PCLO_MOUSE
ID PCLO_MOUSE Reviewed; 5068 AA.
AC Q9QYX7; E9QK94; Q8CF91; Q8CF92; Q9QYX6; Q9QZJ0;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 4.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Protein piccolo {ECO:0000305};
DE AltName: Full=Aczonin {ECO:0000303|PubMed:10508862};
DE AltName: Full=Brain-derived HLMN protein;
DE AltName: Full=Multidomain presynaptic cytomatrix protein;
GN Name=Pclo {ECO:0000312|MGI:MGI:1349390};
GN Synonyms=Acz {ECO:0000303|PubMed:10508862};
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 {ECO:0000312|EMBL:CAB60731.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND INTERACTION WITH
RP PROFILIN.
RC TISSUE=Brain;
RX PubMed=10508862; DOI=10.1083/jcb.147.1.151;
RA Wang X., Kibschull M., Laue M.M., Lichte B., Petrasch-Parwez E.,
RA Kilimann M.W.;
RT "Aczonin, a 550-kd putative scaffolding protein of presynaptic active
RT zones, shares homology regions with rim and bassoon and binds profilin.";
RL J. Cell Biol. 147:151-162(1999).
RN [2] {ECO:0000305}
RP SEQUENCE REVISION.
RA Kilimann M.W.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP INTERACTION WITH RIMS2.
RX PubMed=12401793; DOI=10.1074/jbc.m210146200;
RA Fujimoto K., Shibasaki T., Yokoi N., Kashima Y., Matsumoto M., Sasaki T.,
RA Tajima N., Iwanaga T., Seino S.;
RT "Piccolo, a Ca2+ sensor in pancreatic beta-cells. Involvement of cAMP-
RT GEFII.Rim2.Piccolo complex in cAMP-dependent exocytosis.";
RL J. Biol. Chem. 277:50497-50502(2002).
RN [4]
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 [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4532-4712.
RC TISSUE=Brain;
RA Huang W., Jin W., Huang C., Chen B., Zhang J., Ju G.;
RT "Mus musculus brain-derived reactive mRNA.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1766; SER-3358 AND THR-3376,
RP AND 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 [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-2686 AND SER-2960.
RC TISSUE=Brain;
RX PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200;
RA Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A.,
RA Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A.,
RA Schoepfer R., Burlingame A.L.;
RT "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT preparations using lectin weak affinity chromatography and mass
RT spectrometry.";
RL Mol. Cell. Proteomics 5:923-934(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [10]
RP FUNCTION, INTERACTION WITH BCN, ERC2/CAST1, RIMS1 AND UNC13A, AND TISSUE
RP SPECIFICITY.
RX PubMed=19812333; DOI=10.1523/jneurosci.1255-09.2009;
RA Wang X., Hu B., Zieba A., Neumann N.G., Kasper-Sonnenberg M., Honsbein A.,
RA Hultqvist G., Conze T., Witt W., Limbach C., Geitmann M., Danielson H.,
RA Kolarow R., Niemann G., Lessmann V., Kilimann M.W.;
RT "A protein interaction node at the neurotransmitter release site: domains
RT of Aczonin/Piccolo, Bassoon, CAST, and rim converge on the N-terminal
RT domain of Munc13-1.";
RL J. Neurosci. 29:12584-12596(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-844; SER-856;
RP THR-860; THR-1120; SER-1292; SER-1302; SER-1303; SER-1332; SER-1334;
RP SER-1337; SER-1338; SER-1341; SER-1439; SER-1451; SER-1452; SER-1454;
RP SER-1457; SER-1481; SER-1484; THR-1552; SER-1553; SER-1563; SER-1575;
RP SER-1642; SER-1647; SER-1708; SER-1709; THR-1760; SER-1766; SER-1795;
RP SER-1800; SER-1808; SER-1829; SER-2495; THR-2998; SER-3372; THR-3376;
RP THR-3403; SER-3506; SER-3514; SER-3545; SER-3549; SER-3558; SER-3582;
RP SER-3610; SER-3616; SER-4016; SER-4042; SER-4132; SER-4286; SER-4290;
RP SER-4293; SER-4358 AND SER-4592, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28231469; DOI=10.1016/j.neuron.2017.01.026;
RA Okerlund N.D., Schneider K., Leal-Ortiz S., Montenegro-Venegas C.,
RA Kim S.A., Garner L.C., Waites C.L., Gundelfinger E.D., Reimer R.J.,
RA Garner C.C.;
RT "Bassoon Controls Presynaptic Autophagy through Atg5.";
RL Neuron 93:897-913(2017).
CC -!- FUNCTION: Scaffold protein of the presynaptic cytomatrix at the active
CC zone (CAZ) which is the place in the synapse where neurotransmitter is
CC released (PubMed:19812333). After synthesis, participates in the
CC formation of Golgi-derived membranous organelles termed Piccolo-Bassoon
CC transport vesicles (PTVs) that are transported along axons to sites of
CC nascent synaptic contacts (By similarity). At the presynaptic active
CC zone, regulates the spatial organization of synaptic vesicle cluster,
CC the protein complexes that execute membrane fusion and compensatory
CC endocytosis (By similarity). Organizes as well the readily releasable
CC pool of synaptic vesicles and safeguards a fraction of them to be not
CC immediately available for action potential-induced release (By
CC similarity). Functions also in processes other than assembly such as
CC the regulation of specific presynaptic protein ubiquitination by
CC interacting with SIAH1 or the regulation of presynaptic autophagy
CC (PubMed:28231469) (By similarity). Mediates also synapse to nucleus
CC communication leading to reconfiguration of gene expression by
CC associating with the transcriptional corepressor CTBP1 and by
CC subsequently reducing the size of its pool available for nuclear import
CC (By similarity). {ECO:0000250|UniProtKB:Q9JKS6,
CC ECO:0000269|PubMed:19812333, ECO:0000269|PubMed:28231469}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041};
CC -!- SUBUNIT: Interacts with BSN, ERC2/CAST1, RIMS1 and UNC13A
CC (PubMed:10508862, PubMed:12401793). Interacts (via C-terminus) with
CC TRIO (via N-terminus) (By similarity). Interacts with CTBP1 (By
CC similarity). Interacts with SIAH1; this interaction negatively
CC regulates SIAH1 E3 ligase activity (By similarity). Directly interacts
CC with GIT1 and GIT2 (By similarity). {ECO:0000250|UniProtKB:Q9JKS6,
CC ECO:0000269|PubMed:10508862, ECO:0000269|PubMed:12401793}.
CC -!- SUBCELLULAR LOCATION: Presynaptic active zone
CC {ECO:0000269|PubMed:10508862}. Note=Colocalizes with BSN in developing
CC axons. {ECO:0000250|UniProtKB:Q9JKS6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=L;
CC IsoId=Q9QYX7-1; Sequence=Displayed;
CC Name=2; Synonyms=S;
CC IsoId=Q9QYX7-2; Sequence=VSP_003928, VSP_003929;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Moderately expressed in
CC pituitary gland and pancreatic islets. Low levels found in stomach.
CC {ECO:0000269|PubMed:10508862, ECO:0000269|PubMed:12401793,
CC ECO:0000269|PubMed:19812333}.
CC -!- DOMAIN: C2 domain 1 is involved in binding calcium and phospholipids.
CC Calcium binds with low affinity but with high specificity and induces a
CC large conformational change. {ECO:0000250|UniProtKB:Q9JKS6}.
CC -!- DISRUPTION PHENOTYPE: Knockdown of both Bassoon/BSN and Piccolo/PCLO
CC leads to the formation of presynaptic autophagosomes.
CC {ECO:0000269|PubMed:28231469}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC53723.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Several sequence problems.; Evidence={ECO:0000305};
CC Sequence=BAC53724.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Several sequence problems.; Evidence={ECO:0000305};
CC Sequence=CAB60731.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=CAB60732.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; Y19185; CAB60731.2; ALT_SEQ; mRNA.
DR EMBL; Y19186; CAB60732.2; ALT_SEQ; mRNA.
DR EMBL; AB083477; BAC53723.1; ALT_SEQ; mRNA.
DR EMBL; AB083478; BAC53724.1; ALT_SEQ; mRNA.
DR EMBL; AC125043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC125533; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144625; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF181269; AAD55786.2; -; mRNA.
DR CCDS; CCDS51415.1; -. [Q9QYX7-1]
DR CCDS; CCDS59667.1; -. [Q9QYX7-2]
DR RefSeq; NP_001104266.1; NM_001110796.2. [Q9QYX7-2]
DR RefSeq; NP_036125.4; NM_011995.4. [Q9QYX7-1]
DR SMR; Q9QYX7; -.
DR BioGRID; 205033; 14.
DR IntAct; Q9QYX7; 3.
DR MINT; Q9QYX7; -.
DR STRING; 10090.ENSMUSP00000030691; -.
DR GlyGen; Q9QYX7; 2 sites.
DR iPTMnet; Q9QYX7; -.
DR PhosphoSitePlus; Q9QYX7; -.
DR EPD; Q9QYX7; -.
DR jPOST; Q9QYX7; -.
DR MaxQB; Q9QYX7; -.
DR PaxDb; Q9QYX7; -.
DR PeptideAtlas; Q9QYX7; -.
DR PRIDE; Q9QYX7; -.
DR ProteomicsDB; 289327; -. [Q9QYX7-1]
DR ProteomicsDB; 289328; -. [Q9QYX7-2]
DR Antibodypedia; 2812; 270 antibodies from 24 providers.
DR DNASU; 26875; -.
DR Ensembl; ENSMUST00000030691; ENSMUSP00000030691; ENSMUSG00000061601. [Q9QYX7-1]
DR Ensembl; ENSMUST00000182407; ENSMUSP00000138419; ENSMUSG00000061601. [Q9QYX7-2]
DR GeneID; 26875; -.
DR KEGG; mmu:26875; -.
DR UCSC; uc008wmh.3; mouse. [Q9QYX7-2]
DR UCSC; uc008wmi.2; mouse. [Q9QYX7-1]
DR CTD; 27445; -.
DR MGI; MGI:1349390; Pclo.
DR VEuPathDB; HostDB:ENSMUSG00000061601; -.
DR eggNOG; KOG2060; Eukaryota.
DR GeneTree; ENSGT00620000087961; -.
DR HOGENOM; CLU_000104_0_1_1; -.
DR InParanoid; Q9QYX7; -.
DR OMA; SHAHSGP; -.
DR OrthoDB; 15051at2759; -.
DR PhylomeDB; Q9QYX7; -.
DR BioGRID-ORCS; 26875; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Pclo; mouse.
DR PRO; PR:Q9QYX7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9QYX7; protein.
DR Bgee; ENSMUSG00000061601; Expressed in cingulate cortex and 150 other tissues.
DR ExpressionAtlas; Q9QYX7; baseline and differential.
DR Genevisible; Q9QYX7; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0044316; C:cone cell pedicle; ISO:MGI.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005798; C:Golgi-associated vesicle; ISO:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0060077; C:inhibitory synapse; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0048786; C:presynaptic active zone; ISO:MGI.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0097470; C:ribbon synapse; ISO:MGI.
DR GO; GO:0044317; C:rod spherule; ISO:MGI.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0030133; C:transport vesicle; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR GO; GO:0005522; F:profilin binding; IDA:UniProtKB.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; IDA:SynGO.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:MGI.
DR GO; GO:0030073; P:insulin secretion; IDA:MGI.
DR GO; GO:0048790; P:maintenance of presynaptic active zone structure; IC:SynGO.
DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; ISO:MGI.
DR GO; GO:1903423; P:positive regulation of synaptic vesicle recycling; ISO:MGI.
DR GO; GO:0099526; P:presynapse to nucleus signaling pathway; IMP:SynGO.
DR GO; GO:1904071; P:presynaptic active zone assembly; ISO:MGI.
DR GO; GO:0035418; P:protein localization to synapse; IGI:ParkinsonsUK-UCL.
DR GO; GO:0051036; P:regulation of endosome size; ISO:MGI.
DR GO; GO:0017157; P:regulation of exocytosis; IDA:MGI.
DR GO; GO:1904666; P:regulation of ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0050808; P:synapse organization; ISO:MGI.
DR GO; GO:0097091; P:synaptic vesicle clustering; IDA:SynGO.
DR GO; GO:0016080; P:synaptic vesicle targeting; NAS:UniProtKB.
DR CDD; cd15774; FYVE1_PCLO; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR042720; PCLO_FYVE1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR030629; Piccolo.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR008899; Znf_piccolo.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14113:SF6; PTHR14113:SF6; 3.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF05715; zf-piccolo; 2.
DR SMART; SM00239; C2; 2.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calcium/phospholipid-binding;
KW Cell projection; Glycoprotein; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..5068
FT /note="Protein piccolo"
FT /id="PRO_0000058251"
FT DOMAIN 4424..4518
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 4622..4751
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 4933..5058
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 532..556
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 997..1020
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..500
FT /note="10 X 10 AA tandem approximate repeats of P-A-K-P-Q-
FT P-Q-Q-P-X"
FT REGION 594..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1364..1803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2104..2126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2261..2377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3334..3443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3490..3556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3576..3679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3760..3797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4207..4231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4254..4273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4317..4339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4574..4620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4758..4834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4857..4891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..488
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..681
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1085
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1091..1114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1523..1537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1548..1588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1623
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1652..1675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1719..1760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1775..1789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2272..2289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2308..2331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2332..2366
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3334..3402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3411..3435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3493..3511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3611..3649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3657..3679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3783..3797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4208..4231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4581..4599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4763..4780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4798..4834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4857..4889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 4651
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4651
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4657
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4721
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4721
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4723
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4723
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4723
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4726
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4729
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4729
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 860
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1120
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 1507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 1552
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1553
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1638
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 1640
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 1642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1647
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1709
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1760
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1795
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1800
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1829
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2998
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087"
FT MOD_RES 3372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3376
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 3403
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3506
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3549
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 3558
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 3582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 3610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3616
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3763
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 4016
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 4042
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 4132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 4286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 4290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 4293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 4322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 4358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 4592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 4706
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT CARBOHYD 2686
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:16452088"
FT CARBOHYD 2960
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:16452088"
FT VAR_SEQ 4859..4863
FT /note="TKPTN -> SKRRK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10508862,
FT ECO:0000303|PubMed:12401793"
FT /id="VSP_003928"
FT VAR_SEQ 4864..5068
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10508862,
FT ECO:0000303|PubMed:12401793"
FT /id="VSP_003929"
FT CONFLICT 156
FT /note="D -> E (in Ref. 1; CAB60731/CAB60732)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="A -> S (in Ref. 1; CAB60731/CAB60732)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="H -> Q (in Ref. 1; CAB60731/CAB60732 and 3;
FT BAC53723/BAC53724)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="H -> Q (in Ref. 1; CAB60731/CAB60732 and 3;
FT BAC53723/BAC53724)"
FT /evidence="ECO:0000305"
FT CONFLICT 923
FT /note="P -> Q (in Ref. 1; CAB60731/CAB60732 and 3;
FT BAC53723/BAC53724)"
FT /evidence="ECO:0000305"
FT CONFLICT 951
FT /note="V -> A (in Ref. 1; CAB60731/CAB60732)"
FT /evidence="ECO:0000305"
FT CONFLICT 965
FT /note="P -> H (in Ref. 1; CAB60731/CAB60732)"
FT /evidence="ECO:0000305"
FT CONFLICT 1920
FT /note="Q -> P (in Ref. 1; CAB60731/CAB60732)"
FT /evidence="ECO:0000305"
FT CONFLICT 1931
FT /note="Q -> R (in Ref. 1; CAB60731/CAB60732)"
FT /evidence="ECO:0000305"
FT CONFLICT 2297
FT /note="L -> S (in Ref. 1; CAB60731/CAB60732)"
FT /evidence="ECO:0000305"
FT CONFLICT 2335..2346
FT /note="Missing (in Ref. 3; BAC53723/BAC53724)"
FT /evidence="ECO:0000305"
FT CONFLICT 2855
FT /note="E -> D (in Ref. 1; CAB60731/CAB60732)"
FT /evidence="ECO:0000305"
FT CONFLICT 4042
FT /note="S -> P (in Ref. 1; CAB60731/CAB60732)"
FT /evidence="ECO:0000305"
FT CONFLICT 4670..4678
FT /note="Missing (in Ref. 3; BAC53724)"
FT /evidence="ECO:0000305"
FT CONFLICT 5062
FT /note="M -> V (in Ref. 1; CAB60731/CAB60732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 5068 AA; 550834 MW; DBF54D47501AC79A CRC64;
MGNEASLEGE GLPEGLAAAA GGAGGSGSAL HPGIPAGMEA DLSQLSEEER RQIAAVMSRA
QGLPKGSVPA AAAESPSMHR KQELDSSQAP QQPGKPPDPG RPPQHGLSKS RTTDTFRSEQ
KLPGRSPSTI SLKESKSRTD FKEEYKSSMM PGFFSDVNPL SAVSSVVNKF NPFDLISDSE
AVQEETTKKQ KVAQKDQGKS EGITKPSLQQ PSPKLIPKQQ GPGKEVIPQD IPSKSVSSQQ
AEKTKPQAPG TAKPSQQSPA QTPAQQAKPV AQQPGPAKAT VQQPGPAKSP AQPAGTGKSP
AQPPVTAKPP AQQAGLEKTS LQQPGPKSLA QTPGQGKVPP GPAKSPAQQP GTAKLPAQQP
GPQTAAKVPG PTKTPAQLSG PGKTPAQQPG PTKPSPQQPI PAKPQPQQPV ATKPQPQQPA
PAKPQPQHPT PAKPQPQHPT PAKPQPQQPT PAKPQPQQPT PAKPQPQQPT PAKPQPQHPT
PAKPQPQQPG LGKPSAQQPS KSISQTVTGR PLQAPPTSAA QAPAQGLSKT ICPLCNTTEL
LLHTPEKANF NTCTECQSTV CSLCGFNPNP HLTEIKEWLC LNCQMQRALG GELAAIPSSP
QPTPKAASVQ PATASKSPVP SQQASPKKEL PSKQDSPKAP ESKKPPPLVK QPTLHGPTPA
TAPQPPVAEA LPKPAPPKKP SAALPEQAKA PVADVEPKQP KTTETLTDSP SSAAATSKPA
ILSSQVQAQA QVTTAPPLKT DSAKTSQSFP PTGDTITPLD SKAMPRPASD SKIVSHPGPT
SESKDPVQKK EEPKKAQTKV TPKPDTKPVP KGSPTPSGTR PTTGQATPQS QQPPKPPEQS
RRFSLNLGGI ADAPKSQPTT PQETVTGKLF GFGASIFSQA SNLISTAGQQ APHPQTGPAA
PSKQAPPPSQ TLAAQGPPKS TGPHPSAPAK TTAVKKETKG PAAENLEAKP VQAPTVKKAE
KDKKPPPGKV SKPPPTEPEK AVLAQKPDKT TKPKPACPLC RTELNVGSQD PPNFNTCTEC
KNQVCNLCGF NPTPHLTEIQ EWLCLNCQTQ RAISGQLGDM DKMPPASSGP KASPVPAPAE
PPPQKTPTAA HAKGKKKETE VKAETEKQIP EKETPSIEKT PPAVATDQKL EESEVTKSLV
SVLPEKKPSE EEKALPADKK EKKPPAAEAP PLEEKKPIPD DQKLPPDAKP SASEGEEKRD
LLKAHVQIPE EGPIGKVASL ACEGEQQPDT RPEDLPGATP QTLPKDRQKE SRDVTQPQAE
GTAKEGRGEP SKDRTEKEED KSDTSSSQQP KSPQGLSDTG YSSDGISGSL GEIPSLIPSD
EKDLLKGLKK DSFSQESSPS SPSDLAKLES TVLSILEAQA STLVGEKAEK KTQPQKVSPE
QPQDQQKTQT PSETRDISIS EEEIKESQEK KVTSKKDSAQ GFPSRKEHKE NPELVDDLSP
RRASYDSVED SSESENSPVA RRKRRTSIGS SSSEEYKQED SQGSGEDEDF IRKQIIEMSA
DEDASGSEDE EFIRSQLKEI GGVTESQKRE ETKGKGKSPA GKHRRLTRKS STSFDDDAGR
RHSWHDEDDE TFDESPELKF RETKSQESEE LVVAGGGGLR RFKTIELNST VTDKYSAESS
QKKTTLYFDE EPELEMESLT DSPEDRSRGE GSSSLHASSF TPGTSPTSVS SLDEDSDSSP
SHKKGESKQQ RKARHRSHGP LLPTIEDSSE EEELREEEEL LKEQEKQREL EQQQRKSSSK
KSKKDKDELR AQRRRERPKT PPSNLSPIED ASPTEELRQA AEMEELHRSS CSEYSPSIES
DPEGFEISPE KIIEVQKVYK LPTAVSLYSP TDEQSVMQKE GAQKALKSAE EMYEEMMHKP
HKYKAFPAAN ERDEVFEKEP LYGGMLIEDY IYESLVEDTY NGSVDGSLLT RQDEQNGFMQ
QRGREQKIRL QEQIYDDPMQ KITDLQKEFY ELESLHSIVP QEDIVSSSYI IPESHEIVDL
GSMVTSTSEE KKLLDADAAY EELMKRQQMQ VTDGSSLIQT TMGDDMAEST LDFDRVQDAS
LTSSILSGAS LTDSTSSATL SIPDVKITQH FSTEEFEDEY VTDYTREIQE IIAHESLILT
YSEPSESATS VPPSDTPSLT SSISSVCTTD SSSPVTTLDS LTTVYTEPAD VITKFKDSEE
ISSTYFPGSV IDYPEDIGVS LDRTITPESR TNADQIMISF PGIAPSITES VATKPERPQA
DTISTDLPIS EKELIKGKKE TGDGIILEVL DAYKDKREES EAELTKISLP ETGLAPTPSS
QTKEQPGSPH SVSGEILGQE KPTYRSPSGG LPVSTHPSKS HPFFRSSSLD ISAQPPPPPP
PPPPPPPPPP PPPPPPLPPA TSPKPPTYPK RKLAAAAPVA PTAIVTAHAD AIPTVEATAA
RRSNGLPATK ICAAAPPPVP PKPSSIPTGL VFTHRPEASK PPIAPKPAVP EIPVTTQKTT
DTCPKPTGLP LTSNMSLNLV TSADYKLPSP TSPLSPHSNK SSPRYSKSLM ETYVVITLPS
EPGTPTDSSA AQAITSWPLG SPPKDLVSLE TVFSVVPPMT STEIPSASQP TLYTSGALGT
FSVTPAVTAS LFQTVPTSLT QFLPAEASKP EVSAVSSAVP SVAPRSVSIP IPPEPLALDR
HQYKENGKLP LIGDAIDLRT IPKSEVKVTE KCMDLSASAM DVKRQTTANE VYRRQISAVQ
PSIINLSAAS SLGTPVTMDS KTVAVVTCTD TTIYTTGTES QVGIEHAVTS PLQLTTSKHT
ELQYRKPSSQ AFPMIRDEAP INLSLGPSTQ AVTLAVTKPV TVPPVGVTNG WTDSTISQGI
TDGEVVDLST SKSHRTVVTM DESTSNVVTK IIEDEEKPVD LTAGRRAVCC DMVYKLPFGR
SCTAQQPATT LPEDRFGYRD DHYQYDRSGP YGYRGIGGMK PSMSDTNLAE AGHFFYKSKN
AFDYSGGTEA AVDLTSGRVS TGEVMDYSSK TTGPYPETRQ VISGVGISTP QYSTARMTPP
PGPQYGVGSV LRSSNGVVYS SVATPIPSTF AITTQPGSIF STTVRDLSGI HTTDAITSLS
ALHQSQPMPR SYFITTGASE TDISVTSIDI NASLQTITME TLPAETMDSV PTLTTASEVF
SEVVGEESTL LIVPDEDKQQ QQLDLERELL ELEKIKQQRF AEELEWERQE IQRFREQEKI
MVQKKLEELQ SMKQHLLYQQ EEERQAQFMM RQETLAQQQL QLEQIQQLQQ QLHQQLEEQK
LRQIYQYNYE PSGTASPQTT TEQAILEGQY VATEGSQFWA TEDATTTAST VVAIEIPQSQ
GWYTVQSDGV TQYIAPPGIL STVSEIPLTD VVVKEEKQPK KRSSGAKVRG QYDEMGESMA
DDPRNLKKIV DSGVQTDDEE TADRTYASRR RRTKKSVDTS VQTDDEDQDE WDMPSRSRRK
ARTGKYGDST AEGDKTKPPS KVSSVAVQTV AEISVQTEPL GTIRTPSIRA RVDAKVEIIK
HISAPEKTYK GGSLGCQTET DPDTQSPPYM GATSPPKDKK RPTPLEIGYS SSHLRADPTV
QLAPSPPKSP KVLYSPISPL SPGHALEPAF VPYEKPLPDD ISPQKVLHPD MAKVPPASPK
TAKMMQRSMS DPKPLSPTAD ESSRAPFQYS EGFTAKGSQT TSGTQKKVKR TLPNPPPEEA
STGTQSTYST MGTASRRRMC RTNTMARAKI LQDIDRELDL VERESAKLRK KQAELDEEEK
EIDAKLRYLE MGINRRKEAL LKEREKRERA YLQGVAEDRD YMSDSEVSST RPSRVESQHG
IERPRTAPQT EFSQFIPPQT QTEAQLVPPT SPYTQYQYSS PALPTQAPTP YTQQSHFQQQ
TLYHQQVSPY QTQPTFQAVA TMSFTPQAQP TPTPQPSYQL PSQMMVIQQK PRQTTLYLEP
KITSTYEVIR NQPLMIAPVS TDNTYAVSHL GSKYNSLDLR IGLEERSSMA SSPISSISAD
SFYADIDHHT SRNYVLIDDI GDITKGTAAL SSAFSLHEKD LSKTDRLLRT TETRRSQEVT
DFLAPLQTSS RLHSYVKAEE DSMEDPYELK LLKHQIKQEF RRGTESLDHL AGLSHYYHAD
TSYRHFPKSE KYSISRLTLE KQAAKQLPAA ILYQKQSKHK KALIDPKMSK FSPIQESRDL
EPDYPTYLSS STSSIGGISS RARLLQDDIT FGLRKNITDQ QKFMGSSLGS GLGTLGNTIR
SALQDEADKP YSSGSRSRPS SRPSSVYGLD LSIKRDSSSS SLRLKAQEAE ALDVSFGHSS
SSARTKPTSL PISQSRGRIP IVAQNSEEES PLSPVGQPMG MARAAAGPLP PISADTRDQF
GSSHSLPEVQ QHMREESRTR GYDRDIAFIM DDFQHAMSDS EAYHLRREET DWFDKPRESR
LENGHGLDRK LPERLVHSRP LSQHQEQILQ MNGKTMHYIF PHARIKITRD SKDHTVSGNG
LGIRIVGGKE IPGHSGEIGA YIAKILPGGS AEHSGKLIEG MQVLEWNGIP LTSKTYEEVQ
SIINQQSGEA EICVRLDLNM LSDSENPQHL ELHEPPKVVD KAKSPGVDPK QLAAELQKVS
LQQSPLVMSS VVEKGAHAHS GPTSAGSSSV PSPGQPGSPS VSKKKHGGSK PTDVSKTASH
PITGEIQLQI NYDLGNLIIH ILQARNLVPR DNNGYSDPFV KVYLLPGRGQ VMVVQNASVE
YKRRTKYVQK SLNPEWNQTV IYKSISMEQL MKKTLEVTVW DYDRFSSNDF LGEVLIDLSS
TSHLDNTPRW YPLKEQTESI EHGKSHSSQN SQQSPKPSVI KSRSHGIFPD PSKDMQVPTI
EKSHSSPGSS KSSSEGHLRS HGPSRSQSKT SVAQTHLEDA GAAIAAAEAA VQQLRIQPTK
PTNHRPAETS VSTGSSGSSV GSGYSVDSEG SSCVAGEPNL LPIPRIGKMG QNGQDPVKQP
GMGAADTEAK TQVMGEIKLA LKKEMKTDGE QLIVEILQCR NITYKFKSPD HLPDLYVKIY
VINIATQKKV IKKKTRVCRH DREPSFNETF RFSLSPAGHS LQILLFSNGG KFMKKTLIGE
ACIWLDKVDL RKRIVNWHKL LMSPTQTH
