ID PCLO_CHICK Reviewed; 5120 AA.
AC Q9PU36;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 115.
DE RecName: Full=Protein piccolo {ECO:0000305};
DE AltName: Full=Aczonin {ECO:0000303|PubMed:10508862};
DE Flags: Fragment;
GN Name=PCLO; Synonyms=ACZ {ECO:0000303|PubMed:10508862};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031 {ECO:0000312|EMBL:CAB60725.1};
RN [1] {ECO:0000312|EMBL:CAB60725.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
CC -!- FUNCTION: May act as a scaffolding protein involved in the organization
CC of synaptic active zones and in synaptic vesicle trafficking.
CC {ECO:0000250|UniProtKB:Q9QYX7}.
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 RABAC1/PRA1 and profilin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Presynaptic active zone
CC {ECO:0000250|UniProtKB:Q9QYX7}. Note=Colocalizes with BSN in developing
CC axons. {ECO:0000250|UniProtKB:Q9JKS6}.
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}.
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DR EMBL; Y19187; CAB60725.1; -; mRNA.
DR SMR; Q9PU36; -.
DR STRING; 9031.ENSGALP00000071119; -.
DR PaxDb; 9031-ENSGALP00000039055; -.
DR VEuPathDB; HostDB:geneid_395319; -.
DR eggNOG; KOG2060; Eukaryota.
DR InParanoid; Q9PU36; -.
DR PhylomeDB; Q9PU36; -.
DR Proteomes; UP000000539; Unassembled WGS sequence.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
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:1904071; P:presynaptic active zone assembly; IBA:GO_Central.
DR GO; GO:0035418; P:protein localization to synapse; IBA:GO_Central.
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.
PE 2: Evidence at transcript level;
KW Calcium; Calcium/phospholipid-binding; Cell projection; Metal-binding;
KW Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT CHAIN <1..5120
FT /note="Protein piccolo"
FT /id="PRO_0000058249"
FT DOMAIN 4414..4493
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143,
FT ECO:0000305"
FT DOMAIN 4611..4742
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 4985..5110
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 368..392
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 836..859
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..357
FT /note="10 X 10 AA tandem approximate repeats of P-A-K-P-Q-
FT P-Q-Q-P-X"
FT REGION 428..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1117..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1357..1786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1992..2012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2272..2301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2315..2349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2472..2492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3322..3414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3470..3536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3566..3654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4191..4265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4306..4328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4365..4396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4560..4610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4750..4826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4903..4977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..764
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..923
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1491..1518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1586..1601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1743
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1758..1772
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1993..2012
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2286..2301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2322..2349
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3322..3382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3392..3414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3473..3498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3590..3630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3639..3654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4192..4234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4250..4265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4365..4389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4560..4594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4754..4771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4789..4826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4915..4951
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 4642
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4642
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4712
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4712
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4714
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4714
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4714
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4717
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4720
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 4720
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:CAB60725.1"
SQ SEQUENCE 5120 AA; 560764 MW; A658D9891B65B412 CRC64;
LDTTHHPRQP GKPPDPGPGL SKSRTVDVLK TEQRAPGRSP SSISLRESKS RTDFKEDQKP
SMMPSFFSEA NPLSAVTSVV NKFSPFDLIS DSDAAHEEAG RKQKVTQKEQ GKPEEQRGLA
KHPSQQQSPK LVQQQGPVKP TPQQTESSKP VPQQQQPGEP KQGQKPGPSH PGDSKAEQVK
QPPQPRGPQK SQLQQSEPTK PGQQQTSAKT SAGPTKPLPQ QPDSAKTSSQ APPPTKPSLQ
QSGSVKQPSQ QPARQGGPVK PSAQQAGPPK QQPGSEKPTA QQTGPAKQPP QPGPGKTPLQ
QTGPVKQVPP QAGPTKPSSQ TAGAAKSLAQ QPGLTKPPGQ QPGPEKPLQQ KQASTTQPVE
STPKKTFCPL CTTTELLLHT PEKANYNTCT QCHTVVCSLC GFNPNPHITE IKEWLCLNCQ
MQRALGGDLA SGHGPGPQLP PPKQKTPTPA STAKPSPQLQ PGQKKDASPK PDPSQQADSK
KPVPQKKQPS MPGSPPVKSK QTHAEPSDTG QQIDSTPKSD QVKPTQAEEK QNQPSIQKPT
MDTVPTSAAP GVKQDLADPQ SPSTQQKVTD SPMPETTKPP ADTHPAGDKP DSKPLPQVSR
QKSDPKLASQ SGAKSDAKTQ KPSEPAPVKD DPKKLQTKPA PKPDTKPAPK GPQAGTGPRP
TSAQPAPQPQ QPQKTPEQSR RFSLNLGGIT DAPKPQPTTP QETVTGKLFG FGASIFSQAS
SLISTAGQPG SQTSGPAPPA TKQPQPPSQP PASQAPPKEA AQAQPPPKAA PTKKETKPLA
SEKLGPMASD STLTTKGSDL EKKPSLAKDS KHQTAEAKKP AELSEQEKAS QPKVSCPLCK
TGLNIGSKDP PNFNTCTECK KVVCNLCGFN PMPHIVEVQE WLCLNCQTQR AMSGQLGDMG
KVPLPKLGPS QPVSKPPATP QKQPVPAVSH SPQKSSTPPT PAATKPKEEP SVPKEVPKLQ
QGKLEKTLSA DKIQQGIQKE DAKSKQGKLF KTPSADKIQR VSQKEDSRLQ QTKLTKTPSS
DKILHGVQKE DIKFQEAKLA KIPSADKILH RLQKEDPKLQ QMKMAKALSA DKIQPEAQKE
DVQLQEVRLS KAVSADKIQH GIQKDLNLQH VKIEKTSSVE KIQEAQKESK LQQDKLPKTL
SEDKIPATVS SDHKKLLSKS EEDKKPELLE KSTPHPKDKK EQITAETTGH ITEQKVEVEA
PCDKLHEKKQ EDVKKEDLTT GIPQMVSKPE KAEEEKTPVP VSRLPRSDHV EAVREKIEKE
DDKSDTSSSQ QQKSPQGLSD TGYSSDGISS SLGEIPSHIP SDEKDLPREP SQKDTISQES
PPSPSDLAKL ESTVLSILEA QASTLTDEKS VKRKELYETY SEQTKDQHKT KPLPVTPESY
SSDEEDLEAI QEGERTIAAD SKGGASSQTD YKEEDGGNDT PARRQRYDSV EDSSESENSP
VPRRKRRASV GSSSSDEYKR DDSQGSGDEE DFIRKQIIEM SADEDASGSE DDEFIRNQLK
EISVTESQKK EEVKSKAKGT VGKHRRMARK SSAGYDEDAG RRHSWHDDDD ETFDESPEPK
YRETKSQDGE ELAISGGGGL RRFKTIELNS TITSKYSETP EQQKGILYFD EEPELEMESL
TDSPEDRSRG EGSSSLHASS FTPGTSPTSV SSLDEDSDSS PSHKKLGGES KQQRKARHRS
HGPLLPTIED SSEEEELREE EELLKEQEKQ RELEQQQRKS SSKKSKKDKD ELRAQRRRER
PKTPPSNLSP IEDASPTEEL RQAAEMEELH RSSCSEYSPS IESDPEGFEI SPEKIIEVQK
VYKLPTAVSL YSPTDEKLIG ALKEESGQKT LKSAEEVYEE MIHKTHKSKS FQIASEKDEV
FEKESLYGGM LIEDYIYESL IEDTYNGTVD TNLAMRQDES NEYIQQRGKE KKIRASEQIY
DEPQKITDLQ EDYYSVEPLC SIVPQEDIVS SSYIIPESHE IVVLDSTVTS TTEEKQLLDA
EAAYEELMKK QRMQLTPGSS PTQPTSDLAP TSDMKVSSIG EIADSTSLTS STTSAISDVS
SLSSIALSIP DVKITQHFTA EEIEDEYLTD YAREIQEIIS HETSMLTYSE VSEGAASILP
SDTASLTSST SSVCTTDSSS PIDSATTGYV DTSDAVSKLV DSEDIIAQVP FTSTEEYSEV
SMPYESVAGA TTKPAIASDM DTVHQAAVCL PETAPSVFTT TVIKPKQYAS DTITYDISTA
EKDAARKMKS TVETGIIKIH HEDSHKELSL DMTRINLTGA TSEQPPLCVA SVSVKEPASE
TPAVPTPRVV SKTSTVSMPS SAPALTSKVF SLFRSSSLDS PAQPSPPSPP PPPPPPPPPL
PPPILPKPAI YPKKKSQIQA PMATAPTAVP LVTSVATLES AAVLKNHVVP VTKTYTPTPP
PVPPKPSSIP AGLVFSHRPT EVTKPPIAPK PAVPPLPIAV HKPAETQPKP IGLSLTSSMT
LNLVSSAEYK IASPTSPLSP HSNKSSPRLT KPSQETYVVI TLPSEPGTPT EAITSQAVTS
WPLEAPSKEQ IPQPMQPIFT SSMKAVEIQS MADQSMYITG ALQTIPITTQ STFEKVPSSK
SEAVTTEVAK TTASVVKRPV PSVGLGSVTI TIPPEPIYIS DQPRYRENGR FHPLGDVIDL
RTLTKVDIEM RDSCMDLSAV SMDARRQMPT SDTSGRPVST VQPAIINLST ACVADPSLSI
VTETVAVMTC TATVSYSAST DSLVDLGHAM TTPLQLTTSK HFEPAYRVTS SQPFPVSRDE
VPINLSLGTS AHAVTWAATK PVTVPPVSVT NGWTDLSTSQ EPMEIGAVDL STTKSHRTVV
TMDETTSGII TTVIEDDEKP VDLTAGRRAV CCDMVYKLPF GRSCTAQQPP TTLPEDRFGY
RDDHYQYDRS GSYGYRGMGG MKPSMSDTNL SEAGLFAYKS KNSFDYQVGA TDAAVDLTSG
RVTSGEVMDY SSKTTGPYPE TRQVISGIGI STPQYSQARM VSSLSSPFGA GSVLRSSNGV
VYSSVATPIP STFAITTQPG SIFSTTVRDL PTLQTIDSVP SLSTLQQNQP LPRSYSFLTT
MAAEKDASTT LDIETGLPPL TLESIATEPT NLIPATASEV YTDVIEDEVA LIIAPEEGKQ
QQLDLERELL ELEKIKQQRF AEELEWERQE IQRFREQEKF MVQKKLEELQ SMKHHLLFQQ
EEERQAQYMM RQETLAQQQL QLEQFQQLQQ QLHQQLEEQK IRQIYQYGYD PSGTGSPQTT
TDQALLEGQY ATAENGQFWP TDDATTTASG VLGIEISQSQ TWYTVQSDGI TQYIPRSGIL
SSVSEMSLKD IDVREEKQLK KRSSMPKLRG PYEELEESLE EEPRCYKKIV DSGVQTDDED
GADRGYTNRR RRTKKSVDTS VQTDDEDQDE WDLSSRSGRK PRVGKYSEST TEADKAKQFS
KVSSIAVQTV AEISVQTEPV GTIRTPSIRA RLDAKVEIIK HISAPEKTYK GESLGCQTET
ESDTQSPQYL SASSPQKDKK RPTPLEIGYS SHLRPDSTLQ VVPSPPKSPK VLYSPISPVS
PSKVIESAFV PYEKSITDDI SPQKMLHPDI AKVPPSSPKA AKMMQRSMSD PKPLSPTAED
SSRAQFQYTE GFMTKGSSSI TPSGTQKKVK RTLPNPPPEE ATAGTQSPYT SVGSVSRRRI
CRTTTMARAK ILQDIDRELD LVERESAKLR KKQAELDEEE KEIDAKLRYL EMGINRRKEA
LLKEREKRER AYLQGVAEER DYMSDSEVNN TRSTRIETQH GLERPRTAPQ TEFNQFMPPQ
TQPETQFAPA TSPYGQYQYS SPALPTQAPT QFTQQSHYQQ QQPLYHQQVS PYQTQTAFQT
GATMSFTPQA QPPPTQQPSY QLSSQMMVIQ PKPRQTPLYL EPKITTNYDV IRNQPLMIAP
VSTDNNYAVS QLGSKYTTLD LRIGLDERNS IASSPISSIS ADSFYADIDQ HHTPRNYVLI
DDIGELTKGT GALGSGFSLH EKDLTKTDRL LRTTEARRAQ EVSDFLAPLQ TSSRLHSYVK
ADEDPMEDPY ELKLLKHQIK QEFRRGAESL DHLAGLSQYY HPEGSFRHFP KSEKYSIGRL
TLEKQAAKQL PAALLYQKQS KHKKALIDPK LTKFSPIQES RDLEPDYSTY MTSSSTSSLG
GITTRARLLQ DDITFGLRKN ITDQQKYMGA PLTSSIGAGL GAALGPTMRS TLQDEADKSY
SSGSRSRPSS RPSSVYGLDL SLKRDSSSSS LRLKAQEAEP LDVSFSHAAP SGRTKPTSLP
ISQSRGRIPI VAQNSEEESP LSPVGQPMGM ARAAAGPLPP ISADTRDQFG SSHSLPEVQQ
HMREESRTRG YDRDIAFIMD DFQHAMSDSE AYHLRREETD WFDKPRESRL ENGHGLDRRL
PEKLSHSRPP SQHQDQISCQ INGKPLQYIF PHARLKLLRD PKDHTVSGNG LGIRVVGGKE
IPGSSGEIGA YIAKVLPGGN AEQTGKLIEG MQVLEWNGIP LTGKTYEEVQ NIIIQQCGEA
EICVRLDLNM LSDSENPQHL ELHEPVKAVD KAKSPGVDPK QLAAELQKVS LQQAPLLASS
GVEKSSHVHS GTTSATSSAV PSPGQPGSPS VSKKRHSSKP AEATKSGSHP ITGEIQLQIN
YDKHLGNLII HILQARNLAP RDNNGYSDPF VKVYLLPGRG QVMVVQNASA EYKRRTKYVQ
KSLNPEWNQT VIYKNISTEQ LKKKTLEVTV WDYDRFSSND FLGEVLIDLS SVSQLDNTPR
WYPLKEQSEN IDHGKSHSGQ NSQQSPKPSV IKSRSHGIFP DPSKDMQVPT IEKSHSSPGS
SKSSSEGHLR SHGPSRSQSK TSVTQTHLED AGAAIAAAEA AVQQLRLQPT AHKSGQSNHA
RKQHRHSIAG VLPIQRTQSD NLPPPANDNK DQSQLALRKV MSDGPVKPEG ARSTNHRPAE
SSVSTGSSVS SFGSGYSMDS EGSSSATGEN NLFPIPRIGK MSQNGQEPIK QSGVGLTDAE
GKTQVMGEIK IALKKEMKTD GEQLIVEILQ CRNITYKFKS PDHLPDLYVK LYVVNVSTQK
RVIKKKTRVC RHDREPSFNE TFRFSLSPAG HSLQILLVSN GGKFMKKTLI GEAYIWLDKV
DLRKRTVNWH KLLVSSTQTH
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