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 27-MAR-2024, entry version 208. 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; Evidence={ECO:0000255|PROSITE- CC 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}; 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; 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; 33. DR ELM; Q9Y6V0; -. DR IntAct; Q9Y6V0; 14. DR MINT; Q9Y6V0; -. DR STRING; 9606.ENSP00000334319; -. DR GlyCosmos; Q9Y6V0; 62 sites, 1 glycan. DR GlyGen; Q9Y6V0; 39 sites, 1 O-linked glycan (39 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; 9606-ENSP00000334319; -. DR PeptideAtlas; Q9Y6V0; -. DR ProteomicsDB; 86795; -. [Q9Y6V0-3] DR ProteomicsDB; 86797; -. [Q9Y6V0-5] DR ProteomicsDB; 86798; -. [Q9Y6V0-6] DR Antibodypedia; 2812; 292 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 AGR; HGNC:13406; -. 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; KVTTDHK; -. DR OrthoDB; 4336453at2759; -. 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 1140 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 164 other cell types or tissues. DR ExpressionAtlas; Q9Y6V0; baseline and differential. 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; cd04031; C2A_RIM1alpha; 1. DR CDD; cd15774; FYVE1_PCLO; 1. DR CDD; cd15776; FYVE2_PCLO; 1. DR CDD; cd00992; PDZ_signaling; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 2.60.40.150; C2 domain; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR008899; Znf_piccolo. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR14113; PICCOLO/BASSOON; 1. DR PANTHER; PTHR14113:SF6; PROTEIN PICCOLO; 1. 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; C2 domain (Calcium/lipid-binding domain, CaLB); 2. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR PROSITE; PS50004; C2; 2. DR PROSITE; PS50106; PDZ; 1. DR Genevisible; Q9Y6V0; HS. 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 //