MAP1A_HUMAN
ID MAP1A_HUMAN Reviewed; 2803 AA.
AC P78559; O95643; Q12973; Q15882; Q9UJT4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 6.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Microtubule-associated protein 1A;
DE Short=MAP-1A;
DE AltName: Full=Proliferation-related protein p80;
DE Contains:
DE RecName: Full=MAP1A heavy chain;
DE Contains:
DE RecName: Full=MAP1 light chain LC2;
GN Name=MAP1A; Synonyms=MAP1L;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS LEU-72; SER-335;
RP THR-336; SER-353; SER-357; GLN-364; CYS-1650; SER-1690; PRO-1881; VAL-1912;
RP ARG-1938 AND TYR-2214.
RX PubMed=8812494; DOI=10.1006/geno.1996.0400;
RA Fink J.K., Jones S.M., Esposito C., Wilkowski J.;
RT "Human microtubule-associated protein 1a (MAP1A) gene: genomic
RT organization, cDNA sequence, and developmental- and tissue-specific
RT expression.";
RL Genomics 35:577-585(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1825.
RC TISSUE=Ovarian carcinoma;
RA Chen Z.C., Fadiel A., Naftolin F.;
RT "Identification of a novel protein (P80) in ovarian carcinoma cells.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 78-1687.
RC TISSUE=Brain;
RA Ohtani K., Rutherford T., Sakamoto H., Naftolin F.;
RT "Microtubule associated protein 1A (MAP1A) in human brain -- DNA sequence
RT and physiological role.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-419.
RC TISSUE=Fetal muscle;
RA Chiannilkulchai N., Pasturaud P., Richard I., Auffray C., Beckmann J.S.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1607-1883.
RC TISSUE=Brain;
RX PubMed=7629894; DOI=10.1002/jnr.490400613;
RA Fukuyama R., Rapoport S.I.;
RT "Brain-specific expression of human microtubule-associated protein 1A
RT (MAP1A) gene and its assignment to human chromosome 15.";
RL J. Neurosci. Res. 40:820-825(1995).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2022, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612; THR-616; SER-1326;
RP SER-1329 AND SER-2022, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP CLEAVAGE SITE.
RX PubMed=18419581; DOI=10.1042/bj20071449;
RA Zou B., Yan H., Kawasaki F., Ordway R.W.;
RT "MAP1 structural organization in Drosophila: in vivo analysis of FUTSCH
RT reveals heavy- and light-chain subunits generated by proteolytic processing
RT at a conserved cleavage site.";
RL Biochem. J. 414:63-71(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612; THR-616; SER-667;
RP SER-896; SER-1069; SER-1160; SER-1218; SER-1654; SER-1675; SER-1776;
RP SER-1791; SER-1797; SER-1801; SER-2022; SER-2104 AND SER-2449, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612 AND THR-616, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; THR-504; SER-526;
RP SER-527; SER-605; SER-612; THR-616; SER-644; SER-667; SER-787; SER-896;
RP SER-909; SER-986; SER-1069; SER-1172; SER-1190; SER-1200; SER-1203;
RP SER-1218; SER-1326; SER-1600; SER-1626; SER-1675; SER-1749; SER-1762;
RP SER-1776; SER-1797; SER-1801; SER-1818; THR-1957; SER-2022; SER-2074;
RP SER-2104; SER-2106; SER-2449; SER-2649 AND SER-2664, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Structural protein involved in the filamentous cross-bridging
CC between microtubules and other skeletal elements.
CC -!- SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate with
CC MAP1A and MAP1B proteins. Interacts with TIAM2. Interacts with
CC guanylate kinase-like domain of DLG1, DLG2, DLG4. Binds to CSNK1D (By
CC similarity). MAP1 light chain LC2: Interacts with ELAVL4 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9QYR6}.
CC -!- INTERACTION:
CC P78559; Q9NRI5: DISC1; NbExp=3; IntAct=EBI-929047, EBI-529989;
CC P78559; Q9H492: MAP1LC3A; NbExp=6; IntAct=EBI-929047, EBI-720768;
CC P78559; P31947: SFN; NbExp=3; IntAct=EBI-929047, EBI-476295;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P78559-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P78559-2; Sequence=VSP_040240;
CC -!- TISSUE SPECIFICITY: Brain.
CC -!- DOMAIN: The basic region containing the repeats may be responsible for
CC the binding of MAP1A to microtubules.
CC -!- PTM: Phosphorylated by CSNK1D. {ECO:0000250}.
CC -!- PTM: LC2 is generated from MAP1A by proteolytic processing.
CC {ECO:0000269|PubMed:18419581}.
CC -!- SIMILARITY: Belongs to the MAP1 family. {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; U38291; AAB41132.1; -; Genomic_DNA.
DR EMBL; U38292; AAB41133.1; -; mRNA.
DR EMBL; AC019011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF200415; AAF08305.2; -; mRNA.
DR EMBL; U80458; AAD00355.1; -; mRNA.
DR EMBL; Z47038; CAA87104.1; -; Genomic_DNA.
DR EMBL; U14577; AAA81362.1; -; mRNA.
DR CCDS; CCDS42031.1; -. [P78559-1]
DR PIR; I38857; I38857.
DR RefSeq; NP_002364.5; NM_002373.5. [P78559-1]
DR SMR; P78559; -.
DR BioGRID; 110303; 74.
DR DIP; DIP-36377N; -.
DR IntAct; P78559; 24.
DR MINT; P78559; -.
DR STRING; 9606.ENSP00000300231; -.
DR DrugBank; DB01196; Estramustine.
DR CarbonylDB; P78559; -.
DR GlyGen; P78559; 5 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; P78559; -.
DR MetOSite; P78559; -.
DR PhosphoSitePlus; P78559; -.
DR BioMuta; MAP1A; -.
DR DMDM; 313104325; -.
DR EPD; P78559; -.
DR jPOST; P78559; -.
DR MassIVE; P78559; -.
DR MaxQB; P78559; -.
DR PaxDb; P78559; -.
DR PeptideAtlas; P78559; -.
DR PRIDE; P78559; -.
DR ProteomicsDB; 57652; -. [P78559-1]
DR ProteomicsDB; 57653; -. [P78559-2]
DR Antibodypedia; 6277; 147 antibodies from 24 providers.
DR DNASU; 4130; -.
DR Ensembl; ENST00000300231.6; ENSP00000300231.5; ENSG00000166963.13. [P78559-1]
DR GeneID; 4130; -.
DR KEGG; hsa:4130; -.
DR MANE-Select; ENST00000300231.6; ENSP00000300231.5; NM_002373.6; NP_002364.5.
DR UCSC; uc001zrt.4; human. [P78559-1]
DR CTD; 4130; -.
DR DisGeNET; 4130; -.
DR GeneCards; MAP1A; -.
DR HGNC; HGNC:6835; MAP1A.
DR HPA; ENSG00000166963; Tissue enriched (brain).
DR MIM; 600178; gene.
DR neXtProt; NX_P78559; -.
DR OpenTargets; ENSG00000166963; -.
DR VEuPathDB; HostDB:ENSG00000166963; -.
DR eggNOG; KOG3592; Eukaryota.
DR GeneTree; ENSGT00940000158701; -.
DR InParanoid; P78559; -.
DR PhylomeDB; P78559; -.
DR TreeFam; TF350229; -.
DR PathwayCommons; P78559; -.
DR SignaLink; P78559; -.
DR SIGNOR; P78559; -.
DR BioGRID-ORCS; 4130; 16 hits in 1077 CRISPR screens.
DR ChiTaRS; MAP1A; human.
DR GeneWiki; MAP1A; -.
DR GenomeRNAi; 4130; -.
DR Pharos; P78559; Tbio.
DR PRO; PR:P78559; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; P78559; protein.
DR Bgee; ENSG00000166963; Expressed in lateral nuclear group of thalamus and 190 other tissues.
DR ExpressionAtlas; P78559; baseline and differential.
DR Genevisible; P78559; HS.
DR GO; GO:0030424; C:axon; ISS:ARUK-UCL.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0043194; C:axon initial segment; ISS:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; ISS:ARUK-UCL.
DR GO; GO:0044307; C:dendritic branch; ISS:ARUK-UCL.
DR GO; GO:1901588; C:dendritic microtubule; ISS:ARUK-UCL.
DR GO; GO:0043198; C:dendritic shaft; ISS:ARUK-UCL.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISS:ARUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
DR GO; GO:0150001; C:primary dendrite; ISS:ARUK-UCL.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; ISS:ARUK-UCL.
DR GO; GO:0008093; F:cytoskeletal anchor activity; ISS:ARUK-UCL.
DR GO; GO:0008017; F:microtubule binding; ISS:ARUK-UCL.
DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc.
DR GO; GO:0048156; F:tau protein binding; NAS:ARUK-UCL.
DR GO; GO:0015631; F:tubulin binding; ISS:ARUK-UCL.
DR GO; GO:0099641; P:anterograde axonal protein transport; ISS:ARUK-UCL.
DR GO; GO:0008306; P:associative learning; ISS:ARUK-UCL.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0016358; P:dendrite development; IBA:GO_Central.
DR GO; GO:0007613; P:memory; ISS:ARUK-UCL.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:ARUK-UCL.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:ARUK-UCL.
DR GO; GO:1902817; P:negative regulation of protein localization to microtubule; ISS:ARUK-UCL.
DR GO; GO:0070050; P:neuron cellular homeostasis; ISS:ARUK-UCL.
DR GO; GO:1990535; P:neuron projection maintenance; ISS:ARUK-UCL.
DR GO; GO:1903829; P:positive regulation of protein localization; ISS:ARUK-UCL.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISS:ARUK-UCL.
DR GO; GO:0031114; P:regulation of microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:ARUK-UCL.
DR GO; GO:0099642; P:retrograde axonal protein transport; ISS:ARUK-UCL.
DR GO; GO:0050882; P:voluntary musculoskeletal movement; ISS:ARUK-UCL.
DR InterPro; IPR026074; MAP1.
DR InterPro; IPR015656; MAP1A.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR13843; PTHR13843; 1.
DR PANTHER; PTHR13843:SF6; PTHR13843:SF6; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..2803
FT /note="Microtubule-associated protein 1A"
FT /id="PRO_0000018600"
FT CHAIN 1..2566
FT /note="MAP1A heavy chain"
FT /id="PRO_0000418376"
FT CHAIN 2567..2803
FT /note="MAP1 light chain LC2"
FT /id="PRO_0000018601"
FT REPEAT 415..417
FT /note="1"
FT REPEAT 420..422
FT /note="2"
FT REPEAT 427..429
FT /note="3"
FT REPEAT 431..433
FT /note="4"
FT REPEAT 436..438
FT /note="5"
FT REPEAT 440..442
FT /note="6"
FT REPEAT 444..446
FT /note="7"
FT REPEAT 449..451
FT /note="8"
FT REPEAT 539..541
FT /note="9"
FT REGION 302..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 415..541
FT /note="9 X 3 AA repeats of K-K-[DE]"
FT REGION 486..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 847..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1109..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1573..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1632..1684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1713..1879
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1892..2673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..662
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1067
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1580..1605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1656..1684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1713..1728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1846..1871
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1908..1934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1943..1959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2005..2035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2042..2071
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2076..2090
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2091..2119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2252..2272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2463..2477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2494..2517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2555..2577
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2587..2606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 177
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 616
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 877
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 894
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 896
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 909
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 986
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 996
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 1004
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 1013
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 1019
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 1029
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 1069
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1144
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 1146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 1218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 1264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 1326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 1600
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1749
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1762
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1791
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1797
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1801
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1812
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 1818
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1931
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 1957
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2022
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15144186,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2058
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 2074
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2108
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYR6"
FT MOD_RES 2235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 2252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 2256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 2259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 2260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P34926"
FT MOD_RES 2449
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 2752
FT /note="Q -> QSV (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_040240"
FT VARIANT 72
FT /note="F -> L (in dbSNP:rs2584695)"
FT /evidence="ECO:0000269|PubMed:8812494"
FT /id="VAR_039705"
FT VARIANT 335
FT /note="A -> S (in dbSNP:rs1060935)"
FT /evidence="ECO:0000269|PubMed:8812494"
FT /id="VAR_039706"
FT VARIANT 336
FT /note="K -> T (in dbSNP:rs1060936)"
FT /evidence="ECO:0000269|PubMed:8812494"
FT /id="VAR_039707"
FT VARIANT 353
FT /note="A -> S (in dbSNP:rs1060937)"
FT /evidence="ECO:0000269|PubMed:8812494"
FT /id="VAR_039708"
FT VARIANT 357
FT /note="A -> S (in dbSNP:rs1060938)"
FT /evidence="ECO:0000269|PubMed:8812494"
FT /id="VAR_039709"
FT VARIANT 364
FT /note="K -> Q (in dbSNP:rs2602129)"
FT /evidence="ECO:0000269|PubMed:8812494"
FT /id="VAR_039710"
FT VARIANT 485
FT /note="K -> Q (in dbSNP:rs2584715)"
FT /id="VAR_039711"
FT VARIANT 830
FT /note="T -> A (in dbSNP:rs3803337)"
FT /id="VAR_039712"
FT VARIANT 1078
FT /note="N -> S (in dbSNP:rs8034794)"
FT /id="VAR_039713"
FT VARIANT 1102
FT /note="I -> T (in dbSNP:rs8036179)"
FT /id="VAR_039714"
FT VARIANT 1185
FT /note="R -> H (in dbSNP:rs3803335)"
FT /id="VAR_039715"
FT VARIANT 1245
FT /note="D -> N (in dbSNP:rs12912505)"
FT /id="VAR_039716"
FT VARIANT 1461
FT /note="D -> N (in dbSNP:rs2245715)"
FT /id="VAR_039717"
FT VARIANT 1553
FT /note="Q -> H (in dbSNP:rs2584717)"
FT /id="VAR_039718"
FT VARIANT 1605
FT /note="K -> N (in dbSNP:rs2584697)"
FT /id="VAR_039719"
FT VARIANT 1650
FT /note="W -> C (in dbSNP:rs1060943)"
FT /evidence="ECO:0000269|PubMed:8812494"
FT /id="VAR_039720"
FT VARIANT 1690
FT /note="A -> S (in dbSNP:rs1060946)"
FT /evidence="ECO:0000269|PubMed:8812494"
FT /id="VAR_039721"
FT VARIANT 1827
FT /note="P -> A (in dbSNP:rs2229014)"
FT /id="VAR_039722"
FT VARIANT 1881
FT /note="A -> P (in dbSNP:rs1060950)"
FT /evidence="ECO:0000269|PubMed:8812494"
FT /id="VAR_039723"
FT VARIANT 1912
FT /note="A -> V (in dbSNP:rs2584718)"
FT /evidence="ECO:0000269|PubMed:8812494"
FT /id="VAR_039724"
FT VARIANT 1938
FT /note="S -> R (in dbSNP:rs2584719)"
FT /evidence="ECO:0000269|PubMed:8812494"
FT /id="VAR_039725"
FT VARIANT 2056
FT /note="S -> R (in dbSNP:rs1060953)"
FT /id="VAR_039726"
FT VARIANT 2214
FT /note="H -> Y (in dbSNP:rs1060955)"
FT /evidence="ECO:0000269|PubMed:8812494"
FT /id="VAR_039727"
FT VARIANT 2327
FT /note="D -> V (in dbSNP:rs8026745)"
FT /id="VAR_039728"
FT VARIANT 2405
FT /note="T -> I (in dbSNP:rs8027254)"
FT /id="VAR_059432"
FT VARIANT 2461
FT /note="I -> T (in dbSNP:rs8028849)"
FT /id="VAR_056122"
FT VARIANT 2465
FT /note="D -> N (in dbSNP:rs8027916)"
FT /id="VAR_059433"
FT CONFLICT 134..135
FT /note="VV -> IP (in Ref. 5; CAA87104)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="A -> G (in Ref. 5; CAA87104)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="V -> A (in Ref. 5; CAA87104)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="Q -> H (in Ref. 4; AAD00355)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="S -> G (in Ref. 5; CAA87104)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="K -> Q (in Ref. 4; AAD00355)"
FT /evidence="ECO:0000305"
FT CONFLICT 414..419
FT /note="EKKDKE -> KKKRNS (in Ref. 5; CAA87104)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="K -> P (in Ref. 1; AAB41132/AAB41133)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="E -> D (in Ref. 4; AAD00355)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="K -> Q (in Ref. 4; AAD00355)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="E -> D (in Ref. 4; AAD00355)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="K -> R (in Ref. 4; AAD00355)"
FT /evidence="ECO:0000305"
FT CONFLICT 452..453
FT /note="TK -> SS (in Ref. 4; AAD00355)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="K -> R (in Ref. 4; AAD00355)"
FT /evidence="ECO:0000305"
FT CONFLICT 682
FT /note="Q -> P (in Ref. 1; AAB41132/AAB41133)"
FT /evidence="ECO:0000305"
FT CONFLICT 1025
FT /note="Q -> K (in Ref. 1; AAB41132/AAB41133)"
FT /evidence="ECO:0000305"
FT CONFLICT 1303..1313
FT /note="KYLPGAITSPD -> EVLTWGDHQALN (in Ref. 4; AAD00355)"
FT /evidence="ECO:0000305"
FT CONFLICT 1335..1341
FT /note="Missing (in Ref. 4; AAD00355)"
FT /evidence="ECO:0000305"
FT CONFLICT 1368
FT /note="Q -> T (in Ref. 4; AAD00355)"
FT /evidence="ECO:0000305"
FT CONFLICT 1470
FT /note="A -> T (in Ref. 4; AAD00355)"
FT /evidence="ECO:0000305"
FT CONFLICT 1714
FT /note="G -> V (in Ref. 1; AAB41132/AAB41133)"
FT /evidence="ECO:0000305"
FT CONFLICT 1869
FT /note="E -> A (in Ref. 6; AAA81362)"
FT /evidence="ECO:0000305"
FT CONFLICT 1879..1883
FT /note="GTAEY -> AHSRV (in Ref. 6; AAA81362)"
FT /evidence="ECO:0000305"
FT CONFLICT 2118
FT /note="P -> A (in Ref. 1; AAB41132/AAB41133)"
FT /evidence="ECO:0000305"
FT CONFLICT 2174
FT /note="Q -> E (in Ref. 1; AAB41132/AAB41133)"
FT /evidence="ECO:0000305"
FT CONFLICT 2613
FT /note="A -> D (in Ref. 1; AAB41132/AAB41133)"
FT /evidence="ECO:0000305"
FT CONFLICT 2616
FT /note="A -> V (in Ref. 1; AAB41132/AAB41133)"
FT /evidence="ECO:0000305"
FT CONFLICT 2636
FT /note="P -> S (in Ref. 1; AAB41132/AAB41133)"
FT /evidence="ECO:0000305"
FT CONFLICT 2640
FT /note="A -> V (in Ref. 1; AAB41132/AAB41133)"
FT /evidence="ECO:0000305"
FT CONFLICT 2647
FT /note="P -> S (in Ref. 1; AAB41132/AAB41133)"
FT /evidence="ECO:0000305"
FT CONFLICT 2702
FT /note="C -> W (in Ref. 1; AAB41132/AAB41133)"
FT /evidence="ECO:0000305"
FT CONFLICT P78559-2:2753
FT /note="S -> V (in Ref. 1; AAB41132/AAB41133)"
FT /evidence="ECO:0000305"
FT CONFLICT P78559-2:2754
FT /note="V -> K (in Ref. 1; AAB41132/AAB41133)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2803 AA; 305485 MW; 94733902420F1FFE CRC64;
MDGVAEFSEY VSETVDVPSP FDLLEPPTSG GFLKLSKPCC YIFPGGRGDS ALFAVNGFNI
LVDGGSDRKS CFWKLVRHLD RIDSVLLTHI GADNLPGING LLQRKVAELE EEQSQGSSSY
SDWVKNLISP ELGVVFFNVP EKLRLPDASR KAKRSIEEAC LTLQHLNRLG IQAEPLYRVV
SNTIEPLTLF HKMGVGRLDM YVLNPVKDSK EMQFLMQKWA GNSKAKTGIV LPNGKEAEIS
VPYLTSITAL VVWLPANPTE KIVRVLFPGN APQNKILEGL EKLRHLDFLR YPVATQKDLA
SGAVPTNLKP SKIKQRADSK ESLKATTKTA VSKLAKREEV VEEGAKEARS ELAKELAKTE
KKAKESSEKP PEKPAKPERV KTESSEALKA EKRKLIKDKV GKKHLKEKIS KLEEKKDKEK
KEIKKERKEL KKDEGRKEEK KDAKKEEKRK DTKPELKKIS KPDLKPFTPE VRKTLYKAKV
PGRVKIDRSR AIRGEKELSS EPQTPPAQKG TVPLPTISGH RELVLSSPED LTQDFEEMKR
EERALLAEQR DTGLGDKPFP LDTAEEGPPS TAIQGTPPSV PGLGQEEHVM KEKELVPEVP
EEQGSKDRGL DSGAETEEEK DTWEEKKQRE AERLPDRTEA REESEPEVKE DVIEKAELEE
MEEVHPSDEE EEDATKAEGF YQKHMQEPLK VTPRSREAFG GRELGLQGKA PEKETSLFLS
SLTTPAGATE HVSYIQDETI PGYSETEQTI SDEEIHDEPE ERPAPPRFHT STYDLPGPEG
AGPFEASQPA DSAVPATSGK VYGTPETELT YPTNIVAAPL AEEEHVSSAT SITECDKLSS
FATSVAEDQS VASLTAPQTE ETGKSSLLLD TVTSIPSSRT EATQGLDYVP SAGTISPTSS
LEEDKGFKSP PCEDFSVTGE SEKRGEIIGK GLSGERAVEE EEEETANVEM SEKLCSQYGT
PVFSAPGHAL HPGEPALGEA EERCLSPDDS TVKMASPPPS GPPSATHTPF HQSPVEEKSE
PQDFQEADSW GDTKRTPGVG KEDAAEETVK PGPEEGTLEK EEKVPPPRSP QAQEAPVNID
EGLTGCTIQL LPAQDKAIVF EIMEAGEPTG PILGAEALPG GLRTLPQEPG KPQKDEVLRY
PDRSLSPEDA ESLSVLSVPS PDTANQEPTP KSPCGLTEQY LHKDRWPEVS PEDTQSLSLS
EESPSKETSL DVSSKQLSPE SLGTLQFGEL NLGKEEMGHL MQAEDTSHHT APMSVPEPHA
ATASPPTDGT TRYSAQTDIT DDSLDRKSPA SSFSHSTPSG NGKYLPGAIT SPDEHILTPD
SSFSKSPESL PGPALEDIAI KWEDKVPGLK DRTSEQKKEP EPKDEVLQQK DKTLEHKEVV
EPKDTAIYQK DEALHVKNEA VKQQDKALEQ KGRDLEQKDT ALEQKDKALE PKDKDLEEKD
KALEQKDKIP EEKDKALEQK DTALEQKDKA LEPKDKDLEQ KDRVLEQKEK IPEEKDKALD
QKVRSVEHKA PEDTVAEMKD RDLEQTDKAP EQKHQAQEQK DKVSEKKDQA LEQKYWALGQ
KDEALEQNIQ ALEENHQTQE QESLVQEDKT RKPKMLEEKS PEKVKAMEEK LEALLEKTKA
LGLEESLVQE GRAREQEEKY WRGQDVVQEW QETSPTREEP AGEQKELAPA WEDTSPEQDN
RYWRGREDVA LEQDTYWREL SCERKVWFPH ELDGQGARPH YTEERESTFL DEGPDDEQEV
PLREHATRSP WASDFKDFQE SSPQKGLEVE RWLAESPVGL PPEEEDKLTR SPFEIISPPA
SPPEMVGQRV PSAPGQESPI PDPKLMPHMK NEPTTPSWLA DIPPWVPKDR PLPPAPLSPA
PGPPTPAPES HTPAPFSWGT AEYDSVVAAV QEGAAELEGG PYSPLGKDYR KAEGEREEEG
RAEAPDKSSH SSKVPEASKS HATTEPEQTE PEQREPTPYP DERSFQYADI YEQMMLTGLG
PACPTREPPL GAAGDWPPCL STKEAAAGRN TSAEKELSSP ISPKSLQSDT PTFSYAALAG
PTVPPRPEPG PSMEPSLTPP AVPPRAPILS KGPSPPLNGN ILSCSPDRRS PSPKESGRSH
WDDSTSDSEL EKGAREQPEK EAQSPSPPHP IPMGSPTLWP ETEAHVSPPL DSHLGPARPS
LDFPASAFGF SSLQPAPPQL PSPAEPRSAP CGSLAFSGDR ALALAPGPPT RTRHDEYLEV
TKAPSLDSSL PQLPSPSSPG APLLSNLPRP ASPALSEGSS SEATTPVISS VAERFSPSLE
AAEQESGELD PGMEPAAHSL WDLTPLSPAP PASLDLALAP APSLPGDMGD GILPCHLECS
EAATEKPSPF QVPSEDCAAN GPTETSPNPP GPAPAKAENE EAAACPAWER GAWPEGAERS
SRPDTLLSPE QPVCPAGGSG GPPSSASPEV EAGPQGCATE PRPHRGELSP SFLNPPLPPS
IDDRDLSTEE VRLVGRGGRR RVGGPGTTGG PCPVTDETPP TSASDSGSSQ SDSDVPPETE
ECPSITAEAA LDSDEDGDFL PVDKAGGVSG THHPRPGHDP PPLPQPDPRP SPPRPDVCMA
DPEGLSSESG RVERLREKEK VQGRVGRRAP GKAKPASPAR RLDLRGKRSP TPGKGPADRA
SRAPPRPRST TSQVTPAEEK DGHSPMSKGL VNGLKAGPMA LSSKGSSGAP VYVDLAYIPN
HCSGKTADLD FFRRVRASYY VVSGNDPANG EPSRAVLDAL LEGKAQWGEN LQVTLIPTHD
TEVTREWYQQ THEQQQQLNV LVLASSSTVV MQDESFPACK IEF
