ID APH1A_HUMAN Reviewed; 265 AA. AC Q96BI3; B4DQK0; Q5TB22; Q5TB23; Q969R6; Q9BVG0; Q9Y386; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 11-DEC-2013, entry version 113. DE RecName: Full=Gamma-secretase subunit APH-1A; DE Short=APH-1a; DE AltName: Full=Aph-1alpha; DE AltName: Full=Presenilin-stabilization factor; GN Name=APH1A; Synonyms=PSF; ORFNames=CGI-78, UNQ579/PRO1141; 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), FUNCTION, AND INTERACTION WITH RP PSEN1; PSEN2 AND NCSTN. RC TISSUE=Glioblastoma; RX PubMed=12297508; DOI=10.1074/jbc.M208164200; RA Lee S.-F., Shah S., Li H., Yu C., Han W., Yu G.; RT "Mammalian APH-1 interacts with presenilin and nicastrin and is RT required for intramembrane proteolysis of amyloid-beta precursor RT protein and Notch."; RL J. Biol. Chem. 277:45013-45019(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RA Lee H.-J., Kim T.-W.; RT "PSF is essential for gamma-secretase activity and stabilization of RT presenilin and nicastrin."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., RA Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale RT effort to identify novel human secreted and transmembrane proteins: a RT bioinformatics assessment."; RL Genome Res. 13:2265-2270(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Retinoblastoma, and Thyroid; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [7] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Adrenal gland, Brain, Cervix, Eye, Glial tumor, and Lung; 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 [9] RP TISSUE SPECIFICITY. RX PubMed=12110170; DOI=10.1016/S1534-5807(02)00189-2; RA Francis R., McGrath G., Zhang J., Ruddy D.A., Sym M., Apfeld J., RA Nicoll M., Maxwell M., Hai B., Ellis M.C., Parks A.L., Xu W., Li J., RA Gurney M., Myers R.L., Himes C.S., Hiebsch R., Ruble C., Nye J.S., RA Curtis D.; RT "aph-1 and pen-2 are required for Notch pathway signaling, gamma- RT secretase cleavage of betaAPP, and presenilin protein accumulation."; RL Dev. Cell 3:85-97(2002). RN [10] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=12522139; DOI=10.1074/jbc.C200648200; RA Luo W.-J., Wang H., Li H., Kim B.S., Shah S., Lee H.-J., RA Thinakaran G., Kim T.-W., Yu G., Xu H.; RT "PEN-2 and APH-1 coordinately regulate proteolytic processing of RT presenilin 1."; RL J. Biol. Chem. 278:7850-7854(2003). RN [11] RP SUBCELLULAR LOCATION, AND INTERACTION WITH PSEN1. RX PubMed=12471034; DOI=10.1074/jbc.M209499200; RA Gu Y., Chen F., Sanjo N., Kawarai T., Hasegawa H., Duthie M., Li W., RA Ruan X., Luthra A., Mount H.T.J., Tandon A., Fraser P.E., RA St George-Hyslop P.H.; RT "APH-1 interacts with mature and immature forms of presenilins and RT nicastrin and may play a role in maturation of presenilin.nicastrin RT complexes."; RL J. Biol. Chem. 278:7374-7380(2003). RN [12] RP FUNCTION IN THE GAMMA-SECRETASE COMPLEX. RX PubMed=12763021; DOI=10.1016/S0006-291X(03)00797-6; RA Marlow L., Canet R.M., Haugabook S.J., Hardy J.A., Lahiri D.K., RA Sambamurti K.; RT "APH1, PEN2, and nicastrin increase Abeta levels and gamma-secretase RT activity."; RL Biochem. Biophys. Res. Commun. 305:502-509(2003). RN [13] RP COMPONENT OF A GAMMA-SECRETASE COMPLEX WITH PEN2; PSEN1/PSEN2 AND RP NCSTN. RX PubMed=12740439; DOI=10.1073/pnas.1037392100; RA Kimberly W.T., LaVoie M.J., Ostaszewski B.L., Ye W., Wolfe M.S., RA Selkoe D.J.; RT "Gamma-secretase is a membrane protein complex comprised of RT presenilin, nicastrin, Aph-1, and Pen-2."; RL Proc. Natl. Acad. Sci. U.S.A. 100:6382-6387(2003). RN [14] RP ENZYME ACTIVITY OF A GAMMA-SECRETASE COMPLEX. RX PubMed=12679784; DOI=10.1038/ncb960; RA Edbauer D., Winkler E., Regula J.T., Pesold B., Steiner H., Haass C.; RT "Reconstitution of gamma-secretase activity."; RL Nat. Cell Biol. 5:486-488(2003). RN [15] RP SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY. RX PubMed=14593096; DOI=10.1074/jbc.M310505200; RA Fortna R.R., Crystal A.S., Morais V.A., Pijak D.S., Lee V.M., RA Doms R.W.; RT "Membrane topology and nicastrin-enhanced endoproteolysis of APH-1, a RT component of the gamma-secretase complex."; RL J. Biol. Chem. 279:3685-3693(2004). CC -!- FUNCTION: Essential subunit of the gamma-secretase complex, an CC endoprotease complex that catalyzes the intramembrane cleavage of CC integral proteins such as Notch receptors and APP (beta-amyloid CC precursor protein). It probably represents a stabilizing cofactor CC for the presenilin homodimer that promotes the formation of a CC stable complex. CC -!- SUBUNIT: Component of the gamma-secretase complex, a complex CC composed of a presenilin homodimer (PSEN1 or PSEN2), nicastrin CC (NCSTN), APH1 (APH1A or APH1B) and PEN2. Such minimal complex is CC sufficient for secretase activity, although other components may CC exist. CC -!- INTERACTION: CC Q92542:NCSTN; NbExp=3; IntAct=EBI-2606935, EBI-998440; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass CC membrane protein. Golgi apparatus, Golgi stack membrane; Multi- CC pass membrane protein. Note=Predominantly located in the CC endoplasmic reticulum and in the cis-Golgi. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=L, Aph-alpha1; CC IsoId=Q96BI3-1; Sequence=Displayed; CC Name=2; Synonyms=S, Aph-alpha2; CC IsoId=Q96BI3-2; Sequence=VSP_008355, VSP_008356; CC Name=3; CC IsoId=Q96BI3-3; Sequence=VSP_045424; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in leukocytes, CC lung, placenta, small intestine, liver, kidney, spleen thymus, CC skeletal muscle, heart and brain. Isoform 1 and isoform 2 are CC nearly expressed at the same level. CC -!- SIMILARITY: Belongs to the APH-1 family. CC -!- SEQUENCE CAUTION: CC Sequence=AAD34072.1; Type=Frameshift; Positions=243; CC Sequence=AAN63816.1; Type=Frameshift; Positions=243; 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; AF508787; AAN63816.1; ALT_FRAME; mRNA. DR EMBL; AY113698; AAM61955.1; -; mRNA. DR EMBL; AY113699; AAM61956.1; -; mRNA. DR EMBL; AF151835; AAD34072.1; ALT_FRAME; mRNA. DR EMBL; AY358951; AAQ89310.1; -; mRNA. DR EMBL; AK027879; BAG51389.1; -; mRNA. DR EMBL; AK075295; BAC11529.1; -; mRNA. DR EMBL; AK298832; BAG60962.1; -; mRNA. DR EMBL; AL138795; CAI22811.1; -; Genomic_DNA. DR EMBL; AL138795; CAI22812.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53565.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53566.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53567.1; -; Genomic_DNA. DR EMBL; BC001230; AAH01230.1; -; mRNA. DR EMBL; BC008732; AAH08732.1; -; mRNA. DR EMBL; BC009501; AAH09501.1; -; mRNA. DR EMBL; BC015568; AAH15568.1; -; mRNA. DR EMBL; BC017699; AAH17699.1; -; mRNA. DR EMBL; BC020590; AAH20590.1; -; mRNA. DR IPI; IPI00059964; -. DR IPI; IPI00844196; -. DR RefSeq; NP_001071096.1; NM_001077628.2. DR RefSeq; NP_001230700.1; NM_001243771.1. DR RefSeq; NP_001230701.1; NM_001243772.1. DR RefSeq; NP_057106.2; NM_016022.3. DR UniGene; Hs.108408; -. DR UniGene; Hs.735911; -. DR ProteinModelPortal; Q96BI3; -. DR IntAct; Q96BI3; 16. DR STRING; 9606.ENSP00000358105; -. DR BindingDB; Q96BI3; -. DR ChEMBL; CHEMBL2094135; -. DR PhosphoSite; Q96BI3; -. DR DMDM; 37077707; -. DR PaxDb; Q96BI3; -. DR PRIDE; Q96BI3; -. DR DNASU; 51107; -. DR Ensembl; ENST00000360244; ENSP00000353380; ENSG00000117362. DR Ensembl; ENST00000369109; ENSP00000358105; ENSG00000117362. DR Ensembl; ENST00000414276; ENSP00000397473; ENSG00000117362. DR Ensembl; ENST00000581822; ENSP00000464062; ENSG00000266334. DR Ensembl; ENST00000582205; ENSP00000463082; ENSG00000266334. DR Ensembl; ENST00000584744; ENSP00000464506; ENSG00000266334. DR GeneID; 51107; -. DR KEGG; hsa:51107; -. DR UCSC; uc010pbx.2; human. DR CTD; 51107; -. DR GeneCards; GC01M150237; -. DR HGNC; HGNC:29509; APH1A. DR HPA; CAB037272; -. DR MIM; 607629; gene. DR neXtProt; NX_Q96BI3; -. DR PharmGKB; PA142672599; -. DR eggNOG; NOG300477; -. DR HOGENOM; HOG000007541; -. DR HOVERGEN; HBG050541; -. DR InParanoid; Q96BI3; -. DR KO; K06172; -. DR OMA; FIAFGPP; -. DR PhylomeDB; Q96BI3; -. DR Reactome; REACT_111102; Signal Transduction. DR Reactome; REACT_116125; Disease. DR Reactome; REACT_691; A third proteolytic cleavage releases NICD. DR SignaLink; Q96BI3; -. DR GenomeRNAi; 51107; -. DR NextBio; 53845; -. DR PRO; PR:Q96BI3; -. DR ArrayExpress; Q96BI3; -. DR Bgee; Q96BI3; -. DR CleanEx; HS_APH1A; -. DR Genevestigator; Q96BI3; -. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IDA:HGNC. DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005887; C:integral to plasma membrane; IDA:HGNC. DR GO; GO:0004175; F:endopeptidase activity; IEA:Ensembl. DR GO; GO:0042987; P:amyloid precursor protein catabolic process; IMP:UniProtKB. DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:HGNC. DR GO; GO:0031293; P:membrane protein intracellular domain proteolysis; IMP:UniProtKB. DR GO; GO:0001656; P:metanephros development; IEA:Ensembl. DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome. DR GO; GO:0007220; P:Notch receptor processing; IMP:UniProtKB. DR GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome. DR GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome. DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:HGNC. DR GO; GO:0016485; P:protein processing; IDA:HGNC. DR InterPro; IPR009294; Aph-1. DR PANTHER; PTHR12889; PTHR12889; 1. DR Pfam; PF06105; Aph-1; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Endoplasmic reticulum; KW Golgi apparatus; Membrane; Notch signaling pathway; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 265 Gamma-secretase subunit APH-1A. FT /FTId=PRO_0000221050. FT TOPO_DOM 1 2 Lumenal (Potential). FT TRANSMEM 3 23 Helical; Name=1; (Potential). FT TOPO_DOM 24 31 Cytoplasmic (Potential). FT TRANSMEM 32 52 Helical; Name=2; (Potential). FT TOPO_DOM 53 68 Lumenal (Potential). FT TRANSMEM 69 89 Helical; Name=3; (Potential). FT TOPO_DOM 90 118 Cytoplasmic (Potential). FT TRANSMEM 119 139 Helical; Name=4; (Potential). FT TOPO_DOM 140 158 Lumenal (Potential). FT TRANSMEM 159 179 Helical; Name=5; (Potential). FT TOPO_DOM 180 186 Cytoplasmic (Potential). FT TRANSMEM 187 207 Helical; Name=6; (Potential). FT TOPO_DOM 208 213 Lumenal (Potential). FT TRANSMEM 214 234 Helical; Name=7; (Potential). FT TOPO_DOM 235 265 Cytoplasmic (Potential). FT VAR_SEQ 39 120 AFFWLVSLLLASVVWFILVHVTDRSDARLQYGLLIFGAAVS FT VLLQEVFRFAYYKLLKKADEGLASLSEDGRSPISIRQMAYV FT -> RCSALPTTSCLI (in isoform 3). FT /FTId=VSP_045424. FT VAR_SEQ 246 247 RR -> KD (in isoform 2). FT /FTId=VSP_008355. FT VAR_SEQ 248 265 Missing (in isoform 2). FT /FTId=VSP_008356. FT CONFLICT 236 236 L -> I (in Ref. 8; AAH01230). SQ SEQUENCE 265 AA; 28996 MW; 8E37984A1DECC263 CRC64; MGAAVFFGCT FVAFGPAFAL FLITVAGDPL RVIILVAGAF FWLVSLLLAS VVWFILVHVT DRSDARLQYG LLIFGAAVSV LLQEVFRFAY YKLLKKADEG LASLSEDGRS PISIRQMAYV SGLSFGIISG VFSVINILAD ALGPGVVGIH GDSPYYFLTS AFLTAAIILL HTFWGVVFFD ACERRRYWAL GLVVGSHLLT SGLTFLNPWY EASLLPIYAV TVSMGLWAFI TAGGSLRSIQ RSLLCRRQED SRVMVYSALR IPPED //