PCLO_RAT
ID PCLO_RAT Reviewed; 5085 AA.
AC Q9JKS6; Q9JLT1;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein piccolo;
DE AltName: Full=Aczonin;
DE AltName: Full=Multidomain presynaptic cytomatrix protein;
GN Name=Pclo;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|EMBL:AAF63196.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH RABAC1.
RX PubMed=10707984; DOI=10.1016/s0896-6273(00)80883-1;
RA Fenster S.D., Chung W.J., Zhai R., Cases-Langhoff C., Voss B., Garner A.M.,
RA Kaempf U., Kindler S., Gundelfinger E.D., Garner C.C.;
RT "Piccolo, a presynaptic zinc finger protein structurally related to
RT bassoon.";
RL Neuron 25:203-214(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Fenster S.D., Cases-Langhoff C., Gundelfinger E.D., Garner C.C.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP CALCIUM-BINDING, AND MUTAGENESIS OF ASP-4668; ASP-4674; VAL-4688;
RP 4688-VAL-MET-4689; MET-4689; 4690-VAL-VAL-4691; 4692-GLN-ASN-4693 AND
RP ALA-4694.
RX PubMed=11285225; DOI=10.1093/emboj/20.7.1605;
RA Gerber S.H., Garcia J., Rizo J., Suedhof T.C.;
RT "An unusual C(2)-domain in the active-zone protein piccolo: implications
RT for Ca(2+) regulation of neurotransmitter release.";
RL EMBO J. 20:1605-1619(2001).
RN [4]
RP INTERACTION WITH GIT1 AND GIT2, AND TISSUE SPECIFICITY.
RX PubMed=12473661; DOI=10.1074/jbc.m212287200;
RA Kim S., Ko J., Shin H., Lee J.R., Lim C., Han J.H., Altrock W.D.,
RA Garner C.C., Gundelfinger E.D., Premont R.T., Kaang B.K., Kim E.;
RT "The GIT family of proteins forms multimers and associates with the
RT presynaptic cytomatrix protein Piccolo.";
RL J. Biol. Chem. 278:6291-6300(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-1304; SER-1346;
RP SER-1353; SER-1451; SER-1463; SER-1464; SER-1469; SER-1493; SER-1496;
RP SER-1517; SER-1519; SER-1650; THR-1652; SER-1654; SER-1721; SER-1812;
RP SER-1820; SER-1841; THR-3392; THR-3419; SER-3571; SER-3574; SER-3577;
RP SER-3598; SER-3624; SER-3626; SER-3632; SER-3781; SER-4034; SER-4150;
RP SER-4340 AND SER-4723, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22875941; DOI=10.1523/jneurosci.0195-12.2012;
RA Maas C., Torres V.I., Altrock W.D., Leal-Ortiz S., Wagh D.,
RA Terry-Lorenzo R.T., Fejtova A., Gundelfinger E.D., Ziv N.E., Garner C.C.;
RT "Formation of Golgi-derived active zone precursor vesicles.";
RL J. Neurosci. 32:11095-11108(2012).
RN [7]
RP FUNCTION, INTERACTION WITH SIAH1, AND DISRUPTION PHENOTYPE.
RX PubMed=23403927; DOI=10.1038/emboj.2013.27;
RA Waites C.L., Leal-Ortiz S.A., Okerlund N., Dalke H., Fejtova A.,
RA Altrock W.D., Gundelfinger E.D., Garner C.C.;
RT "Bassoon and Piccolo maintain synapse integrity by regulating protein
RT ubiquitination and degradation.";
RL EMBO J. 32:954-969(2013).
RN [8]
RP FUNCTION, AND INTERACTION WITH CTBP1.
RX PubMed=25652077; DOI=10.15252/embj.201488796;
RA Ivanova D., Dirks A., Montenegro-Venegas C., Schoene C., Altrock W.D.,
RA Marini C., Frischknecht R., Schanze D., Zenker M., Gundelfinger E.D.,
RA Fejtova A.;
RT "Synaptic activity controls localization and function of CtBP1 via binding
RT to Bassoon and Piccolo.";
RL EMBO J. 34:1056-1077(2015).
RN [9]
RP FUNCTION, AND INTERACTION WITH TRIO.
RX PubMed=27907191; DOI=10.1371/journal.pone.0167535;
RA Terry-Lorenzo R.T., Torres V.I., Wagh D., Galaz J., Swanson S.K.,
RA Florens L., Washburn M.P., Waites C.L., Gundelfinger E.D., Reimer R.J.,
RA Garner C.C.;
RT "Trio, a Rho Family GEF, Interacts with the Presynaptic Active Zone
RT Proteins Piccolo and Bassoon.";
RL PLoS ONE 11:E0167535-E0167535(2016).
RN [10]
RP STRUCTURE BY NMR OF 4635-4776, AND ALTERNATIVE SPLICING (ISOFORM 3).
RX PubMed=14718922; DOI=10.1038/nsmb707;
RA Garcia J., Gerber S.H., Sugita S., Suedhof T.C., Rizo J.;
RT "A conformational switch in the Piccolo C2A domain regulated by alternative
RT splicing.";
RL Nat. Struct. Mol. Biol. 11:45-53(2004).
RN [11]
RP FUNCTION.
RX PubMed=29194628; DOI=10.1113/jp274885;
RA Parthier D., Kuner T., Koerber C.;
RT "The presynaptic scaffolding protein Piccolo organizes the readily
RT releasable pool at the calyx of Held.";
RL J. Physiol. (Lond.) 596:1485-1499(2018).
CC -!- FUNCTION: Scaffold protein of the presynaptic cytomatrix at the active
CC zone (CAZ) which is the place in the synapse where neurotransmitter is
CC released (PubMed:22875941). 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 (PubMed:22875941). 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 (PubMed:27907191). 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
CC (PubMed:29194628). Functions also in processes other than assembly such
CC as the regulation of specific presynaptic protein ubiquitination by
CC interacting with SIAH1 or the regulation of presynaptic autophagy
CC (PubMed:23403927, PubMed:27907191). Mediates also synapse to nucleus
CC communication leading to reconfiguration of gene expression by
CC associating with the transcriptional corepressor CTBP1 and by
CC subsequently reducing the size of its pool available for nuclear import
CC (PubMed:25652077). {ECO:0000269|PubMed:22875941,
CC ECO:0000269|PubMed:23403927, ECO:0000269|PubMed:25652077,
CC ECO:0000269|PubMed:27907191, ECO:0000269|PubMed:29194628}.
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)
CC (PubMed:27907191). Interacts with CTBP1 (PubMed:25652077). Interacts
CC with SIAH1; this interaction negatively regulates SIAH1 E3 ligase
CC activity (PubMed:23403927). Directly interacts with GIT1 and GIT2
CC (PubMed:12473661). {ECO:0000250|UniProtKB:Q9QYX7,
CC ECO:0000269|PubMed:12473661, ECO:0000269|PubMed:23403927,
CC ECO:0000269|PubMed:25652077, ECO:0000269|PubMed:27907191}.
CC -!- INTERACTION:
CC Q9JKS6; Q920M9: Siah1; NbExp=2; IntAct=EBI-2271602, EBI-957514;
CC -!- SUBCELLULAR LOCATION: Presynaptic active zone
CC {ECO:0000250|UniProtKB:Q9QYX7}. Note=Colocalizes with BSN in developing
CC axons. {ECO:0000269|PubMed:11285225}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9JKS6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JKS6-2; Sequence=VSP_003930, VSP_003931;
CC Name=3;
CC IsoId=Q9JKS6-3; Sequence=VSP_018194;
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:12473661}.
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:0000269|PubMed:11285225}.
CC -!- DISRUPTION PHENOTYPE: Loss of both Bassoon/BSN and Piccolo/PCLO leads
CC to the aberrant degradation of multiple presynaptic proteins,
CC culminating in synapse degeneration. {ECO:0000269|PubMed:23403927}.
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DR EMBL; AF138789; AAF07822.2; -; mRNA.
DR EMBL; AF227534; AAF63196.1; -; mRNA.
DR RefSeq; NP_001104267.1; NM_001110797.1. [Q9JKS6-2]
DR RefSeq; NP_064483.1; NM_020098.1. [Q9JKS6-1]
DR PDB; 1RH8; NMR; -; A=4635-4776.
DR PDBsum; 1RH8; -.
DR SMR; Q9JKS6; -.
DR BioGRID; 248576; 3.
DR IntAct; Q9JKS6; 2.
DR MINT; Q9JKS6; -.
DR STRING; 10116.ENSRNOP00000008637; -.
DR CarbonylDB; Q9JKS6; -.
DR GlyGen; Q9JKS6; 2 sites.
DR iPTMnet; Q9JKS6; -.
DR PhosphoSitePlus; Q9JKS6; -.
DR PaxDb; Q9JKS6; -.
DR PRIDE; Q9JKS6; -.
DR GeneID; 56768; -.
DR KEGG; rno:56768; -.
DR CTD; 27445; -.
DR RGD; 69406; Pclo.
DR eggNOG; KOG2060; Eukaryota.
DR InParanoid; Q9JKS6; -.
DR OrthoDB; 15051at2759; -.
DR PhylomeDB; Q9JKS6; -.
DR EvolutionaryTrace; Q9JKS6; -.
DR PRO; PR:Q9JKS6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0044316; C:cone cell pedicle; IDA:RGD.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005798; C:Golgi-associated vesicle; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
DR GO; GO:0060077; C:inhibitory synapse; IDA:RGD.
DR GO; GO:0031594; C:neuromuscular junction; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0048786; C:presynaptic active zone; IDA:UniProtKB.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0097470; C:ribbon synapse; IDA:RGD.
DR GO; GO:0044317; C:rod spherule; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
DR GO; GO:0030133; C:transport vesicle; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR GO; GO:0005522; F:profilin binding; ISS:UniProtKB.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; ISO:RGD.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0030073; P:insulin secretion; ISO:RGD.
DR GO; GO:0098815; P:modulation of excitatory postsynaptic potential; IMP:RGD.
DR GO; GO:1903423; P:positive regulation of synaptic vesicle recycling; IMP:RGD.
DR GO; GO:0099526; P:presynapse to nucleus signaling pathway; ISO:RGD.
DR GO; GO:1904071; P:presynaptic active zone assembly; IDA:UniProtKB.
DR GO; GO:0035418; P:protein localization to synapse; ISO:RGD.
DR GO; GO:0051036; P:regulation of endosome size; IMP:RGD.
DR GO; GO:0017157; P:regulation of exocytosis; ISO:RGD.
DR GO; GO:1904666; P:regulation of ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IDA:UniProtKB.
DR GO; GO:0097091; P:synaptic vesicle clustering; ISO:RGD.
DR GO; GO:0016080; P:synaptic vesicle targeting; NAS:UniProtKB.
DR CDD; cd15774; FYVE1_PCLO; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR042720; PCLO_FYVE1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR030629; Piccolo.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR008899; Znf_piccolo.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14113:SF6; PTHR14113:SF6; 3.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF05715; zf-piccolo; 2.
DR SMART; SM00239; C2; 2.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Calcium/phospholipid-binding;
KW Cell projection; Glycoprotein; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..5085
FT /note="Protein piccolo"
FT /id="PRO_0000058252"
FT DOMAIN 4442..4536
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143,
FT ECO:0000305"
FT DOMAIN 4639..4768
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 4950..5075
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 523..547
FT /note="C4-type"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:10707984"
FT ZN_FING 1010..1033
FT /note="C4-type"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:10707984"
FT REGION 1..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..491
FT /note="12 X 10 AA tandem approximate repeats of P-A-K-P-Q-
FT P-Q-Q-P-X"
FT REGION 585..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1622..1815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2116..2139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2275..2385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2456..2486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3350..3457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3503..3572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3602..3695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3774..3816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4225..4248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4272..4291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4335..4357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4589..4638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4775..4851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4874..4908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..474
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..694
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..931
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1094
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1482
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1535..1549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1560..1600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1664..1687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1731..1772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2290..2314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2324..2347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2348..2382
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2469..2486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3350..3418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3427..3451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3509..3527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3627..3667
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3675..3695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3801..3816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4226..4248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4589..4622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4780..4797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4815..4851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4874..4906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 4668
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4668
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4674
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4738
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4738
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4740
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4740
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4740
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4743
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4746
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4746
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 873
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1133
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1464
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1466
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1469
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1564
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1587
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1650
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1652
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1659
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1721
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1772
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1807
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 1812
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1841
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3014
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3392
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 3419
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 3522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3530
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3561
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3565
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 3571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 3574
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 3577
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 3598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 3624
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 3626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 3632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 3781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 4034
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 4150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 4304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 4308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 4311
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 4340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 4376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 4609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYX7"
FT MOD_RES 4723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 2702
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 2976
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 4687..4695
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018194"
FT VAR_SEQ 4876..4880
FT /note="TKPTN -> SKRRK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10707984"
FT /id="VSP_003930"
FT VAR_SEQ 4881..5085
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10707984"
FT /id="VSP_003931"
FT MUTAGEN 4668
FT /note="D->A: Complete loss of calcium-binding and calcium-
FT dependent phospholipid binding activity."
FT /evidence="ECO:0000269|PubMed:11285225"
FT MUTAGEN 4674
FT /note="D->A: Complete loss of calcium-binding and calcium-
FT dependent phospholipid binding activity."
FT /evidence="ECO:0000269|PubMed:11285225"
FT MUTAGEN 4688..4689
FT /note="VM->SS: 10-fold increase in affinity for calcium."
FT /evidence="ECO:0000269|PubMed:11285225"
FT MUTAGEN 4688
FT /note="V->S: Small increase in affinity for calcium."
FT /evidence="ECO:0000269|PubMed:11285225"
FT MUTAGEN 4689
FT /note="M->S: Increased affinity for calcium."
FT /evidence="ECO:0000269|PubMed:11285225"
FT MUTAGEN 4690..4691
FT /note="VV->SS: 10-fold increase in affinity for calcium."
FT /evidence="ECO:0000269|PubMed:11285225"
FT MUTAGEN 4692..4693
FT /note="QN->AA: Moderate increase in affinity for calcium."
FT /evidence="ECO:0000269|PubMed:11285225"
FT MUTAGEN 4694
FT /note="A->S: No effect on calcium-binding activity."
FT /evidence="ECO:0000269|PubMed:11285225"
FT STRAND 4642..4650
FT /evidence="ECO:0007829|PDB:1RH8"
FT STRAND 4653..4663
FT /evidence="ECO:0007829|PDB:1RH8"
FT STRAND 4668..4671
FT /evidence="ECO:0007829|PDB:1RH8"
FT STRAND 4676..4681
FT /evidence="ECO:0007829|PDB:1RH8"
FT HELIX 4696..4699
FT /evidence="ECO:0007829|PDB:1RH8"
FT TURN 4700..4705
FT /evidence="ECO:0007829|PDB:1RH8"
FT HELIX 4706..4709
FT /evidence="ECO:0007829|PDB:1RH8"
FT STRAND 4712..4719
FT /evidence="ECO:0007829|PDB:1RH8"
FT HELIX 4724..4727
FT /evidence="ECO:0007829|PDB:1RH8"
FT STRAND 4731..4739
FT /evidence="ECO:0007829|PDB:1RH8"
FT STRAND 4741..4743
FT /evidence="ECO:0007829|PDB:1RH8"
FT STRAND 4745..4754
FT /evidence="ECO:0007829|PDB:1RH8"
FT HELIX 4759..4761
FT /evidence="ECO:0007829|PDB:1RH8"
FT STRAND 4766..4769
FT /evidence="ECO:0007829|PDB:1RH8"
SQ SEQUENCE 5085 AA; 552716 MW; 5A1BB543201A7450 CRC64;
MGNEASLEGE GLPEGLAAAA GAGGSGSALH PGIPAGMEAD LSQLSEEERR QIAAVMSRAQ
GLPKGSVPPA AAESPSMHRK QELDSSQAPQ QPGKPPDPGR PTQPGLSKSR TTDTFRSEQK
LPGRSPSTIS LKESKSRTDF KEEYKSSMMP GFFSDVNPLS AVSSVVNKFN PFDLISDSEA
SQEETTKKQK VVQKEQGKSE GMAKPPLQQP SPKPIPKQQG QVKEVIQQDS SPKSVSSQQA
EKVKPQAPGT GKPSQQSPAQ TPAQQASPGK PVAQQPGSAK ATVQQPGPAK SPAQPAGTGK
SPAQPPAKTP GQQAGLEKTS SSQQPGPKSL AQTPGHGKFP LGPVKSPAQQ PGTAKHPAQQ
PGPQTAAKVP GPTKTPAQQS GPGKTPAQQP GPTKPSPQQP IPAKPQPQQP VATKTQPQQS
APAKPQPQQP APAKPQPQQP TPAKPQPQPP TPAKPQPQPP TATKPQPQPP TATKPHHQQP
GLAKPSAQQP TKSISQTVTG RPLQPPPTSA AQTPAQGLSK TICPLCNTTE LLLHIPEKAN
FNTCTECQST VCSLCGFNPN PHLTEIKEWL CLNCQMQRAL GGDLAAAIPS SPQPTPKAAT
APTATASKSP VPSQQASPKK EPPSKQDSPK ALESKKPPEP KKPPEPKKPP EPKKPPPLVK
QPTLHGPTPA TAPQLPVAEA LPEPAPPKEP SGPLPEQAKA PVGDVEPKQP KMTETRADIQ
SSSTTKPDIL SSQVQSQAQV KTASPLKTDS AKPSQSFPPT GEKTTPLDSK AMPRPASDSK
IISQPGPGSE SKDPKHIDPI QKKDEPKKAQ PKGSPKPETK PVPKGSPTPS GTRPTAGQAA
PPSQQPPKPQ EQSRRFSLNL GGITDAPKSQ PTTPQETVTG KLFGFGASIF SQASNLISTA
GQQGPHPQTG PAAPSKQAPT PSQSPAAQGP AKSTGQLPPA PAKATAVKKE AKAAAAENLE
SKPEQAPTAK KTEKDKKPPP AKVGKPPPSE PEKAVPAHKP DKTTKPKPAC PLCRTELNLG
SQEPPNFNTC TECKNQVCNL CGFNPTPHLT EIQEWLCLNC QTQRAISGQL GDMGKMPPAP
SGPKASPMPA PAEPSSQKTP TGTQVKGKKK EAEGKTEAEK PVPEKETASI EKTPPMVTTD
QKLEESEGKK SKVSALPEKK PSEEEKAISA DKKERKPPAE EKPPLEEKKP IPVDKKLPPE
AKPLSSEGEE KHEILKAHVQ IPEEEPTGKV AAKAGEEEQQ PDSRPEALPG ATPLTLPKAG
EKERAVAQPQ AEGSSKDGQG ERSKEKTEKE EDKSDTSSSQ QPKSPQGLSD TGYSSDGISG
SLGEIPSLIP SDEKDLLKGL KKDSFSQESS PSSPSDLAKL ESTVLSILEA QASTLVGEKA
EKKTQPQKIS PEKPQDQQKT QTASETLDIT ISEEEIKESQ EKKVSPKKDS EQGFPSRKEH
KEKPELVDDL SPRRASYDSV EDSSESENSP VVRRKRRTSI GSSSSDEYKQ EDSQGSGEEE
DFIRKQIIEM SADEDASGSE DEEFIRSQLK EISGVGESQK REEAKGKGKG VAGKHRRLTR
KSSTSFDDDA GRRHSWHDED DETFDESPEL KFRETKSQES EELVVAGGGG LRRFKTIELN
STIADKYSSE SSQKKTILYF DEEPELEMES LTDSPEDRSR GEGSSSLHAS SFTPGTSPTS
VSSLDEDSDS SPSHKKGESK QQRKARHRSH GPLLPTIEDS SEEEELREEE ELLKEQEKQR
ELEQQQRKSS SKKSKKDKDE LRAQRRRERP KTPPSNLSPI EDASPTEELR QAAEMEELHR
SSCSEYSPSI ESDPEGFEIS PEKIIEVQKV YKLPAAVSLY SPTDEQSVMQ KEGVQKALKS
AEEMYEEMMQ KPHKYKAFPA ANERDEVFEK EPLYGGMLIE DYIYESLVED TYNGSVDGSL
LTRQEEQNGF MQQRGREQKV RLQEQIYDDP MQKISDLQKE FYELESLHSV VPQEDIVSSS
YIIPESHEIV DLGSMVMSTS EEKKLLDADS AYEELMRRQQ VQVTDGSSPV QTTIGDDMAE
STLDFDRVQD ASLTSSILSG ASLTDSTSSA TLSIPDVKIT QQFSAEELED EYVTDYTREI
QDIIAHESLI LTYSEPSESA TSVPPSDTPS LTSSISSVCT TDSSSPVTTL DSLTTVYTEP
ADVMTKFKDS EEISSTYFPG SIIDYPEDIS VSLDRTIMPE SRTNEDRIVL SFSGMAPSVV
ESVGTKPERP QADTISTDLP ISEKDLIKGK KETGDGIILE VLDAYKDKRE ESEAELTKIS
LPEPGLAQAP SSVTAPQIKE QHVSPHSVSG KISGQEKPTY RLPSGSLPVS THPSKSRPFF
RSSSLDISAQ PPPPPPPPPP SPSTSSPPPT PPLPPATSPK PPTYPKKKLA VAATVTSTTI
VTTHVDALTM VEAAAARRSN GLPATKMCAI APPPVPPKPS QIPTGLVFTH RPEAIKPPIA
PKPAVPQIPV TTQKPTDTCP KPTGLSLTST MSLNLVTSAD YNVPSPTSPL SPHSNKSSPR
YSKSLMDTYV VITLPSEPGT PTDSSAAQAI TSWPLGSPPK DLVSLETVFS VVPPMTSTEI
PSASQPTLYT SGALGTFSVT PAVTASLFQT VPTSLTQFLP AEASKPEVSA VSSAVPSVAP
RSVSIPIPPE PLALDRHQYK ENGKLPLIGD AIDLRTIPKS EVKVTEKCMD LSASAMDVKR
QTTANEVYRR QISAVQPSII NLSAASSLGT PVTMDSKTVA VVTCTDTTIY TTGTESQVGI
EHAVTSPLQL TTSKHTELPY RKPSSQAFPT IRDEAPINLS LGPSAQAVTL AVTKPVTVPP
VGVTNGWTDS TLSQGVADGE VVDLSTSKSH RTVVTMDEST SNVVTKIIED DEKPVDLTAG
RRAVCCDMVY TLPFGRSCTA QQPATTLPED RFGYRDDHYQ YDRSGPYGYR GIGGMKPSMS
DTNLPEAGHF FYKSKNAFDY SGGTGAAVDL TSGRVSTGEV MDYSSKTTGP YPETRQVISG
VGISTPQYST ARLTPPPGPQ YGVGSVLRSS NGVVYSSVAT PIPSTFAITT QPGSIFSTTV
RDLSGIPTTD AMTSLSALHQ SQPMPRSYFI TTGASETDIA VTGIDINASL QTITMETLPA
ETMDSVPTLT TASEVFSEVV GEESTLLIVP DEDKQQQQLD LERELLELEK IKQQRFAEEL
EWERQEIQRF REQEKIMVQK KLEELQSMKQ HLLYQQEEER QAQFMMRQET LAQQQLQLEQ
IQQLQQQLHQ QLEEQKLRQI YQYNYDPSGT SSPQTTTEQA ILEGQYAATE GSQFWATEDA
TTTASTVVAI EIPQSQGWYT VQSDGVTQYI APPGILSTVS EIPLTDVVVK EEKQPKKRSS
GAKVRGQYDE MGESVADDPR NLKKIVDSGV QTDDEETADR SYASRRRRTK KSVDTSVQTD
DEDQDEWDMP SRSRRKARTG KYGDSTAEGD KTKPLSKVSS VAVQTVAEIS VQTEPVGTIR
TPSIRARVDA KVEIIKHISA PEKTYKGGSL GCQTETDSDT QSPPYLGATS PPKDKKRPTP
LEIGYSSSHL RADPTVQLAP SPPKSPKVLY SPISPLSPGN ALEPAFVPYE KPLPDDISPQ
KVLHPDMAKV PPASPKTAKM MQRSMSDPKP LSPTADESSR APFQYSEGFT TKGSQTMTAS
GTQKKVKRTL PNPPPEEVST GTQSTYSTMG TASRRRMCRT NTMARAKILQ DIDRELDLVE
RESAKLRKKQ AELDEEEKEI DAKLRYLEMG INRRKEALLK EREKRERAYL QGVAEDRDYM
SDSEVSSTRP SRVESQHGVE RPRTAPQTEF SQFIPPQTQT EAQLVPPTSP YTQYQYSSPA
LPTQAPTPYT QQSHFQQQTL YHQQVSPYQT QPTFQAVATM SFTPQAQPTP TPQPSYQLPS
QMMVIQQKPR QTTLYLEPKI TSNYEVIRNQ PLMIAPVSTD NTYAVSHLGS KYNSLDLRIG
LEERSSMAGS PISSISADSF YADIDHHTSR NYVLIDDIGD ITKGTAALST VFSLHEKDLS
KTDRLLRTTE TRRSQEVTDF LAPLQTSSRL HSYVKADEDP MEDPYELKLL KHQIKQEFRR
GTESLDHLAG LSHYYHADTS YRHFPKSEKY SISRLTLEKQ AAKQLPAAIL YQKQSKHKKS
LIDPKMSKFS PIQESRDLEP DYPTYMSSGT SSIGGISSRA RLLQDDITFG LRKNITDQQK
FMGSSLGSGL GTLGNTIRSA LQDEADKPYS SGSRSRPSSR PSSVYGLDLS IKRDSSSSSL
RLKAQEAEAL DVSFGHSSSS ARTKPTSLPI SQSRGRIPIV AQSSEEESPL SPVGQPMGMA
RAAAGPLPPI SADTRDQFGS SHSLPEVQQH MREESRTRGY DRDIAFIMDD FQHAMSDSEA
YHLRREETDW FDKPRESRLE NGHGLDRKLP ERLVHSRPLS QHQEQILQMN GKTIHYIFPH
ARVKITRDFK DHTGSGNGLG IRIVGGKEIP GHSGEIGAYI AKILPGESAE HTGPLMEGMQ
VLEWNGVPLT SKTYEEVQSI INQQSGEAEI CVRLDLNMLS DSENPQHLEL HEPPKVDKAK
SPGVDPKQLA AELQKVSLQQ SPLVMSSVVE KGSHAHSGPT SAGSSSVPSP GQPGSPSVSK
KKHSSTKPTD GPKAASHPIT GEIQLQINYD LGNLIIHILQ ARNLVPRDNN GYSDPFVKVY
LLPGRGQVMV VQNASAEYKR RTKYVQKSLN PEWNQTVIYK SISMEQLMKK TLEVTVWDYD
RFSSNDFLGE VLIDLSSTSH LDNTPRWYPL KEQTESIDHG KSHSSQNSQQ SPKPSVIKSR
SHGIFPDPSK DMQVPTIEKS HSSPGSSKSS SEGHLRSHGP SRSQSKTSVA QTHLEDAGVA
IAAAEAAVQQ LRIQPTKPTN HRPAESSVST GSSGSSVGSG YSVDSEGSSC VAGEPNLLPI
PRIGKMGQNG QDPVKQPGMG ATDTEGKTQV MGEIKLALKK EMKTDGEQLI VEILQCRNIT
YKFKSPDHLP DLYVKLYVIN ISTQKKVIKK KTRVCRHDRE PSFNETFRFS LSPAGHSLQI
LLFSNGGKFM KKTLIGEACI WLDKVDLRKR IVNWHKLLVS PTQTH
