UN13A_HUMAN
ID UN13A_HUMAN Reviewed; 1703 AA.
AC Q9UPW8; E5RHY9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 4.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Protein unc-13 homolog A {ECO:0000305};
DE AltName: Full=Munc13-1;
GN Name=UNC13A {ECO:0000312|HGNC:HGNC:23150}; Synonyms=KIAA1032;
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=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1703.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [3]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12871971; DOI=10.1074/jbc.m303203200;
RA Sheu L., Pasyk E.A., Ji J., Huang X., Gao X., Varoqueaux F., Brose N.,
RA Gaisano H.Y.;
RT "Regulation of insulin exocytosis by Munc13-1.";
RL J. Biol. Chem. 278:27556-27563(2003).
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23999003; DOI=10.1016/j.jdermsci.2013.07.010;
RA Yoo J.C., Lim T.Y., Park J.S., Hah Y.S., Park N., Hong S.G., Park J.Y.,
RA Yoon T.J.;
RT "SYT14L, especially its C2 domain, is involved in regulating melanocyte
RT differentiation.";
RL J. Dermatol. Sci. 72:246-251(2013).
CC -!- FUNCTION: Plays a role in vesicle maturation during exocytosis as a
CC target of the diacylglycerol second messenger pathway. Involved in
CC neurotransmitter release by acting in synaptic vesicle priming prior to
CC vesicle fusion and participates in the activity-dependent refilling of
CC readily releasable vesicle pool (RRP). Essential for synaptic vesicle
CC maturation in most excitatory/glutamatergic but not inhibitory/GABA-
CC mediated synapses. Facilitates neuronal dense core vesicles fusion as
CC well as controls the location and efficiency of their synaptic release
CC (By similarity). Also involved in secretory granule priming in insulin
CC secretion. Plays a role in dendrite formation by melanocytes
CC (PubMed:23999003). {ECO:0000250|UniProtKB:Q4KUS2,
CC ECO:0000250|UniProtKB:Q62768, ECO:0000269|PubMed:23999003}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- SUBUNIT: Interacts with the N-termini of STX1A and/or STX1B1 and DOC2A.
CC Interacts with BSN. Interacts with RIMS1 which recruits UNC13A to the
CC active zone. Forms homodimers via its first C2 domain. Also interacts
CC via this domain with the zinc finger domain of RIMS2. Part of a complex
CC consisting of ERC2, RIMS1 and UNC13A. Also part of a complex consisting
CC of UNC13A, RIMS2 and RAB3A (By similarity). Interacts with FBXO45 (via
CC SRY domain); leading to the degradation of UNC13A by the proteasome (By
CC similarity). {ECO:0000250|UniProtKB:Q4KUS2,
CC ECO:0000250|UniProtKB:Q62768}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q62768}. Cell
CC membrane {ECO:0000250|UniProtKB:Q62768}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q62768}. Presynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q62768}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q62768}. Presynaptic active zone
CC {ECO:0000250|UniProtKB:Q62768}. Note=Translocated to the plasma
CC membrane in response to phorbol ester binding.
CC {ECO:0000250|UniProtKB:Q62768}.
CC -!- TISSUE SPECIFICITY: Expressed in pancreatic islet cells
CC (PubMed:12871971). Expressed in melanocytes (PubMed:23999003).
CC {ECO:0000269|PubMed:12871971, ECO:0000269|PubMed:23999003}.
CC -!- DOMAIN: The C2 domains are not involved in calcium-dependent
CC phospholipid binding. {ECO:0000250}.
CC -!- DOMAIN: The C-terminal region containing both MHD domains and the third
CC C2 domain is required for synaptic vesicle priming activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the unc-13 family. {ECO:0000305}.
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DR EMBL; AC008761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB028955; BAA82984.2; -; mRNA.
DR CCDS; CCDS46013.2; -.
DR RefSeq; NP_001073890.2; NM_001080421.2.
DR AlphaFoldDB; Q9UPW8; -.
DR BMRB; Q9UPW8; -.
DR SMR; Q9UPW8; -.
DR BioGRID; 116665; 10.
DR IntAct; Q9UPW8; 4.
DR STRING; 9606.ENSP00000429562; -.
DR iPTMnet; Q9UPW8; -.
DR PhosphoSitePlus; Q9UPW8; -.
DR BioMuta; UNC13A; -.
DR DMDM; 374095515; -.
DR EPD; Q9UPW8; -.
DR jPOST; Q9UPW8; -.
DR MassIVE; Q9UPW8; -.
DR MaxQB; Q9UPW8; -.
DR PaxDb; Q9UPW8; -.
DR PeptideAtlas; Q9UPW8; -.
DR PRIDE; Q9UPW8; -.
DR ProteomicsDB; 85464; -.
DR Antibodypedia; 43803; 33 antibodies from 18 providers.
DR DNASU; 23025; -.
DR Ensembl; ENST00000519716.7; ENSP00000429562.2; ENSG00000130477.16.
DR GeneID; 23025; -.
DR KEGG; hsa:23025; -.
DR MANE-Select; ENST00000519716.7; ENSP00000429562.2; NM_001080421.3; NP_001073890.2.
DR UCSC; uc060vkq.1; human.
DR CTD; 23025; -.
DR DisGeNET; 23025; -.
DR GeneCards; UNC13A; -.
DR HGNC; HGNC:23150; UNC13A.
DR HPA; ENSG00000130477; Group enriched (brain, pituitary gland, retina).
DR MalaCards; UNC13A; -.
DR MIM; 609894; gene.
DR neXtProt; NX_Q9UPW8; -.
DR OpenTargets; ENSG00000130477; -.
DR Orphanet; 803; Amyotrophic lateral sclerosis.
DR PharmGKB; PA134879020; -.
DR VEuPathDB; HostDB:ENSG00000130477; -.
DR eggNOG; KOG1011; Eukaryota.
DR GeneTree; ENSGT00940000161905; -.
DR InParanoid; Q9UPW8; -.
DR OrthoDB; 117172at2759; -.
DR TreeFam; TF312844; -.
DR PathwayCommons; Q9UPW8; -.
DR SignaLink; Q9UPW8; -.
DR SIGNOR; Q9UPW8; -.
DR BioGRID-ORCS; 23025; 13 hits in 1069 CRISPR screens.
DR ChiTaRS; UNC13A; human.
DR GenomeRNAi; 23025; -.
DR Pharos; Q9UPW8; Tbio.
DR PRO; PR:Q9UPW8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9UPW8; protein.
DR Bgee; ENSG00000130477; Expressed in right hemisphere of cerebellum and 153 other tissues.
DR ExpressionAtlas; Q9UPW8; baseline and differential.
DR Genevisible; Q9UPW8; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0048786; C:presynaptic active zone; TAS:ParkinsonsUK-UCL.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005516; F:calmodulin binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0019992; F:diacylglycerol binding; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0017075; F:syntaxin-1 binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0061789; P:dense core granule priming; IBA:GO_Central.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR GO; GO:0099011; P:neuronal dense core vesicle exocytosis; ISS:UniProtKB.
DR GO; GO:0007269; P:neurotransmitter secretion; ISS:ParkinsonsUK-UCL.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IDA:UniProtKB.
DR GO; GO:0099525; P:presynaptic dense core vesicle exocytosis; IBA:GO_Central.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; TAS:ParkinsonsUK-UCL.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0016081; P:synaptic vesicle docking; IBA:GO_Central.
DR GO; GO:0016188; P:synaptic vesicle maturation; IBA:GO_Central.
DR GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
DR CDD; cd00029; C1; 1.
DR CDD; cd04027; C2B_Munc13; 1.
DR Gene3D; 2.60.40.150; -; 3.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR010439; MUN_dom.
DR InterPro; IPR014770; Munc13_1.
DR InterPro; IPR014772; Munc13_dom-2.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR027080; Unc-13.
DR InterPro; IPR037302; Unc-13_C2B.
DR InterPro; IPR027082; Unc13A.
DR PANTHER; PTHR10480; PTHR10480; 1.
DR PANTHER; PTHR10480:SF1; PTHR10480:SF1; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00168; C2; 3.
DR Pfam; PF06292; MUN; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00239; C2; 3.
DR SMART; SM01145; DUF1041; 1.
DR SUPFAM; SSF49562; SSF49562; 3.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50004; C2; 3.
DR PROSITE; PS51258; MHD1; 1.
DR PROSITE; PS51259; MHD2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Differentiation; Exocytosis; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT CHAIN 1..1703
FT /note="Protein unc-13 homolog A"
FT /id="PRO_0000188573"
FT DOMAIN 1..97
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 659..783
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1093..1236
FT /note="MHD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00587"
FT DOMAIN 1345..1512
FT /note="MHD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00588"
FT DOMAIN 1526..1653
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT ZN_FING 553..603
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 186..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 320..357
FT /evidence="ECO:0000255"
FT COMPBIAS 188..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..353
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 567
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 570
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 584
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 587
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 595
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 603
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 692
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 692
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 698
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 744
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 744
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 746
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 746
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 763
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62768"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62768"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62768"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62768"
FT VARIANT 359
FT /note="A -> T (in dbSNP:rs34752754)"
FT /id="VAR_061872"
FT CONFLICT 1034
FT /note="L -> P (in Ref. 2; BAA82984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1703 AA; 193014 MW; C8F6CEBEEF8E050B CRC64;
MSLLCVGVKK AKFDGAQEKF NTYVTLKVQN VKSTTIAVRG SQPSWEQDFM FEINRLDLGL
TVEVWNKGLI WDTMVGTVWI PLRTIRQSNE EGPGEWLTLD SQVIMADSEI CGTKDPTFHR
ILLDTRFELP LDIPEEEARY WAKKLEQLNA MRDQDEYSFQ DEQDKPLPVP SNQCCNWNYF
GWGEQHNDDP DSAVDDRDSD YRSETSNSIP PPYYTTSQPN ASVHQYSVRP PPLGSRESYS
DSMHSYEEFS EPQALSPTGS SRYASSGELS QGSSQLSEDF DPDEHSLQGS DMEDERDRDS
YHSCHSSVSY HKDSPRWDQD EEELEEDLED FLEEEELPED EEELEEEEEE VPDDLGSYAQ
REDVAVAEPK DFKRISLPPA APGKEDKAPV APTEAPDMAK VAPKPATPDK VPAAEQIPEA
EPPKDEESFR PREDEEGQEG QDSMSRAKAN WLRAFNKVRM QLQEARGEGE MSKSLWFKGG
PGGGLIIIDS MPDIRKRKPI PLVSDLAMSL VQSRKAGITS ALASSTLNNE ELKNHVYKKT
LQALIYPISC TTPHNFEVWT ATTPTYCYEC EGLLWGIARQ GMRCTECGVK CHEKCQDLLN
ADCLQRAAEK SSKHGAEDRT QNIIMVLKDR MKIRERNKPE IFELIQEIFA VTKTAHTQQM
KAVKQSVLDG TSKWSAKISI TVVCAQGLQA KDKTGSSDPY VTVQVGKTKK RTKTIYGNLN
PVWEENFHFE CHNSSDRIKV RVWDEDDDIK SRVKQRFKRE SDDFLGQTII EVRTLSGEMD
VWYNLDKRTD KSAVSGAIRL HISVEIKGEE KVAPYHVQYT CLHENLFHFV TDVQNNGVVK
IPDAKGDDAW KVYYDETAQE IVDEFAMRYG VESIYQAMTH FACLSSKYMC PGVPAVMSTL
LANINAYYAH TTASTNVSAS DRFAASNFGK ERFVKLLDQL HNSLRIDLSM YRNNFPASSP
ERLQDLKSTV DLLTSITFFR MKVQELQSPP RASQVVKDCV KACLNSTYEY IFNNCHELYS
REYQTDPAKK GEVLPEEQGP SIKNLDFWSK LITLIVSIIE EDKNSYTPCL NQFPQELNVG
KISAEVMWNL FAQDMKYAME EHDKHRLCKS ADYMNLHFKV KWLYNEYVTE LPAFKDRVPE
YPAWFEPFVI QWLDENEEVS RDFLHGALER DKKDGFQQTS EHALFSCSVV DVFSQLNQSF
EIIKKLECPD PQIVGHYMRR FAKTISNVLL QYADIISKDF ASYCSKEKEK VPCILMNNTQ
QLRVQLEKMF EAMGGKELDA EASDILKELQ VKLNNVLDEL SRVFATSFQP HIEECVKQMG
DILSQVKGTG NVPASACSSV AQDADNVLQP IMDLLDSNLT LFAKICEKTV LKRVLKELWK
LVMNTMEKTI VLPPLTDQTM IGNLLRKHGK GLEKGRVKLP SHSDGTQMIF NAAKELGQLS
KLKDHMVREE AKSLTPKQCA VVELALDTIK QYFHAGGVGL KKTFLEKSPD LQSLRYALSL
YTQATDLLIK TFVQTQSAQG LGVEDPVGEV SVHVELFTHP GTGEHKVTVK VVAANDLKWQ
TSGIFRPFIE VNIIGPQLSD KKRKFATKSK NNSWAPKYNE SFQFTLSADA GPECYELQVC
VKDYCFARED RTVGLAVLQL RELAQRGSAA CWLPLGRRIH MDDTGLTVLR ILSQRSNDEV
AKEFVKLKSD TRSAEEGGAA PAP
