ID HYALP_HUMAN Reviewed; 509 AA. AC P38567; Q8TC30; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 04-NOV-2026, entry version 204. DE RecName: Full=Hyaluronidase PH-20; DE Short=Hyal-PH20; DE EC=3.2.1.35; DE AltName: Full=Hyaluronoglucosaminidase PH-20; DE AltName: Full=Sperm adhesion molecule 1; DE AltName: Full=Sperm surface protein PH-20; DE Flags: Precursor; GN Name=SPAM1; Synonyms=HYAL3, PH20; 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 [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Testis; RX PubMed=8234258; DOI=10.1073/pnas.90.21.10071; RA Lin Y., Kimmel L.H., Myles D.G., Primakoff P.; RT "Molecular cloning of the human and monkey sperm surface protein PH-20."; RL Proc. Natl. Acad. Sci. U.S.A. 90:10071-10075(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION. RC TISSUE=Testis; RX PubMed=8282124; DOI=10.1016/0014-5793(93)80873-s; RA Gmachl M., Sagan S., Ketter S., Kreil G.; RT "The human sperm protein PH-20 has hyaluronidase activity."; RL FEBS Lett. 336:545-548(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=8575780; DOI=10.1006/geno.1995.9931; RA Jones M.H., Davey P.M., Aplin H., Affara N.A.; RT "Expression analysis, genomic structure, and mapping to 7q31 of the human RT sperm adhesion molecule gene SPAM1."; RL Genomics 29:796-800(1995). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; 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 [8] RP MUTAGENESIS OF ASP-146; GLU-148; ARG-211; GLU-284 AND ARG-287, AND RP GLYCOSYLATION. RX PubMed=9288901; DOI=10.1111/j.1432-1033.1997.t01-1-00810.x; RA Arming S., Strobl B., Wechselberger C., Kreil G.; RT "In vitro mutagenesis of PH-20 hyaluronidase from human sperm."; RL Eur. J. Biochem. 247:810-814(1997). RN [9] RP VARIANT GLN-5. RX PubMed=21248752; DOI=10.1038/nature09639; RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M., RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.; RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene RT PBRM1 in renal carcinoma."; RL Nature 469:539-542(2011). CC -!- FUNCTION: Involved in sperm-egg adhesion. Upon fertilization sperm must CC first penetrate a layer of cumulus cells that surrounds the egg before CC reaching the zona pellucida. The cumulus cells are embedded in a matrix CC containing hyaluronic acid which is formed prior to ovulation. This CC protein aids in penetrating the layer of cumulus cells by digesting CC hyaluronic acid. {ECO:0000269|PubMed:8282124}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D- CC glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35; CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P38567-1; Sequence=Displayed; CC Name=2; CC IsoId=P38567-2; Sequence=VSP_042714; CC -!- TISSUE SPECIFICITY: Testis. {ECO:0000269|PubMed:8234258}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9288901}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42361/SPAM1"; 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; L13781; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; S67798; AAC60607.2; -; mRNA. DR EMBL; X84347; CAA59086.1; -; mRNA. DR EMBL; AC004690; AAQ96882.1; -; Genomic_DNA. DR EMBL; CH236947; EAL24329.1; -; Genomic_DNA. DR EMBL; CH471070; EAW83606.1; -; Genomic_DNA. DR EMBL; BC026163; AAH26163.1; -; mRNA. DR CCDS; CCDS5790.1; -. [P38567-2] DR CCDS; CCDS5791.1; -. [P38567-1] DR PIR; S40465; S40465. DR RefSeq; NP_001167515.1; NM_001174044.2. [P38567-1] DR RefSeq; NP_001167516.1; NM_001174045.2. [P38567-1] DR RefSeq; NP_001167517.1; NM_001174046.2. [P38567-1] DR RefSeq; NP_003108.2; NM_003117.5. [P38567-2] DR RefSeq; NP_694859.1; NM_153189.3. [P38567-1] DR PDB; 9JUB; EM; 3.10 A; A=37-442. DR AlphaFoldDB; P38567; -. DR EMDB; EMD-61826; -. DR SMR; P38567; -. DR BioGRID; 112559; 2. DR FunCoup; P38567; 151. DR STRING; 9606.ENSP00000345849; -. DR DrugBank; DB08818; Hyaluronic acid. DR CAZy; GH56; Glycoside Hydrolase Family 56. DR GlyCosmos; P38567; 6 sites, No reported glycans. DR GlyGen; P38567; 6 sites. DR iPTMnet; P38567; -. DR PhosphoSitePlus; P38567; -. DR BioMuta; SPAM1; -. DR DMDM; 585673; -. DR MassIVE; P38567; -. DR PaxDb; 9606-ENSP00000345849; -. DR PeptideAtlas; P38567; -. DR ProteomicsDB; 55298; -. [P38567-1] DR ProteomicsDB; 55299; -. [P38567-2] DR Antibodypedia; 2991; 203 antibodies from 28 providers. DR DNASU; 6677; -. DR Ensembl; ENST00000223028.11; ENSP00000223028.7; ENSG00000106304.16. [P38567-1] DR Ensembl; ENST00000340011.9; ENSP00000345849.5; ENSG00000106304.16. [P38567-2] DR Ensembl; ENST00000402183.3; ENSP00000386028.3; ENSG00000106304.16. [P38567-2] DR Ensembl; ENST00000439500.5; ENSP00000402123.1; ENSG00000106304.16. [P38567-1] DR Ensembl; ENST00000460182.5; ENSP00000417934.1; ENSG00000106304.16. [P38567-1] DR Ensembl; ENST00000682466.1; ENSP00000508393.1; ENSG00000106304.16. [P38567-1] DR GeneID; 6677; -. DR KEGG; hsa:6677; -. DR MANE-Select; ENST00000682466.1; ENSP00000508393.1; NM_153189.3; NP_694859.1. DR UCSC; uc003vle.4; human. [P38567-1] DR AGR; HGNC:11217; -. DR ClinPGx; PA36053; -. DR CTD; 6677; -. DR DisGeNET; 6677; -. DR GeneCards; SPAM1; -. DR HGNC; HGNC:11217; SPAM1. DR HPA; ENSG00000106304; Tissue enriched (testis). DR MIM; 600930; gene. DR OpenTargets; ENSG00000106304; -. DR VEuPathDB; HostDB:ENSG00000106304; -. DR eggNOG; ENOG502R6HD; Eukaryota. DR GeneTree; ENSGT01020000230364; -. DR HOGENOM; CLU_036366_0_1_1; -. DR InParanoid; P38567; -. DR OMA; AAKLYMR; -. DR OrthoDB; 5796153at2759; -. DR PAN-GO; P38567; 3 GO annotations based on evolutionary models. DR PhylomeDB; P38567; -. DR BioCyc; MetaCyc:HS02884-MONOMER; -. DR BRENDA; 3.2.1.35; 2681. DR PathwayCommons; P38567; -. DR Reactome; R-HSA-2160916; Hyaluronan degradation. DR Reactome; R-HSA-2534343; Interaction With Cumulus Cells And The Zona Pellucida. DR Agora; ENSG00000106304; -. DR BioGRID-ORCS; 6677; 7 hits in 1134 CRISPR screens. DR GeneWiki; SPAM1; -. DR GenomeRNAi; 6677; -. DR Pharos; P38567; Tbio. DR PRO; PR:P38567; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P38567; protein. DR Bgee; ENSG00000106304; Expressed in sperm and 25 other cell types or tissues. DR ExpressionAtlas; P38567; baseline and differential. DR GO; GO:0001669; C:acrosomal vesicle; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IBA:GO_Central. DR GO; GO:0007339; P:binding of sperm to zona pellucida; TAS:ProtInc. DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:ProtInc. DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IEA:InterPro. DR GO; GO:0030214; P:hyaluronan catabolic process; IBA:GO_Central. DR FunFam; 3.20.20.70:FF:000065; Hyaluronidase; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR017853; GH_hydrolase_sf. DR InterPro; IPR018155; Hyaluronidase. DR InterPro; IPR001439; Hyaluronidase_PH20/Hyal5. DR PANTHER; PTHR11769; HYALURONIDASE; 1. DR PANTHER; PTHR11769:SF20; HYALURONIDASE PH-20; 1. DR Pfam; PF01630; Glyco_hydro_56; 1. DR PIRSF; PIRSF038193; Hyaluronidase; 1. DR PIRSF; PIRSF500773; Hyaluronidase_PH20_Hyal5; 1. DR PRINTS; PR00846; GLHYDRLASE56. DR PRINTS; PR00848; SPERMPH20. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane; KW Disulfide bond; Glycoprotein; Glycosidase; GPI-anchor; Hydrolase; KW Lipoprotein; Membrane; Proteomics identification; Reference proteome; KW Signal. FT SIGNAL 1..35 FT /evidence="ECO:0000250" FT CHAIN 36..490 FT /note="Hyaluronidase PH-20" FT /id="PRO_0000012089" FT PROPEP 491..509 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000012090" FT ACT_SITE 148 FT /note="Proton donor" FT /evidence="ECO:0000250" FT LIPID 490 FT /note="GPI-anchor amidated serine" FT /evidence="ECO:0000255" FT CARBOHYD 82 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 166 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 235 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 254 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 368 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 393 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 60..351 FT /evidence="ECO:0000250" FT DISULFID 224..238 FT /evidence="ECO:0000250" FT DISULFID 376..387 FT /evidence="ECO:0000250" FT DISULFID 381..435 FT /evidence="ECO:0000250" FT DISULFID 437..464 FT /evidence="ECO:0000250" FT VAR_SEQ 496..509 FT /note="VSILFLIISSVASL -> WRLEVWDQGISRIGFF (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_042714" FT VARIANT 5 FT /note="K -> Q (found in a renal cell carcinoma sample; FT somatic mutation)" FT /evidence="ECO:0000269|PubMed:21248752" FT /id="VAR_064756" FT VARIANT 47 FT /note="V -> A (in dbSNP:rs34633019)" FT /id="VAR_049213" FT MUTAGEN 146 FT /note="D->N: Reduces activity by 80%." FT /evidence="ECO:0000269|PubMed:9288901" FT MUTAGEN 148 FT /note="E->Q: Loss of activity." FT /evidence="ECO:0000269|PubMed:9288901" FT MUTAGEN 211 FT /note="R->G: Reduces activity by over 90%." FT /evidence="ECO:0000269|PubMed:9288901" FT MUTAGEN 284 FT /note="E->Q: Loss of activity." FT /evidence="ECO:0000269|PubMed:9288901" FT MUTAGEN 287 FT /note="R->T: Loss of activity." FT /evidence="ECO:0000269|PubMed:9288901" FT CONFLICT 48 FT /note="P -> A (in Ref. 2; AAC60607)" FT /evidence="ECO:0000305" FT CONFLICT 499 FT /note="L -> W (in Ref. 2; AAC60607)" FT /evidence="ECO:0000305" FT STRAND 48..56 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 74..77 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:9JUB" FT HELIX 122..134 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 140..145 FT /evidence="ECO:0007829|PDB:9JUB" FT TURN 159..162 FT /evidence="ECO:0007829|PDB:9JUB" FT HELIX 163..175 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 177..179 FT /evidence="ECO:0007829|PDB:9JUB" FT HELIX 181..188 FT /evidence="ECO:0007829|PDB:9JUB" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:9JUB" FT HELIX 193..208 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 214..220 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 229..233 FT /evidence="ECO:0007829|PDB:9JUB" FT HELIX 240..248 FT /evidence="ECO:0007829|PDB:9JUB" FT HELIX 250..253 FT /evidence="ECO:0007829|PDB:9JUB" FT HELIX 271..287 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 290..292 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 294..296 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 300..304 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 309..311 FT /evidence="ECO:0007829|PDB:9JUB" FT HELIX 318..321 FT /evidence="ECO:0007829|PDB:9JUB" FT HELIX 322..326 FT /evidence="ECO:0007829|PDB:9JUB" FT TURN 330..332 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 334..339 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 342..347 FT /evidence="ECO:0007829|PDB:9JUB" FT HELIX 348..357 FT /evidence="ECO:0007829|PDB:9JUB" FT HELIX 358..362 FT /evidence="ECO:0007829|PDB:9JUB" FT HELIX 363..375 FT /evidence="ECO:0007829|PDB:9JUB" FT HELIX 376..381 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 382..385 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 388..390 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 392..394 FT /evidence="ECO:0007829|PDB:9JUB" FT TURN 402..404 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 406..409 FT /evidence="ECO:0007829|PDB:9JUB" FT STRAND 415..418 FT /evidence="ECO:0007829|PDB:9JUB" FT HELIX 423..432 FT /evidence="ECO:0007829|PDB:9JUB" SQ SEQUENCE 509 AA; 57848 MW; 5ADB4739747E32E8 CRC64; MGVLKFKHIF FRSFVKSSGV SQIVFTFLLI PCCLTLNFRA PPVIPNVPFL WAWNAPSEFC LGKFDEPLDM SLFSFIGSPR INATGQGVTI FYVDRLGYYP YIDSITGVTV NGGIPQKISL QDHLDKAKKD ITFYMPVDNL GMAVIDWEEW RPTWARNWKP KDVYKNRSIE LVQQQNVQLS LTEATEKAKQ EFEKAGKDFL VETIKLGKLL RPNHLWGYYL FPDCYNHHYK KPGYNGSCFN VEIKRNDDLS WLWNESTALY PSIYLNTQQS PVAATLYVRN RVREAIRVSK IPDAKSPLPV FAYTRIVFTD QVLKFLSQDE LVYTFGETVA LGASGIVIWG TLSIMRSMKS CLLLDNYMET ILNPYIINVT LAAKMCSQVL CQEQGVCIRK NWNSSDYLHL NPDNFAIQLE KGGKFTVRGK PTLEDLEQFS EKFYCSCYST LSCKEKADVK DTDAVDVCIA DGVCIDAFLK PPMETEEPQI FYNASPSTLS ATMFIVSILF LIISSVASL //