays a role in the necroptotic function of
CC RIPK3. Autophosphorylates at Thr-228 and Ser-229 following activation
CC by ZBP1: phosphorylation at these sites is a hallmark of necroptosis
CC and is required for binding MLKL. Phosphorylation at Thr-185 is
CC important for its kinase activity, interaction with PELI1 and for its
CC ability to mediate TNF-induced necroptosis (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y572}.
CC -!- PTM: Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by
CC BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B.
CC Ubiquitinated by STUB1 leading to its subsequent proteasome-dependent
CC degradation. {ECO:0000250|UniProtKB:Q9Y572}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AF036537; AAD02059.2; -; mRNA.
DR EMBL; AABR06083269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474049; EDM14285.1; -; Genomic_DNA.
DR EMBL; CH474049; EDM14286.1; -; Genomic_DNA.
DR EMBL; BC158580; AAI58581.1; -; mRNA.
DR RefSeq; NP_647558.1; NM_139342.1.
DR AlphaFoldDB; Q9Z2P5; -.
DR SMR; Q9Z2P5; -.
DR IntAct; Q9Z2P5; 1.
DR MINT; Q9Z2P5; -.
DR STRING; 10116.ENSRNOP00000027759; -.
DR iPTMnet; Q9Z2P5; -.
DR PhosphoSitePlus; Q9Z2P5; -.
DR PaxDb; Q9Z2P5; -.
DR GeneID; 246240; -.
DR KEGG; rno:246240; -.
DR UCSC; RGD:628899; rat.
DR CTD; 11035; -.
DR RGD; 628899; Ripk3.
DR VEuPathDB; HostDB:ENSRNOG00000020465; -.
DR eggNOG; KOG0192; Eukaryota.
DR HOGENOM; CLU_559689_0_0_1; -.
DR InParanoid; Q9Z2P5; -.
DR OMA; PFRNQMP; -.
DR OrthoDB; 769579at2759; -.
DR TreeFam; TF106506; -.
DR Reactome; R-RNO-3295583; TRP channels.
DR Reactome; R-RNO-5213460; RIPK1-mediated regulated necrosis.
DR Reactome; R-RNO-5675482; Regulation of necroptotic cell death.
DR PRO; PR:Q9Z2P5; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Proteomes; UP000234681; Chromosome 15.
DR Bgee; ENSRNOG00000020465; Expressed in spleen and 18 other tissues.
DR Genevisible; Q9Z2P5; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0004704; F:NF-kappaB-inducing kinase activity; ISO:RGD.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:1990000; P:amyloid fibril formation; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:RGD.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0097528; P:execution phase of necroptosis; ISS:UniProtKB.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0048535; P:lymph node development; ISS:UniProtKB.
DR GO; GO:0070266; P:necroptotic process; ISS:UniProtKB.
DR GO; GO:0097527; P:necroptotic signaling pathway; ISO:RGD.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0051351; P:positive regulation of ligase activity; ISO:RGD.
DR GO; GO:0060545; P:positive regulation of necroptotic process; ISS:UniProtKB.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; ISO:RGD.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:RGD.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; ISO:RGD.
DR GO; GO:0010922; P:positive regulation of phosphatase activity; ISO:RGD.
DR GO; GO:0090312; P:positive regulation of protein deacetylation; ISO:RGD.
DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0097300; P:programmed necrotic cell death; ISO:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0046006; P:regulation of activated T cell proliferation; ISS:UniProtKB.
DR GO; GO:0070235; P:regulation of activation-induced cell death of T cells; ISS:UniProtKB.
DR GO; GO:0002819; P:regulation of adaptive immune response; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:2000452; P:regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation; ISS:UniProtKB.
DR GO; GO:0032649; P:regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0001914; P:regulation of T cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0048536; P:spleen development; ISS:UniProtKB.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISS:UniProtKB.
DR GO; GO:0043029; P:T cell homeostasis; ISS:UniProtKB.
DR GO; GO:0048538; P:thymus development; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR025735; RHIM_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF12721; RHIM; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Apoptosis; ATP-binding; Cytoplasm; Kinase; Methylation; Necrosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..478
FT /note="Receptor-interacting serine/threonine-protein kinase
FT 3"
FT /id="PRO_0000086612"
FT DOMAIN 22..290
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 311..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 437..461
FT /note="RIP homotypic interaction motif (RHIM)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y572"
FT COMPBIAS 373..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZL0"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZL0"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y572"
FT MOD_RES 201
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9Y572"
FT MOD_RES 228
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZL0"
FT MOD_RES 229
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9Y572"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZL0"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZL0"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZL0"
FT MOD_RES 335
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZL0"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZL0"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZL0"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZL0"
FT MOD_RES 392
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZL0"
FT MOD_RES 474
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZL0"
FT CONFLICT 153
FT /note="P -> L (in Ref. 1; AAD02059)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 52218 MW; 87C83BFD16287136 CRC64;
MSSVKLWLNG ASSISLVGSE ELENLGFVGK GGFGAVFRAR HTAWNLDVAV KIVNSKKISR
EVKAMVNLRH ENVLLLLGVT ENLEWDYVYG PALVTGFMEN GSLSGLLQPS CPRPWPLLCR
LLEEVVLGMC YLHSLNPSLL HRDLKPSNVL LDPELHAKLA DFGLSTFQGG SQSGSGSGSR
DSGGTLAYLA PELLDNDGKA SKASDVYSFG VLVWTVLAGR EAEVVDKTSL IRGAVCNRQR
RPPLTELPPD SPETPGLEGL KELMTHCWSS EPKDRPSFQD CESKTNNVYI LVQDKVDAAV
SKVKHYLSQY RSSDTKLSAR ESSQKGTEVD CPRETIVYEM LDRLHLEEPS GSVPERLTSL
TERRGKEASF GHATPAGTSS DTLAGTPQIP HTLPSRGTTP RPAFTETPGP DPQRNQGDGR
NSNPWYTWNA PNPMTGLQSI VLNNCSEVQI GQHNCMSVQP RTAFPKKEPA QFGRGRGW
