MPRIP_MOUSE
ID MPRIP_MOUSE Reviewed; 1024 AA.
AC P97434; Q3TBR5; Q3TC85; Q3TRS0; Q3U1Y8; Q3U3E4; Q5SWZ3; Q5SWZ4; Q5SWZ7;
AC Q6P559; Q80YC8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Myosin phosphatase Rho-interacting protein;
DE AltName: Full=Rho-interacting protein 3;
DE Short=RIP3;
DE AltName: Full=p116Rip;
GN Name=Mprip; Synonyms=Kiaa0864, Mrip, Rhoip3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INTERACTION
RP WITH RHOA.
RC TISSUE=Brain;
RX PubMed=9199174; DOI=10.1083/jcb.137.7.1603;
RA Gebbink M.F.B.G., Kranenburg O., Poland M., van Horck F.P.G., Houssa B.,
RA Moolenaar W.H.;
RT "Identification of a novel, putative Rho-specific GDP/GTP exchange factor
RT and a RhoA-binding protein: control of neuronal morphology.";
RL J. Cell Biol. 137:1603-1613(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 114-1024 (ISOFORM 5).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 11-1024 (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH F-ACTIN.
RX PubMed=12732640; DOI=10.1074/jbc.m302399200;
RA Mulder J., Poland M., Gebbink M.F.G.B., Calafat J., Moolenaar W.H.,
RA Kranenburg O.;
RT "p116Rip is a novel filamentous actin-binding protein.";
RL J. Biol. Chem. 278:27216-27223(2003).
RN [6]
RP FUNCTION, INTERACTION WITH PPP1R12A AND PPP1R12C, AND MUTAGENESIS OF
RP LEU-857; LEU-905 AND ILE-919.
RX PubMed=15469989; DOI=10.1091/mbc.e04-04-0275;
RA Mulder J., Ariaens A., van den Boomen D., Moolenaar W.H.;
RT "p116Rip targets myosin phosphatase to the actin cytoskeleton and is
RT essential for RhoA/ROCK-regulated neuritogenesis.";
RL Mol. Biol. Cell 15:5516-5527(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219; SER-221; SER-225;
RP SER-227; SER-289; SER-364; SER-617; SER-976; SER-1013 AND SER-1015,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1015 (ISOFORM 2),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979 (ISOFORM 3), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP INTERACTION WITH MYZAP.
RX PubMed=20093627; DOI=10.1161/circresaha.109.213256;
RA Seeger T.S., Frank D., Rohr C., Will R., Just S., Grund C., Lyon R.,
RA Luedde M., Koegl M., Sheikh F., Rottbauer W., Franke W.W., Katus H.A.,
RA Olson E.N., Frey N.;
RT "Myozap, a novel intercalated disc protein, activates serum response
RT factor-dependent signaling and is required to maintain cardiac function in
RT vivo.";
RL Circ. Res. 106:880-890(2010).
CC -!- FUNCTION: Targets myosin phosphatase to the actin cytoskeleton.
CC Required for the regulation of the actin cytoskeleton by RhoA and
CC ROCK1. Depletion leads to an increased number of stress fibers in
CC smooth muscle cells through stabilization of actin fibers by
CC phosphorylated myosin. Overexpression of MRIP as well as its F-actin-
CC binding region leads to disassembly of stress fibers in neuronal cells.
CC {ECO:0000269|PubMed:12732640, ECO:0000269|PubMed:15469989}.
CC -!- SUBUNIT: Binds RHOA, PPP1R12A/MBS and PPP1R12C/MBS85 through adjacent
CC coiled coil domains. Interacts with MYZAP. Binds F-actin through its N-
CC terminus. {ECO:0000269|PubMed:12732640, ECO:0000269|PubMed:15469989,
CC ECO:0000269|PubMed:20093627, ECO:0000269|PubMed:9199174}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12732640}. Note=Colocalizes with F-actin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P97434-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97434-2; Sequence=VSP_017293;
CC Name=3;
CC IsoId=P97434-3; Sequence=VSP_017292, VSP_017293;
CC Name=4;
CC IsoId=P97434-4; Sequence=VSP_017290;
CC Name=5;
CC IsoId=P97434-5; Sequence=VSP_017291;
CC -!- TISSUE SPECIFICITY: Expressed in Kidney, Brain, Heart and Lung.
CC {ECO:0000269|PubMed:9199174}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE36957.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U73200; AAB18198.1; -; mRNA.
DR EMBL; AK154807; BAE32843.1; -; mRNA.
DR EMBL; AK155630; BAE33355.1; -; mRNA.
DR EMBL; AK158296; BAE34450.1; -; mRNA.
DR EMBL; AK162530; BAE36957.1; ALT_INIT; mRNA.
DR EMBL; AK170849; BAE42072.1; -; mRNA.
DR EMBL; AK171089; BAE42242.1; -; mRNA.
DR EMBL; AL596204; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049803; AAH49803.1; -; mRNA.
DR EMBL; BC063067; AAH63067.1; -; mRNA.
DR CCDS; CCDS24774.1; -. [P97434-2]
DR CCDS; CCDS24775.1; -. [P97434-1]
DR PIR; T30868; T30868.
DR RefSeq; NP_036157.2; NM_012027.2. [P97434-1]
DR RefSeq; NP_957697.1; NM_201245.3. [P97434-2]
DR RefSeq; XP_006533503.1; XM_006533440.1. [P97434-3]
DR AlphaFoldDB; P97434; -.
DR SMR; P97434; -.
DR BioGRID; 205073; 13.
DR IntAct; P97434; 12.
DR MINT; P97434; -.
DR STRING; 10090.ENSMUSP00000112072; -.
DR iPTMnet; P97434; -.
DR PhosphoSitePlus; P97434; -.
DR EPD; P97434; -.
DR jPOST; P97434; -.
DR MaxQB; P97434; -.
DR PaxDb; P97434; -.
DR PeptideAtlas; P97434; -.
DR PRIDE; P97434; -.
DR ProteomicsDB; 291497; -. [P97434-1]
DR ProteomicsDB; 291498; -. [P97434-2]
DR ProteomicsDB; 291499; -. [P97434-3]
DR ProteomicsDB; 291500; -. [P97434-4]
DR ProteomicsDB; 291501; -. [P97434-5]
DR Antibodypedia; 13293; 221 antibodies from 31 providers.
DR DNASU; 26936; -.
DR Ensembl; ENSMUST00000072031; ENSMUSP00000071914; ENSMUSG00000005417. [P97434-2]
DR Ensembl; ENSMUST00000108751; ENSMUSP00000104382; ENSMUSG00000005417. [P97434-4]
DR Ensembl; ENSMUST00000116371; ENSMUSP00000112072; ENSMUSG00000005417. [P97434-1]
DR GeneID; 26936; -.
DR KEGG; mmu:26936; -.
DR UCSC; uc007jen.2; mouse. [P97434-1]
DR UCSC; uc007jeo.2; mouse. [P97434-2]
DR UCSC; uc007jep.2; mouse. [P97434-4]
DR UCSC; uc011xvo.1; mouse. [P97434-5]
DR CTD; 23164; -.
DR MGI; MGI:1349438; Mprip.
DR VEuPathDB; HostDB:ENSMUSG00000005417; -.
DR eggNOG; KOG4807; Eukaryota.
DR GeneTree; ENSGT00940000155286; -.
DR HOGENOM; CLU_011327_0_0_1; -.
DR InParanoid; P97434; -.
DR OrthoDB; 428862at2759; -.
DR TreeFam; TF329258; -.
DR BioGRID-ORCS; 26936; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Mprip; mouse.
DR PRO; PR:P97434; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P97434; protein.
DR Bgee; ENSMUSG00000005417; Expressed in spermatid and 261 other tissues.
DR ExpressionAtlas; P97434; baseline and differential.
DR Genevisible; P97434; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0032507; P:maintenance of protein location in cell; ISO:MGI.
DR GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR CDD; cd13275; PH_M-RIP; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR039597; M-RIP_PH.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00169; PH; 2.
DR SMART; SM00233; PH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1024
FT /note="Myosin phosphatase Rho-interacting protein"
FT /id="PRO_0000223870"
FT DOMAIN 43..150
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 386..482
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..382
FT /note="Interaction with F-actin"
FT REGION 152..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..823
FT /note="Interaction with RHOA"
FT /evidence="ECO:0000269|PubMed:9199174"
FT REGION 823..878
FT /note="Interaction with PPP1R12A"
FT /evidence="ECO:0000250"
FT REGION 972..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 672..976
FT /evidence="ECO:0000255"
FT COMPBIAS 173..205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 295
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 492
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 617
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 645
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 976
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 992
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WCQ1"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1015
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 168..205
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017290"
FT VAR_SEQ 347..382
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_017292"
FT VAR_SEQ 402..409
FT /note="WKKHWFVL -> TQVPFLRTKIGTF (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017291"
FT VAR_SEQ 1016..1024
FT /note="VIEQVSWDN -> LKEGLTVQERLKLFESRDLKKD (in isoform 2
FT and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_017293"
FT MUTAGEN 857
FT /note="L->P: Loss of interaction with PPP1R12C and
FT PPP1R12A."
FT /evidence="ECO:0000269|PubMed:15469989"
FT MUTAGEN 905
FT /note="L->P: No effect."
FT /evidence="ECO:0000269|PubMed:15469989"
FT MUTAGEN 919
FT /note="I->P: Loss of interaction with PPP1R12C and
FT PPP1R12A."
FT /evidence="ECO:0000269|PubMed:15469989"
FT CONFLICT 43
FT /note="K -> E (in Ref. 2; BAE32843)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="Q -> R (in Ref. 2; BAE33355)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="S -> T (in Ref. 1; AAB18198)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="S -> P (in Ref. 2; BAE42242)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="S -> P (in Ref. 2; BAE32843)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="A -> T (in Ref. 2; BAE42242/BAE42072)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="R -> P (in Ref. 1; AAB18198)"
FT /evidence="ECO:0000305"
FT MOD_RES P97434-2:1015
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES P97434-3:979
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1024 AA; 116408 MW; 7BE3BFB89011ECC5 CRC64;
MSAAKENPCR KFQANIFNKS KCQNCFKPRE SHLLNDEDLT QAKPIYGGWL LLAPDGTDFD
NPVHRSRKWQ RRFFILYEHG LLRYALDEMP TTLPQGTINM NQCTDVVDGE ARTGQKFSLC
ILTPDKEHFI RAETKEIISG WLEMLMVYPR TNKQNQKKKR KVEPPTPQEP GPAKMAVTSS
SGGSSGSSSS IPSAEKVPTT KSTLWQEEMR AKDQPDGTSL SPAQSPSQSQ PPAACTPREP
GLESKEDEST ISGDRVDGGR KVRVESGYFS LEKAKQDLRA EEQLPPLLSP PSPSTPHSRR
SQVIEKFEAL DIEKAEHMET NMLILTTPSS DTRQGRSERR AIPRKRDFAS EAPTAPLSDA
CPLSPHRRAK SLDRRSTESS MTPDLLNFKK GWLTKQYEDG QWKKHWFVLA DQSLRYYRDS
VAEEAADLDG EINLSTCYDV TEYPVQRNYG FQIHTKEGEF TLSAMTSGIR RNWIQTIMKH
VLPASAPDVT SSLPEGKNKS TSFETCSRST EKQEAEPGEP DPEQKKSRAR ERRREGRSKT
FDWAEFRPIQ QALAQERASA VGSSDSGDPG CLEAEPGELE RERARRREER RKRFGMLDTI
DGPGMEDTAL RMDIDRSPGL LGTPDLKTQN VHVEIEQRWH QVETTPLREE KQVPIAPLHL
SLEDRSERLS THELTSLLEK ELEQSQKEAS DLLEQNRLLQ DQLRVALGRE QSAREGYVLQ
ATCERGFAAM EETHQKKIED LQRQHQRELE KLREEKDRLL AEETAATISA IEAMKNAHRE
EMERELEKSQ RSQISSINSD IEALRRQYLE ELQSVQRELE VLSEQYSQKC LENAHLAQAL
EAERQALRQC QRENQELNAH NQELNNRLAA EITRLRTLLT GDGGGESTGL PLTQGKDAYE
LEVLLRVKES EIQYLKQEIS SLKDELQTAL RDKKYASDKY KDIYTELSIA KAKADCDISR
LKEQLKAATE ALGEKSPEGT TVSGYDIMKS KSNPDFLKKD RSCVTRQLRN IRSKSVIEQV
SWDN
