ID SYPH_HUMAN Reviewed; 313 AA. AC P08247; B2R7L6; B7Z359; Q6P2F7; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1991, sequence version 3. DT 11-NOV-2015, entry version 144. DE RecName: Full=Synaptophysin; DE AltName: Full=Major synaptic vesicle protein p38; GN Name=SYP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3120152; DOI=10.1093/nar/15.22.9607; RA Suedhof T.C., Lottspeich F., Greengard P., Mehl E., Jahn R.; RT "The cDNA and derived amino acid sequences for rat and human RT synaptophysin."; RL Nucleic Acids Res. 15:9607-9607(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1975480; RA Oezcelik T., Lafreniere R.G., Archer B.T. III, Johnston P.A., RA Willard H.F., Francke U., Suedhof T.C.; RT "Synaptophysin: structure of the human gene and assignment to the X RT chromosome in man and mouse."; RL Am. J. Hum. Genet. 47:551-561(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9344658; DOI=10.1006/geno.1997.4941; RA Fisher S.E., Ciccodicola A., Tanaka K., Curci A., Desicato S., RA D'Urso M., Craig I.W.; RT "Sequence-based exon prediction around the synaptophysin locus reveals RT a gene-rich area containing novel genes in human proximal Xp."; RL Genomics 45:340-347(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Amygdala; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP INTERACTION WITH SRCIN1. RX PubMed=18662323; DOI=10.1111/j.1471-4159.2008.05585.x; RA Ito H., Atsuzawa K., Sudo K., Di Stefano P., Iwamoto I., Morishita R., RA Takei S., Semba R., Defilippi P., Asano T., Usuda N., Nagata K.; RT "Characterization of a multidomain adaptor protein, p140Cap, as part RT of a pre-synaptic complex."; RL J. Neurochem. 107:61-72(2008). RN [9] RP VARIANT MRXSYP ARG-217, AND VARIANTS [LARGE SCALE ANALYSIS] GLN-2; RP LEU-158; ASN-166; ASN-248; GLU-277 AND SER-293. RX PubMed=19377476; DOI=10.1038/ng.367; RA Tarpey P.S., Smith R., Pleasance E., Whibley A., Edkins S., Hardy C., RA O'Meara S., Latimer C., Dicks E., Menzies A., Stephens P., Blow M., RA Greenman C., Xue Y., Tyler-Smith C., Thompson D., Gray K., Andrews J., RA Barthorpe S., Buck G., Cole J., Dunmore R., Jones D., Maddison M., RA Mironenko T., Turner R., Turrell K., Varian J., West S., Widaa S., RA Wray P., Teague J., Butler A., Jenkinson A., Jia M., Richardson D., RA Shepherd R., Wooster R., Tejada M.I., Martinez F., Carvill G., RA Goliath R., de Brouwer A.P., van Bokhoven H., Van Esch H., Chelly J., RA Raynaud M., Ropers H.H., Abidi F.E., Srivastava A.K., Cox J., Luo Y., RA Mallya U., Moon J., Parnau J., Mohammed S., Tolmie J.L., RA Shoubridge C., Corbett M., Gardner A., Haan E., Rujirabanjerd S., RA Shaw M., Vandeleur L., Fullston T., Easton D.F., Boyle J., RA Partington M., Hackett A., Field M., Skinner C., Stevenson R.E., RA Bobrow M., Turner G., Schwartz C.E., Gecz J., Raymond F.L., RA Futreal P.A., Stratton M.R.; RT "A systematic, large-scale resequencing screen of X-chromosome coding RT exons in mental retardation."; RL Nat. Genet. 41:535-543(2009). CC -!- FUNCTION: Possibly involved in structural functions as organizing CC other membrane components or in targeting the vesicles to the CC plasma membrane. Involved in the regulation of short-term and CC long-term synaptic plasticity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homohexamer or homotetramer. Interacts with SRCIN1. CC {ECO:0000269|PubMed:18662323}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, CC synaptic vesicle membrane; Multi-pass membrane protein. Cell CC junction, synapse, synaptosome. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P08247-1; Sequence=Displayed; CC Name=2; CC IsoId=P08247-2; Sequence=VSP_056897; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Characteristic of a type of small (30-80 nm) CC neurosecretory vesicles, including presynaptic vesicles, but also CC vesicles of various neuroendocrine cells of both neuronal and CC epithelial phenotype. CC -!- DOMAIN: The calcium-binding activity is thought to be localized in CC the cytoplasmic tail of the protein. CC -!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its CC subsequent proteasomal degradation. {ECO:0000250}. CC -!- DISEASE: Mental retardation, X-linked, SYP-related (MRXSYP) CC [MIM:300802]: A disorder characterized by significantly below CC average general intellectual functioning associated with CC impairments in adaptive behavior and manifested during the CC developmental period. {ECO:0000269|PubMed:19377476}. Note=The CC disease is caused by mutations affecting the gene represented in CC this entry. CC -!- SIMILARITY: Belongs to the synaptophysin/synaptobrevin family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 MARVEL domain. {ECO:0000255|PROSITE- CC ProRule:PRU00581}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Synaptophysin entry; CC URL="https://en.wikipedia.org/wiki/Synaptophysin"; 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; X06389; CAA29686.1; -; mRNA. DR EMBL; U93305; AAB92358.1; -; Genomic_DNA. DR EMBL; AK295524; BAH12095.1; -; mRNA. DR EMBL; AK313030; BAG35863.1; -; mRNA. DR EMBL; AK315953; BAH14324.1; -; mRNA. DR EMBL; AF196779; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471224; EAW50685.1; -; Genomic_DNA. DR EMBL; BC064550; AAH64550.1; -; mRNA. DR CCDS; CCDS14321.1; -. [P08247-1] DR PIR; A35699; A35699. DR RefSeq; NP_003170.1; NM_003179.2. [P08247-1] DR RefSeq; XP_011542253.1; XM_011543951.1. [P08247-2] DR UniGene; Hs.632804; -. DR ProteinModelPortal; P08247; -. DR BioGrid; 112721; 37. DR IntAct; P08247; 1. DR STRING; 9606.ENSP00000263233; -. DR TCDB; 9.B.130.1.4; the tetraspan vesicle membrane protein (tvp) family. DR PhosphoSite; P08247; -. DR BioMuta; SYP; -. DR DMDM; 135162; -. DR MaxQB; P08247; -. DR PaxDb; P08247; -. DR PRIDE; P08247; -. DR DNASU; 6855; -. DR Ensembl; ENST00000263233; ENSP00000263233; ENSG00000102003. [P08247-1] DR Ensembl; ENST00000479808; ENSP00000418169; ENSG00000102003. [P08247-1] DR GeneID; 6855; -. DR KEGG; hsa:6855; -. DR UCSC; uc004dmz.1; human. [P08247-1] DR CTD; 6855; -. DR GeneCards; SYP; -. DR H-InvDB; HIX0203320; -. DR HGNC; HGNC:11506; SYP. DR HPA; CAB000076; -. DR HPA; CAB055505; -. DR HPA; HPA002858; -. DR MIM; 300802; phenotype. DR MIM; 313475; gene. DR neXtProt; NX_P08247; -. DR Orphanet; 777; X-linked non-syndromic intellectual disability. DR PharmGKB; PA36288; -. DR eggNOG; ENOG410IDYC; Eukaryota. DR eggNOG; ENOG4111J4N; LUCA. DR GeneTree; ENSGT00390000010039; -. DR HOGENOM; HOG000252913; -. DR HOVERGEN; HBG006681; -. DR InParanoid; P08247; -. DR OMA; GWAAPFM; -. DR OrthoDB; EOG7WT43S; -. DR PhylomeDB; P08247; -. DR TreeFam; TF315804; -. DR ChiTaRS; SYP; human. DR GeneWiki; Synaptophysin; -. DR GenomeRNAi; 6855; -. DR NextBio; 26757; -. DR PRO; PR:P08247; -. DR Proteomes; UP000005640; Chromosome X. DR Bgee; P08247; -. DR CleanEx; HS_SYP; -. DR ExpressionAtlas; P08247; baseline and differential. DR Genevisible; P08247; HS. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0060076; C:excitatory synapse; IEA:Ensembl. DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; NAS:UniProtKB. DR GO; GO:0043005; C:neuron projection; ISS:ParkinsonsUK-UCL. DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl. DR GO; GO:0008021; C:synaptic vesicle; ISS:ParkinsonsUK-UCL. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043195; C:terminal bouton; IEA:Ensembl. DR GO; GO:0015485; F:cholesterol binding; IDA:UniProtKB. DR GO; GO:0043621; F:protein self-association; TAS:ParkinsonsUK-UCL. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl. DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB. DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISS:UniProtKB. DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IBA:GO_Central. DR GO; GO:2000474; P:regulation of opioid receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; ISS:UniProtKB. DR GO; GO:0016188; P:synaptic vesicle maturation; NAS:UniProtKB. DR GO; GO:0048499; P:synaptic vesicle membrane organization; NAS:UniProtKB. DR InterPro; IPR008253; Marvel. DR InterPro; IPR001285; Synaptophysin/porin. DR InterPro; IPR028714; SYP. DR PANTHER; PTHR10306; PTHR10306; 2. DR PANTHER; PTHR10306:SF10; PTHR10306:SF10; 2. DR Pfam; PF01284; MARVEL; 1. DR PRINTS; PR00220; SYNAPTOPHYSN. DR PROSITE; PS51225; MARVEL; 1. DR PROSITE; PS00604; SYNAPTOP; 1. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cell junction; Complete proteome; KW Cytoplasmic vesicle; Disease mutation; Glycoprotein; Membrane; KW Mental retardation; Phosphoprotein; Polymorphism; Reference proteome; KW Repeat; Synapse; Synaptosome; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT CHAIN 1 313 Synaptophysin. FT /FTId=PRO_0000179161. FT TOPO_DOM 1 25 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 26 49 Helical. {ECO:0000255}. FT TOPO_DOM 50 106 Vesicular. {ECO:0000255}. FT TRANSMEM 107 130 Helical. {ECO:0000255}. FT TOPO_DOM 131 137 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 138 161 Helical. {ECO:0000255}. FT TOPO_DOM 162 199 Vesicular. {ECO:0000255}. FT TRANSMEM 200 223 Helical. {ECO:0000255}. FT TOPO_DOM 224 313 Cytoplasmic. {ECO:0000255}. FT DOMAIN 21 227 MARVEL. {ECO:0000255|PROSITE- FT ProRule:PRU00581}. FT REGION 254 305 Repeats, Gly-rich. FT MOD_RES 81 81 Phosphotyrosine. FT {ECO:0000250|UniProtKB:Q62277}. FT CARBOHYD 59 59 N-linked (GlcNAc...). {ECO:0000255}. FT VAR_SEQ 1 118 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_056897. FT VARIANT 2 2 L -> Q. {ECO:0000269|PubMed:19377476}. FT /FTId=VAR_062983. FT VARIANT 158 158 S -> L. {ECO:0000269|PubMed:19377476}. FT /FTId=VAR_062984. FT VARIANT 166 166 D -> N. {ECO:0000269|PubMed:19377476}. FT /FTId=VAR_062985. FT VARIANT 217 217 G -> R (in MRXSYP). FT {ECO:0000269|PubMed:19377476}. FT /FTId=VAR_062986. FT VARIANT 248 248 D -> N. {ECO:0000269|PubMed:19377476}. FT /FTId=VAR_062987. FT VARIANT 277 277 D -> E (in an individual affected by FT mental retardation; unknown pathological FT role). {ECO:0000269|PubMed:19377476}. FT /FTId=VAR_062988. FT VARIANT 293 293 G -> S (in an individual affected by FT mental retardation; unknown pathological FT role; dbSNP:rs139475570). FT {ECO:0000269|PubMed:19377476}. FT /FTId=VAR_062989. FT CONFLICT 196 196 P -> L (in Ref. 7; AAH64550). FT {ECO:0000305}. SQ SEQUENCE 313 AA; 33845 MW; 592289C43B12EFA7 CRC64; MLLLADMDVV NQLVAGGQFR VVKEPLGFVK VLQWVFAIFA FATCGSYSGE LQLSVDCANK TESDLSIEVE FEYPFRLHQV YFDAPTCRGG TTKVFLVGDY SSSAEFFVTV AVFAFLYSMG ALATYIFLQN KYRENNKGPM LDFLATAVFA FMWLVSSSAW AKGLSDVKMA TDPENIIKEM PVCRQTGNTC KELRDPVTSG LNTSVVFGFL NLVLWVGNLW FVFKETGWAA PFLRAPPGAP EKQPAPGDAY GDAGYGQGPG GYGPQDSYGP QGGYQPDYGQ PAGSGGSGYG PQGDYGQQGY GPQGAPTSFS NQM //