PCLO_HUMAN
ID PCLO_HUMAN Reviewed; 5142 AA.
AC Q9Y6V0; A4D1A7; A6NNX9; O43373; O60305; Q08E72; Q9BVC8; Q9UIV2; Q9Y6U9;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 5.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Protein piccolo;
DE AltName: Full=Aczonin;
GN Name=PCLO {ECO:0000250|UniProtKB:Q9QYX7};
GN Synonyms=ACZ {ECO:0000312|EMBL:CAB60727.1}, KIAA0559;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 21-661 (ISOFORM 5).
RC TISSUE=Placenta;
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-849 (ISOFORM 5).
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 [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3724-5142 (ISOFORM 6).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [6]
RP TISSUE SPECIFICITY, AND INVOLVEMENT IN PCH3.
RX PubMed=25832664; DOI=10.1212/wnl.0000000000001523;
RA Ahmed M.Y., Chioza B.A., Rajab A., Schmitz-Abe K., Al-Khayat A.,
RA Al-Turki S., Baple E.L., Patton M.A., Al-Memar A.Y., Hurles M.E.,
RA Partlow J.N., Hill R.S., Evrony G.D., Servattalab S., Markianos K.,
RA Walsh C.A., Crosby A.H., Mochida G.H.;
RT "Loss of PCLO function underlies pontocerebellar hypoplasia type III.";
RL Neurology 84:1745-1750(2015).
RN [7]
RP STRUCTURE BY NMR OF 4459-4592.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-003, a PDZ domain of hypothetical KIAA0559
RT protein from human.";
RL Submitted (JAN-2004) to the PDB data bank.
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 (By similarity). 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 (By
CC similarity). Mediates also synapse to nucleus communication leading to
CC reconfiguration of gene expression by associating with the
CC transcriptional corepressor CTBP1 and by subsequently reducing the size
CC of its pool available for nuclear import (By similarity).
CC {ECO:0000250|UniProtKB:Q9JKS6}.
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 (By
CC similarity). Interacts (via C-terminus) with TRIO (via N-terminus) (By
CC similarity). Interacts with CTBP1 (By similarity). Interacts with
CC SIAH1; this interaction negatively regulates SIAH1 E3 ligase activity
CC (By similarity). Directly interacts with GIT1 and GIT2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9JKS6, ECO:0000250|UniProtKB:Q9QYX7}.
CC -!- SUBCELLULAR LOCATION: Presynaptic active zone
CC {ECO:0000250|UniProtKB:Q9QYX7}. Note=Colocalizes with BSN in developing
CC axons. {ECO:0000250|UniProtKB:Q9JKS6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=5;
CC IsoId=Q9Y6V0-5; Sequence=Displayed;
CC Name=3;
CC IsoId=Q9Y6V0-3; Sequence=VSP_059461, VSP_059462, VSP_059463,
CC VSP_059464, VSP_059465;
CC Name=6;
CC IsoId=Q9Y6V0-6; Sequence=VSP_059464, VSP_059465;
CC -!- TISSUE SPECIFICITY: Moderately expressed in the developing cerebral
CC cortex. {ECO:0000269|PubMed:25832664}.
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 -!- DISEASE: Pontocerebellar hypoplasia 3 (PCH3) [MIM:608027]: A form of
CC pontocerebellar hypoplasia, a disorder characterized by structural
CC defects of the pons and cerebellum. Brain MRI shows an abnormally small
CC cerebellum and brainstem, decreased cerebral white matter, and a thin
CC corpus callosum. PCH3 features include seizures, short stature, optic
CC atrophy, progressive microcephaly, severe developmental delay.
CC {ECO:0000269|PubMed:25832664}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB97937.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAD21789.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EAL24187.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC004006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004082; AAB97937.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC080093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004886; AAD21789.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AC004903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236949; EAL24187.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC001304; AAH01304.2; -; mRNA.
DR EMBL; BC122565; AAI22566.1; -; mRNA.
DR EMBL; BC125271; AAI25272.1; -; mRNA.
DR EMBL; Y19188; CAB60727.1; -; mRNA.
DR EMBL; AB011131; BAA25485.1; -; mRNA.
DR CCDS; CCDS47630.1; -. [Q9Y6V0-5]
DR CCDS; CCDS47631.1; -. [Q9Y6V0-6]
DR PIR; T00332; T00332.
DR PIR; T00634; T00634.
DR RefSeq; NP_055325.2; NM_014510.2. [Q9Y6V0-6]
DR RefSeq; NP_149015.2; NM_033026.5. [Q9Y6V0-5]
DR PDB; 1UJD; NMR; -; A=4489-4592.
DR PDBsum; 1UJD; -.
DR SMR; Q9Y6V0; -.
DR BioGRID; 118178; 30.
DR ELM; Q9Y6V0; -.
DR IntAct; Q9Y6V0; 14.
DR MINT; Q9Y6V0; -.
DR STRING; 9606.ENSP00000334319; -.
DR GlyGen; Q9Y6V0; 62 sites, 1 O-linked glycan (62 sites).
DR iPTMnet; Q9Y6V0; -.
DR PhosphoSitePlus; Q9Y6V0; -.
DR BioMuta; PCLO; -.
DR DMDM; 332278245; -.
DR EPD; Q9Y6V0; -.
DR jPOST; Q9Y6V0; -.
DR MassIVE; Q9Y6V0; -.
DR MaxQB; Q9Y6V0; -.
DR PaxDb; Q9Y6V0; -.
DR PeptideAtlas; Q9Y6V0; -.
DR PRIDE; Q9Y6V0; -.
DR ProteomicsDB; 86795; -. [Q9Y6V0-3]
DR ProteomicsDB; 86797; -. [Q9Y6V0-5]
DR ProteomicsDB; 86798; -. [Q9Y6V0-6]
DR Antibodypedia; 2812; 270 antibodies from 24 providers.
DR DNASU; 27445; -.
DR Ensembl; ENST00000333891.14; ENSP00000334319.8; ENSG00000186472.20. [Q9Y6V0-5]
DR Ensembl; ENST00000423517.6; ENSP00000388393.2; ENSG00000186472.20. [Q9Y6V0-6]
DR Ensembl; ENST00000618073.1; ENSP00000482390.1; ENSG00000186472.20. [Q9Y6V0-3]
DR GeneID; 27445; -.
DR KEGG; hsa:27445; -.
DR MANE-Select; ENST00000333891.14; ENSP00000334319.8; NM_033026.6; NP_149015.2.
DR UCSC; uc003uhv.3; human. [Q9Y6V0-5]
DR CTD; 27445; -.
DR DisGeNET; 27445; -.
DR GeneCards; PCLO; -.
DR HGNC; HGNC:13406; PCLO.
DR HPA; ENSG00000186472; Group enriched (brain, pituitary gland, retina).
DR MalaCards; PCLO; -.
DR MIM; 604918; gene.
DR MIM; 608027; phenotype.
DR neXtProt; NX_Q9Y6V0; -.
DR OpenTargets; ENSG00000186472; -.
DR Orphanet; 97249; Pontocerebellar hypoplasia type 3.
DR PharmGKB; PA33072; -.
DR VEuPathDB; HostDB:ENSG00000186472; -.
DR eggNOG; KOG2060; Eukaryota.
DR GeneTree; ENSGT00620000087961; -.
DR HOGENOM; CLU_000104_0_1_1; -.
DR InParanoid; Q9Y6V0; -.
DR OMA; SHAHSGP; -.
DR OrthoDB; 15051at2759; -.
DR TreeFam; TF326082; -.
DR PathwayCommons; Q9Y6V0; -.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR SignaLink; Q9Y6V0; -.
DR BioGRID-ORCS; 27445; 7 hits in 1064 CRISPR screens.
DR ChiTaRS; PCLO; human.
DR EvolutionaryTrace; Q9Y6V0; -.
DR GeneWiki; PCLO; -.
DR GenomeRNAi; 27445; -.
DR Pharos; Q9Y6V0; Tbio.
DR PRO; PR:Q9Y6V0; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y6V0; protein.
DR Bgee; ENSG00000186472; Expressed in Brodmann (1909) area 23 and 163 other tissues.
DR ExpressionAtlas; Q9Y6V0; baseline and differential.
DR Genevisible; Q9Y6V0; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; NAS:UniProtKB.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR GO; GO:0099526; P:presynapse to nucleus signaling pathway; IEA:Ensembl.
DR GO; GO:1904071; P:presynaptic active zone assembly; IBA:GO_Central.
DR GO; GO:0035418; P:protein localization to synapse; IBA:GO_Central.
DR GO; GO:0017157; P:regulation of exocytosis; IEA:Ensembl.
DR GO; GO:0097091; P:synaptic vesicle clustering; IEA:Ensembl.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; 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; 2.
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 3D-structure; Alternative splicing; Calcium; Calcium/phospholipid-binding;
KW Cell projection; Metal-binding; Neurodegeneration; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..5142
FT /note="Protein piccolo"
FT /id="PRO_0000058250"
FT DOMAIN 4496..4590
FT /note="PDZ"
FT DOMAIN 4694..4823
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 5007..5132
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 589..613
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 1059..1082
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..555
FT /note="10 X 10 AA tandem approximate repeats of P-A-K-P-Q-
FT P-Q-Q-P-X"
FT REGION 650..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..1058
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1423..1868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2169..2192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2365..2438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2504..2536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3407..3508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3558..3626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3652..3746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3833..3908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4278..4301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4389..4411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4597..4618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4645..4690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4830..4907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4930..4986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..223
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..316
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..369
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..528
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..811
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..886
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..986
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1032
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1194..1282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1427..1454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1516..1543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1544..1564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1613..1653
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1674..1688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1717..1740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1784..1825
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1840..1854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2365..2385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2402..2436
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2517..2536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3407..3473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3482..3506
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3566..3584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3681..3720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3729..3746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3855..3908
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4280..4301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4599..4616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4645..4677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4835..4852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4870..4907
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4930..4971
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 4729
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4793
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4793
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4795
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4795
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4795
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4798
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4801
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4801
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 918
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 922
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1402
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1517
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1549
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1570
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 1572
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 1617
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1640
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1703
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 1705
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 1707
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1773
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1774
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1825
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1831
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1860
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1865
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1873
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 2562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3069
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3447
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3474
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3577
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 3628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 3652
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 3680
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3835
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 4088
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 4204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 4358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 4362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 4365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 4394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT MOD_RES 4430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 4664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 4778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JKS6"
FT VAR_SEQ 1..4570
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_059461"
FT VAR_SEQ 4571..4588
FT /note="VQSIISQQSGEAEICVRL -> MKKFRVSLVSKVGKQKYV (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_059462"
FT VAR_SEQ 4742..4750
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_059463"
FT VAR_SEQ 4931..4935
FT /note="TKPPN -> SKRRK (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_059464"
FT VAR_SEQ 4936..5142
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_059465"
FT VARIANT 2671
FT /note="T -> P (in dbSNP:rs10261848)"
FT /id="VAR_056959"
FT VARIANT 2804
FT /note="A -> T (in dbSNP:rs976714)"
FT /id="VAR_056960"
FT CONFLICT 441
FT /note="V -> A (in Ref. 4; CAB60727)"
FT /evidence="ECO:0000305"
FT CONFLICT 443..496
FT /note="Missing (in Ref. 4; CAB60727)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="A -> T (in Ref. 4; CAB60727)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="S -> P (in Ref. 3; AAI22566)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="S -> F (in Ref. 4; CAB60727)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="S -> F (in Ref. 4; CAB60727)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="V -> A (in Ref. 4; CAB60727)"
FT /evidence="ECO:0000305"
FT CONFLICT 814
FT /note="S -> T (in Ref. 4; CAB60727)"
FT /evidence="ECO:0000305"
FT CONFLICT 4814
FT /note="S -> A (in Ref. 3; AAH01304)"
FT /evidence="ECO:0000305"
FT STRAND 4494..4499
FT /evidence="ECO:0007829|PDB:1UJD"
FT STRAND 4503..4506
FT /evidence="ECO:0007829|PDB:1UJD"
FT STRAND 4514..4522
FT /evidence="ECO:0007829|PDB:1UJD"
FT STRAND 4524..4528
FT /evidence="ECO:0007829|PDB:1UJD"
FT STRAND 4530..4537
FT /evidence="ECO:0007829|PDB:1UJD"
FT HELIX 4542..4546
FT /evidence="ECO:0007829|PDB:1UJD"
FT STRAND 4554..4558
FT /evidence="ECO:0007829|PDB:1UJD"
FT HELIX 4568..4575
FT /evidence="ECO:0007829|PDB:1UJD"
FT STRAND 4582..4589
FT /evidence="ECO:0007829|PDB:1UJD"
SQ SEQUENCE 5142 AA; 560699 MW; 18F145349952C935 CRC64;
MGNEASLEGE GLPEGLAAAA AAGGGASGAG SPSHTAIPAG MEADLSQLSE EERRQIAAVM
SRAQGLPKGS VPPAAAESPS MHRKQELDSS HPPKQSGRPP DPGRPAQPGL SKSRTTDTFR
SEQKLPGRSP STISLKESKS RTDLKEEHKS SMMPGFLSEV NALSAVSSVV NKFNPFDLIS
DSEASQEETT KKQKVVQKEQ GKPEGIIKPP LQQQPPKPIP KQQGPGRDPL QQDGTPKSIS
SQQPEKIKSQ PPGTGKPIQG PTQTPQTDHA KLPLQRDASR PQTKQADIVR GESVKPSLPS
PSKPPIQQPT PGKPPAQQPG HEKSQPGPAK PPAQPSGLTK PLAQQPGTVK PPVQPPGTTK
PPAQPLGPAK PPAQQTGSEK PSSEQPGPKA LAQPPGVGKT PAQQPGPAKP PTQQVGTPKP
LAQQPGLQSP AKAPGPTKTP VQQPGPGKIP AQQAGPGKTS AQQTGPTKPP SQLPGPAKPP
PQQPGPAKPP PQQPGSAKPP SQQPGSTKPP PQQPGPAKPS PQQPGSTKPP SQQPGSAKPS
AQQPSPAKPS AQQSTKPVSQ TGSGKPLQPP TVSPSAKQPP SQGLPKTICP LCNTTELLLH
VPEKANFNTC TECQTTVCSL CGFNPNPHLT EVKEWLCLNC QMKRALGGDL APVPSSPQPK
LKTAPVTTTS AVSKSSPQPQ QTSPKKDAAP KQDLSKAPEP KKPPPLVKQP TLHGSPSAKA
KQPPEADSLS KPAPPKEPSV PSEQDKAPVA DDKPKQPKMV KPTTDLVSSS SATTKPDIPS
SKVQSQAEEK TTPPLKTDSA KPSQSFPPTG EKVSPFDSKA IPRPASDSKI ISHPGPSSES
KGQKQVDPVQ KKEEPKKAQT KMSPKPDAKP MPKGSPTPPG PRPTAGQTVP TPQQSPKPQE
QSRRFSLNLG SITDAPKSQP TTPQETVTGK LFGFGASIFS QASNLISTAG QPGPHSQSGP
GAPMKQAPAP SQPPTSQGPP KSTGQAPPAP AKSIPVKKET KAPAAEKLEP KAEQAPTVKR
TETEKKPPPI KDSKSLTAEP QKAVLPTKLE KSPKPESTCP LCKTELNIGS KDPPNFNTCT
ECKNQVCNLC GFNPTPHLTE IQEWLCLNCQ TQRAISGQLG DIRKMPPAPS GPKASPMPVP
TESSSQKTAV PPQVKLVKKQ EQEVKTEAEK VILEKVKETL SMEKIPPMVT TDQKQEESKL
EKDKASALQE KKPLPEEKKL IPEEEKIRSE EKKPLLEEKK PTPEDKKLLP EAKTSAPEEQ
KHDLLKSQVQ IAEEKLEGRV APKTVQEGKQ PQTKMEGLPS GTPQSLPKED DKTTKTIKEQ
PQPPCTAKPD QVEPGKEKTE KEDDKSDTSS SQQPKSPQGL SDTGYSSDGI SSSLGEIPSL
IPTDEKDILK GLKKDSFSQE SSPSSPSDLA KLESTVLSIL EAQASTLADE KSEKKTQPHE
VSPEQPKDQE KTQSLSETLE ITISEEEIKE SQEERKDTFK KDSQQDIPSS KDHKEKSEFV
DDITTRREPY DSVEESSESE NSPVPQRKRR TSVGSSSSDE YKQEDSQGSG EEEDFIRKQI
IEMSADEDAS GSEDDEFIRN QLKEISSSTE SQKKEETKGK GKITAGKHRR LTRKSSTSID
EDAGRRHSWH DEDDEAFDES PELKYRETKS QESEELVVTG GGGLRRFKTI ELNSTIADKY
SAESSQKKTS LYFDEEPELE MESLTDSPED RSRGEGSSSL HASSFTPGTS PTSVSSLDED
SDSSPSHKKG ESKQQRKARH RPHGPLLPTI EDSSEEEELR EEEELLKEQE KQREIEQQQR
KSSSKKSKKD KDELRAQRRR ERPKTPPSNL SPIEDASPTE ELRQAAEMEE LHRSSCSEYS
PSIESDPEGF EISPEKIIEV QKVYKLPTAV SLYSPTDEQS IMQKEGSQKA LKSAEEMYEE
MMHKTHKYKA FPAANERDEV FEKEPLYGGM LIEDYIYESL VEDTYNGSVD GSLLTRQEEE
NGFMQQKGRE QKIRLSEQIY EDPMQKITDL QKEFYELESL HSVVPQEDIV SSSFIIPESH
EIVDLGTMVT STEEERKLLD ADAAYEELMK RQQMQLTPGS SPTQAPIGED MTESTMDFDR
MPDASLTSSV LSGASLTDST SSATLSIPDV KITQHFSTEE IEDEYVTDYT REIQEIIAHE
SLILTYSEPS ESATSVPPSD TPSLTSSVSS VCTTDSSSPI TTLDSITTVY TEPVDMITKF
EDSEEISSST YFPGSIIDYP EEISVSLDRT APPDGRASAD HIVISLSDMA SSIIESVVPK
PEGPVADTVS TDLLISEKDP VKKAKKETGN GIILEVLEAY RDKKELEAER TKSSLSETVF
DHPPSSVIAL PMKEQLSTTY FTSGETFGQE KPASQLPSGS PSVSSLPAKP RPFFRSSSLD
ISAQPPPPPP PPPPPPPPPP PPPPPPLPPP TSPKPTILPK KKLTVASPVT TATPLFDAVT
TLETTAVLRS NGLPVTRICT TAPPPVPPKP SSIPSGLVFT HRPEPSKPPI APKPVIPQLP
TTTQKPTDIH PKPTGLSLTS SMTLNLVTSA DYKLPSPTSP LSPHSNKSSP RFSKSLTETY
VVITLPSEPG TPTDSSASQA ITSWPLGSPS KDLVSVEPVF SVVPPVTAVE IPISSEQTFY
ISGALQTFSA TPVTAPSSFQ AAPTSVTQFL TTEVSKTEVS ATRSTAPSVG LSSISITIPP
EPLALDNIHL EKPQYKEDGK LQLVGDVIDL RTVPKVEVKT TDKCIDLSAS TMDVKRQITA
NEVYGKQISA VQPSIINLSV TSSIVTPVSL ATETVTFVTC TASASYTTGT ESLVGAEHAM
TTPLQLTTSK HAEPPYRIPS DQVFPIAREE APINLSLGTP AHAVTLAITK PVTVPPVGVT
NGWTDSTVSQ GITDGEVVDL STTKSHRTVV TMDESTSSVM TKIIEDEKPV DLTAGRRAVC
CDVVYKLPFG RSCTAQQPAT TLPEDRFGYR DDHYQYDRSG PYGYRGIGGM KPSMSDTNLA
EAGHFFYKSK NAFDYSEGTD TAVDLTSGRV TTGEVMDYSS KTTGPYPETR QVISGAGIST
PQYSTARMTP PPGPQYCVGS VLRSSNGVVY SSVATPTPST FAITTQPGSI FSTTVRDLSG
IHTADAVTSL PAMHHSQPMP RSYFITTGAS ETDIAVTGID ISASLQTITM ESLTAETIDS
VPTLTTASEV FPEVVGDESA LLIVPEEDKQ QQQLDLEREL LELEKIKQQR FAEELEWERQ
EIQRFREQEK IMVQKKLEEL QSMKQHLLFQ QEEERQAQFM MRQETLAQQQ LQLEQIQQLQ
QQLHQQLEEQ KIRQIYQYNY DPSGTASPQT TTEQAILEGQ YAALEGSQFW ATEDATTTAS
AVVAIEIPQS QGWYTVQSDG VTQYIAPPGI LSTVSEIPLT DVVVKEEKQP KKRSSGAKVR
GQYDDMGENM TDDPRSFKKI VDSGVQTDDE DATDRSYVSR RRRTKKSVDT SVQTDDEDQD
EWDMPTRSRR KARVGKYGDS MTEADKTKPL SKVSSIAVQT VAEISVQTEP VGTIRTPSIR
ARVDAKVEII KHISAPEKTY KGGSLGCQTE ADSDTQSPQY LSATSPPKDK KRPTPLEIGY
SSHLRADSTV QLAPSPPKSP KVLYSPISPL SPGKALESAF VPYEKPLPDD ISPQKVLHPD
MAKVPPASPK TAKMMQRSMS DPKPLSPTAD ESSRAPFQYT EGYTTKGSQT MTSSGAQKKV
KRTLPNPPPE EISTGTQSTF STMGTVSRRR ICRTNTMARA KILQDIDREL DLVERESAKL
RKKQAELDEE EKEIDAKLRY LEMGINRRKE ALLKEREKRE RAYLQGVAED RDYMSDSEVS
STRPTRIESQ HGIERPRTAP QTEFSQFIPP QTQTESQLVP PTSPYTQYQY SSPALPTQAP
TSYTQQSHFE QQTLYHQQVS PYQTQPTFQA VATMSFTPQV QPTPTPQPSY QLPSQMMVIQ
QKPRQTTLYL EPKITSNYEV IRNQPLMIAP VSTDNTFAVS HLGSKYNSLD LRIGLEERSS
MASSPISSIS ADSFYADIDH HTPRNYVLID DIGEITKGTA ALSTAFSLHE KDLSKTDRLL
RTTETRRSQE VTDFLAPLQS SSRLHSYVKA EEDPMEDPYE LKLLKHQIKQ EFRRGTESLD
HLAGLSHYYH ADTSYRHFPK SEKYSISRLT LEKQAAKQLP AAILYQKQSK HKKSLIDPKM
SKFSPIQESR DLEPDYSSYM TSSTSSIGGI SSRARLLQDD ITFGLRKNIT DQQKFMGSSL
GTGLGTLGNT IRSALQDEAD KPYSSGSRSR PSSRPSSVYG LDLSIKRDSS SSSLRLKAQE
AEALDVSFSH ASSSARTKPT SLPISQSRGR IPIVAQNSEE ESPLSPVGQP MGMARAAAGP
LPPISADTRD QFGSSHSLPE VQQHMREESR TRGYDRDIAF IMDDFQHAMS DSEAYHLRRE
ETDWFDKPRE SRLENGHGLD RKLPERLVHS RPLSQHQEQI IQMNGKTMHY IFPHARIKIT
RDSKDHTVSG NGLGIRIVGG KEIPGHSGEI GAYIAKILPG GSAEQTGKLM EGMQVLEWNG
IPLTSKTYEE VQSIISQQSG EAEICVRLDL NMLSDSENSQ HLELHEPPKA VDKAKSPGVD
PKQLAAELQK VSLQQSPLVL SSVVEKGSHV HSGPTSAGSS SVPSPGQPGS PSVSKKKHGS
SKPTDGTKVV SHPITGEIQL QINYDLGNLI IHILQARNLV PRDNNGYSDP FVKVYLLPGR
GQVMVVQNAS AEYKRRTKHV QKSLNPEWNQ TVIYKSISME QLKKKTLEVT VWDYDRFSSN
DFLGEVLIDL SSTSHLDNTP RWYPLKEQTE SIDHGKSHSS QSSQQSPKPS VIKSRSHGIF
PDPSKDMQVP TIEKSHSSPG SSKSSSEGHL RSHGPSRSQS KTSVTQTHLE DAGAAIAAAE
AAVQQLRIQP TKPPNHRPAE SSVSTGSSGS SFGSGYSVDS EGSSSTAGET NLFPIPRIGK
MGQNGQEPVK QPGVGVGLAD TEAKTQVMGE IKIALKKEMK TDGEQLIVEI LQCRNITYKF
KSPDHLPDLY VKIYVMNIST QKKVIKKKTR VCRHDREPSF NETFRFSLSP AGHSLQILLF
SNGGKFMKKT LIGEACIWLD KVDLRKRIVN WHKLLVSPTQ TH
