PDLI5_MOUSE
ID PDLI5_MOUSE Reviewed; 591 AA.
AC Q8CI51; Q3UGD0; Q9QYN0; Q9QYN1; Q9QYN2;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=PDZ and LIM domain protein 5 {ECO:0000305};
DE AltName: Full=Enigma homolog {ECO:0000303|PubMed:10833443};
DE AltName: Full=Enigma-like PDZ and LIM domains protein {ECO:0000303|PubMed:10833443};
GN Name=Pdlim5 {ECO:0000312|MGI:MGI:1927489};
GN Synonyms=Enh {ECO:0000303|PubMed:10833443};
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] (ISOFORMS 1; 2 AND 3).
RC STRAIN=129/SvJ;
RX PubMed=10833443; DOI=10.1006/bbrc.2000.2787;
RA Nakagawa N., Hoshijima M., Oyasu M., Saito N., Tanizawa K., Kuroda S.;
RT "ENH, containing PDZ and LIM domains, heart/skeletal muscle-specific
RT protein, associates with cytoskeletal proteins through the PDZ domain.";
RL Biochem. Biophys. Res. Commun. 272:505-512(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 MRNA] (ISOFORM 1).
RC STRAIN=FVB/N;
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 [4]
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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-316 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-102; SER-105 AND SER-218 (ISOFORM 3), AND IDENTIFICATION
RP 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-89 AND LYS-350, SUCCINYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-89, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP STRUCTURE BY NMR OF 5-94.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PDZ domain of enigma homologue protein.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: May play an important role in the heart development by
CC scaffolding PKC to the Z-disk region. May play a role in the regulation
CC of cardiomyocyte expansion. Isoforms lacking the LIM domains may
CC negatively modulate the scaffolding activity of isoform 1.
CC Overexpression promotes the development of heart hypertrophy.
CC Contributes to the regulation of dendritic spine morphogenesis in
CC neurons. May be required to restrain postsynaptic growth of excitatory
CC synapses. Isoform 1, but not isoform 2, expression favors spine
CC thinning and elongation. {ECO:0000250|UniProtKB:Q62920}.
CC -!- SUBUNIT: Interacts with various PKC isoforms through the LIM domains.
CC Interacts with actin and alpha-actinin through the PDZ domain.
CC Interacts (via LIM domains) with SIPA1L1/SPAR; this interaction may
CC occur preferentially with isoform 1. {ECO:0000250|UniProtKB:Q62920}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic density
CC {ECO:0000250|UniProtKB:Q62920}. Presynapse
CC {ECO:0000250|UniProtKB:Q62920}. Postsynapse
CC {ECO:0000250|UniProtKB:Q62920}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q62920}. Note=Detected both at presynaptic and
CC postsynaptic sites, exclusively at excitatory synapses, but not
CC inhibitory synapses, in hippocampal neurons.
CC {ECO:0000250|UniProtKB:Q62920}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=ENH1;
CC IsoId=Q8CI51-1; Sequence=Displayed;
CC Name=2; Synonyms=ENH2;
CC IsoId=Q8CI51-2; Sequence=VSP_010469, VSP_010470;
CC Name=3; Synonyms=ENH3;
CC IsoId=Q8CI51-3; Sequence=VSP_010467, VSP_010468, VSP_010469,
CC VSP_010470;
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DR EMBL; AB016586; BAA88827.1; -; mRNA.
DR EMBL; AB016587; BAA88828.1; -; mRNA.
DR EMBL; AB016588; BAA88829.1; -; mRNA.
DR EMBL; AK147999; BAE28279.1; -; mRNA.
DR EMBL; BC037476; AAH37476.1; -; mRNA.
DR CCDS; CCDS17875.1; -. [Q8CI51-1]
DR CCDS; CCDS17876.1; -. [Q8CI51-2]
DR CCDS; CCDS38656.1; -. [Q8CI51-3]
DR RefSeq; NP_001177781.1; NM_001190852.1.
DR RefSeq; NP_001177783.1; NM_001190854.1.
DR RefSeq; NP_001177784.1; NM_001190855.1.
DR RefSeq; NP_001177785.1; NM_001190856.1.
DR RefSeq; NP_062782.2; NM_019808.3. [Q8CI51-1]
DR PDB; 1WF7; NMR; -; A=5-94.
DR PDBsum; 1WF7; -.
DR AlphaFoldDB; Q8CI51; -.
DR BMRB; Q8CI51; -.
DR SMR; Q8CI51; -.
DR BioGRID; 207938; 104.
DR IntAct; Q8CI51; 26.
DR MINT; Q8CI51; -.
DR STRING; 10090.ENSMUSP00000029941; -.
DR iPTMnet; Q8CI51; -.
DR PhosphoSitePlus; Q8CI51; -.
DR SwissPalm; Q8CI51; -.
DR EPD; Q8CI51; -.
DR jPOST; Q8CI51; -.
DR MaxQB; Q8CI51; -.
DR PaxDb; Q8CI51; -.
DR PeptideAtlas; Q8CI51; -.
DR PRIDE; Q8CI51; -.
DR ProteomicsDB; 288087; -. [Q8CI51-1]
DR ProteomicsDB; 288088; -. [Q8CI51-2]
DR ProteomicsDB; 288089; -. [Q8CI51-3]
DR Antibodypedia; 4614; 417 antibodies from 30 providers.
DR DNASU; 56376; -.
DR Ensembl; ENSMUST00000029941; ENSMUSP00000029941; ENSMUSG00000028273. [Q8CI51-1]
DR Ensembl; ENSMUST00000196908; ENSMUSP00000143098; ENSMUSG00000028273. [Q8CI51-2]
DR GeneID; 56376; -.
DR KEGG; mmu:56376; -.
DR UCSC; uc008rol.2; mouse. [Q8CI51-1]
DR UCSC; uc008ron.2; mouse. [Q8CI51-2]
DR CTD; 10611; -.
DR MGI; MGI:1927489; Pdlim5.
DR VEuPathDB; HostDB:ENSMUSG00000028273; -.
DR eggNOG; KOG1703; Eukaryota.
DR GeneTree; ENSGT00940000155292; -.
DR HOGENOM; CLU_038114_0_1_1; -.
DR InParanoid; Q8CI51; -.
DR OMA; QDTFVQR; -.
DR OrthoDB; 1013114at2759; -.
DR PhylomeDB; Q8CI51; -.
DR TreeFam; TF106408; -.
DR BioGRID-ORCS; 56376; 1 hit in 72 CRISPR screens.
DR EvolutionaryTrace; Q8CI51; -.
DR PRO; PR:Q8CI51; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8CI51; protein.
DR Bgee; ENSMUSG00000028273; Expressed in soleus muscle and 260 other tissues.
DR ExpressionAtlas; Q8CI51; baseline and differential.
DR Genevisible; Q8CI51; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0042805; F:actinin binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
DR GO; GO:0005080; F:protein kinase C binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0051963; P:regulation of synapse assembly; ISS:UniProtKB.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR031847; DUF4749.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF15936; DUF4749; 1.
DR Pfam; PF00412; LIM; 3.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00132; LIM; 3.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell projection;
KW Cytoplasm; Isopeptide bond; LIM domain; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Ubl conjugation; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT CHAIN 2..591
FT /note="PDZ and LIM domain protein 5"
FT /id="PRO_0000075878"
FT DOMAIN 2..85
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 413..472
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 472..531
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 531..591
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 121..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62920"
FT MOD_RES 89
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 89
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62920"
FT MOD_RES 350
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96HC4"
FT VAR_SEQ 98..206
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10833443"
FT /id="VSP_010467"
FT VAR_SEQ 237
FT /note="G -> GNPGTVKISPKR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10833443"
FT /id="VSP_010468"
FT VAR_SEQ 307..337
FT /note="NSTQEPSQQPASSGASPLSASEGPESPGSSR -> KEKIPLHVFSPKYTKLR
FT DWHHEVSARALNVQ (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10833443"
FT /id="VSP_010469"
FT VAR_SEQ 338..591
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10833443"
FT /id="VSP_010470"
FT CONFLICT 74
FT /note="T -> M (in Ref. 3; AAH37476)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="A -> T (in Ref. 1; BAA88827/BAA88829)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="E -> D (in Ref. 1; BAA88827/BAA88829)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="E -> K (in Ref. 1; BAA88827/BAA88829)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="R -> K (in Ref. 1; BAA88827/BAA88829)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="G -> R (in Ref. 1; BAA88827)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="S -> P (in Ref. 1; BAA88827)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="F -> Y (in Ref. 1; BAA88827)"
FT /evidence="ECO:0000305"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:1WF7"
FT STRAND 18..21
FT /evidence="ECO:0007829|PDB:1WF7"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:1WF7"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:1WF7"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:1WF7"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1WF7"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:1WF7"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:1WF7"
FT MOD_RES Q8CI51-2:316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8CI51-3:102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8CI51-3:105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8CI51-3:218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 591 AA; 63299 MW; E12B9EE1A3D97DC1 CRC64;
MSNYSVSLVG PAPWGFRLQG GKDFNMPLTI SSLKDGGKAS QAHVRIGDVV LSIDGISAQG
MTHLEAQNKI KACTGSLNMT LQRASAAAKS EPVSVQKGEP KEVVKPVPIT SPAVSKVTST
TNMAYNKAPR PFGSVSSPKV TSIPSPSSAF TPAHAATSSH ASPTPVAAAT PLHLSASGLH
VSANLSADQC SSPPNTGKPA VNVPRQPTVT SVCSESAQEL AEGQRRGSQG DIKQQNGPPR
KHIVERNTEF YHIPTHSDAS KKRLIEDTED WRPRTGTTQS RSFRILAQIT GTEHLTESEN
DNTKKANSTQ EPSQQPASSG ASPLSASEGP ESPGSSRPSV AGLRSAAAFK PVGSTSVKSP
SWQRPNQAAP STGRISNNAR SSGTGASVGP PQPSDQDTLV QRAEHIPAGK RTPMCAHCNQ
VIRGPFLVAL GKSWHPEEFN CAHCKNTMAY IGFVEEKGAL YCELCYEKFF APECGRCQRK
ILGEVINALK QTWHVSCFVC VACGKPIRNN VFHLEDGEPY CETDYYALFG TICRGCEFPI
EAGDMFLEAL GYTWHDTCFV CSVCCESLEG QTFFSKKDKP LCKKHAHSVN F
