AMPH_HUMAN
ID AMPH_HUMAN Reviewed; 695 AA.
AC P49418; A4D1X8; A4D1X9; O43538; Q75MJ8; Q75MK5; Q75MM3; Q8N4G0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Amphiphysin;
GN Name=AMPH; Synonyms=AMPH1;
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).
RC TISSUE=Cerebellum;
RX PubMed=8076697; DOI=10.1016/0014-5793(94)00826-4;
RA David C., Solimena M., de Camilli P.;
RT "Autoimmunity in stiff-man syndrome with breast cancer is targeted to the
RT C-terminal region of human amphiphysin, a protein similar to the yeast
RT proteins, Rvs167 and Rvs161.";
RL FEBS Lett. 351:73-79(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=7757077; DOI=10.1093/hmg/4.2.265;
RA Yamamoto R., Li X., Winter S., Francke U., Kilimann M.W.;
RT "Primary structure of human amphiphysin, the dominant autoantigen of
RT paraneoplastic stiff-man syndrome, and mapping of its gene (AMPH) to
RT chromosome 7p13-p14.";
RL Hum. Mol. Genet. 4:265-268(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
RX PubMed=9513187; DOI=10.1007/bf03401727;
RA Floyd S.R., Butler M.H., Cremona O., David C., Freyberg Z., Zhang X.,
RA Solimena M., Tokunaga A., Ishizu H., Tsutsui K., De Camilli P.V.;
RT "Expression of amphiphysin I, an autoantigen of paraneoplastic neurological
RT syndromes, in breast cancer.";
RL Mol. Med. 4:29-39(1998).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-496.
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH AP2B1.
RX PubMed=16903783; DOI=10.1371/journal.pbio.0040262;
RA Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y.,
RA Mills I.G., Benmerah A., McMahon H.T.;
RT "Role of the AP2 beta-appendage hub in recruiting partners for clathrin-
RT coated vesicle assembly.";
RL PLoS Biol. 4:E262-E262(2006).
RN [9]
RP INTERACTION WITH REPS1 AND SGIP1.
RX PubMed=20946875; DOI=10.1016/j.bbrc.2010.10.045;
RA Dergai O., Novokhatska O., Dergai M., Skrypkina I., Tsyba L., Moreau J.,
RA Rynditch A.;
RT "Intersectin 1 forms complexes with SGIP1 and Reps1 in clathrin-coated
RT pits.";
RL Biochem. Biophys. Res. Commun. 402:408-413(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 322-330 IN COMPLEX WITH AP2A2.
RX PubMed=12057195; DOI=10.1016/s0969-2126(02)00784-0;
RA Brett T.J., Traub L.M., Fremont D.H.;
RT "Accessory protein recruitment motifs in clathrin-mediated endocytosis.";
RL Structure 10:797-809(2002).
CC -!- FUNCTION: May participate in mechanisms of regulated exocytosis in
CC synapses and certain endocrine cell types. May control the properties
CC of the membrane associated cytoskeleton.
CC -!- SUBUNIT: Heterodimer with BIN1 (By similarity). Binds SH3GLB1 (By
CC similarity). Interacts with REPS1 and SGIP1(PubMed:20946875). Binds
CC AP2A2 (PubMed:12057195). Interacts with AP2B1 (PubMed:16903783).
CC Interacts with DNM1 AND SYNJ1 (By similarity).
CC {ECO:0000250|UniProtKB:O08838, ECO:0000269|PubMed:12057195,
CC ECO:0000269|PubMed:16903783, ECO:0000269|PubMed:20946875}.
CC -!- INTERACTION:
CC P49418; Q0P5N6: ARL16; NbExp=7; IntAct=EBI-7121510, EBI-10186132;
CC P49418; Q86V38: ATN1; NbExp=3; IntAct=EBI-7121510, EBI-11954292;
CC P49418; Q05D60: DEUP1; NbExp=3; IntAct=EBI-7121510, EBI-748597;
CC P49418; Q08209-2: PPP3CA; NbExp=3; IntAct=EBI-7121510, EBI-11959013;
CC P49418; P48454: PPP3CC; NbExp=3; IntAct=EBI-7121510, EBI-2827192;
CC P49418; P54274: TERF1; NbExp=2; IntAct=EBI-7121510, EBI-710997;
CC P49418; P08081: Clta; Xeno; NbExp=3; IntAct=EBI-7121510, EBI-916140;
CC P49418; P69682: Necap1; Xeno; NbExp=3; IntAct=EBI-7121510, EBI-7592718;
CC P49418; Q9CR95: Necap1; Xeno; NbExp=6; IntAct=EBI-7121510, EBI-7592476;
CC P49418; P58197: Tfap2a; Xeno; NbExp=2; IntAct=EBI-7121510, EBI-7069641;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
CC Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=128 kDa;
CC IsoId=P49418-1; Sequence=Displayed;
CC Name=2; Synonyms=108 kDa;
CC IsoId=P49418-2; Sequence=VSP_000245;
CC -!- TISSUE SPECIFICITY: Neurons, certain endocrine cell types and
CC spermatocytes.
CC -!- MISCELLANEOUS: Antibodies against AMPH are detected in patients with
CC stiff-man syndrome, a rare disease of the central nervous system
CC characterized by progressive rigidity of the body musculature with
CC superimposed painful spasms.
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DR EMBL; U07616; AAA21865.1; -; mRNA.
DR EMBL; X81438; CAA57197.1; -; mRNA.
DR EMBL; AF034996; AAC02977.1; -; mRNA.
DR EMBL; AC011309; AAS07391.1; -; Genomic_DNA.
DR EMBL; AC012490; AAS07563.1; -; Genomic_DNA.
DR EMBL; AC007245; AAS07541.1; -; Genomic_DNA.
DR EMBL; CH236951; EAL23989.1; -; Genomic_DNA.
DR EMBL; CH236951; EAL23990.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW94110.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW94111.1; -; Genomic_DNA.
DR EMBL; BC034376; AAH34376.1; -; mRNA.
DR CCDS; CCDS47574.1; -. [P49418-2]
DR CCDS; CCDS5456.1; -. [P49418-1]
DR PIR; S62400; S62400.
DR RefSeq; NP_001626.1; NM_001635.3. [P49418-1]
DR RefSeq; NP_647477.1; NM_139316.2. [P49418-2]
DR PDB; 1KY7; X-ray; 2.15 A; P=322-330.
DR PDB; 1UTC; X-ray; 2.30 A; P/Q=379-387.
DR PDB; 3SOG; X-ray; 2.30 A; A=34-236.
DR PDB; 4ATM; X-ray; 1.78 A; A=1-242.
DR PDB; 5M5S; X-ray; 1.88 A; E/F/G/H=349-358.
DR PDB; 5M61; X-ray; 1.84 A; E/F/G/H=349-360.
DR PDBsum; 1KY7; -.
DR PDBsum; 1UTC; -.
DR PDBsum; 3SOG; -.
DR PDBsum; 4ATM; -.
DR PDBsum; 5M5S; -.
DR PDBsum; 5M61; -.
DR AlphaFoldDB; P49418; -.
DR SMR; P49418; -.
DR BioGRID; 106770; 58.
DR DIP; DIP-40729N; -.
DR ELM; P49418; -.
DR IntAct; P49418; 27.
DR MINT; P49418; -.
DR STRING; 9606.ENSP00000348602; -.
DR iPTMnet; P49418; -.
DR PhosphoSitePlus; P49418; -.
DR BioMuta; AMPH; -.
DR DMDM; 1351924; -.
DR EPD; P49418; -.
DR jPOST; P49418; -.
DR MassIVE; P49418; -.
DR MaxQB; P49418; -.
DR PaxDb; P49418; -.
DR PeptideAtlas; P49418; -.
DR PRIDE; P49418; -.
DR ProteomicsDB; 56004; -. [P49418-1]
DR ProteomicsDB; 56005; -. [P49418-2]
DR Antibodypedia; 3258; 494 antibodies from 41 providers.
DR DNASU; 273; -.
DR Ensembl; ENST00000325590.9; ENSP00000317441.5; ENSG00000078053.17. [P49418-2]
DR Ensembl; ENST00000356264.7; ENSP00000348602.2; ENSG00000078053.17. [P49418-1]
DR GeneID; 273; -.
DR KEGG; hsa:273; -.
DR MANE-Select; ENST00000356264.7; ENSP00000348602.2; NM_001635.4; NP_001626.1.
DR UCSC; uc003tgu.4; human. [P49418-1]
DR CTD; 273; -.
DR DisGeNET; 273; -.
DR GeneCards; AMPH; -.
DR HGNC; HGNC:471; AMPH.
DR HPA; ENSG00000078053; Group enriched (brain, pituitary gland, retina).
DR MIM; 600418; gene.
DR neXtProt; NX_P49418; -.
DR OpenTargets; ENSG00000078053; -.
DR PharmGKB; PA24779; -.
DR VEuPathDB; HostDB:ENSG00000078053; -.
DR eggNOG; KOG3771; Eukaryota.
DR GeneTree; ENSGT00950000182882; -.
DR HOGENOM; CLU_017859_4_0_1; -.
DR InParanoid; P49418; -.
DR OMA; QADQSMI; -.
DR OrthoDB; 1366218at2759; -.
DR PhylomeDB; P49418; -.
DR TreeFam; TF313542; -.
DR PathwayCommons; P49418; -.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; P49418; -.
DR SIGNOR; P49418; -.
DR BioGRID-ORCS; 273; 8 hits in 1072 CRISPR screens.
DR ChiTaRS; AMPH; human.
DR EvolutionaryTrace; P49418; -.
DR GeneWiki; Amphiphysin; -.
DR GenomeRNAi; 273; -.
DR Pharos; P49418; Tbio.
DR PRO; PR:P49418; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P49418; protein.
DR Bgee; ENSG00000078053; Expressed in middle temporal gyrus and 144 other tissues.
DR ExpressionAtlas; P49418; baseline and differential.
DR Genevisible; P49418; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031256; C:leading edge membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005543; F:phospholipid binding; IDA:FlyBase.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0006897; P:endocytosis; TAS:ProtInc.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR CDD; cd12140; SH3_Amphiphysin_I; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR003005; Amphiphysin.
DR InterPro; IPR003017; Amphiphysin_1.
DR InterPro; IPR035470; Amphiphysin_I_SH3.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR46514:SF2; PTHR46514:SF2; 1.
DR Pfam; PF03114; BAR; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR01251; AMPHIPHYSIN.
DR PRINTS; PR01252; AMPHIPHYSIN1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Membrane; Phosphoprotein;
KW Reference proteome; SH3 domain; Synapse.
FT CHAIN 1..695
FT /note="Amphiphysin"
FT /id="PRO_0000192947"
FT DOMAIN 24..240
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT DOMAIN 622..695
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 244..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 10..83
FT /evidence="ECO:0000255"
FT COILED 144..191
FT /evidence="ECO:0000255"
FT COMPBIAS 260..276
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..309
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 280
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7TQF7"
FT VAR_SEQ 425..466
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9513187"
FT /id="VSP_000245"
FT VARIANT 218
FT /note="K -> E (in dbSNP:rs35166354)"
FT /id="VAR_053004"
FT VARIANT 376
FT /note="M -> I (in dbSNP:rs17171345)"
FT /id="VAR_053005"
FT VARIANT 496
FT /note="K -> T (in dbSNP:rs35024632)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_053006"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:4ATM"
FT HELIX 24..84
FT /evidence="ECO:0007829|PDB:4ATM"
FT HELIX 92..115
FT /evidence="ECO:0007829|PDB:4ATM"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:4ATM"
FT HELIX 128..156
FT /evidence="ECO:0007829|PDB:4ATM"
FT HELIX 163..196
FT /evidence="ECO:0007829|PDB:4ATM"
FT HELIX 198..237
FT /evidence="ECO:0007829|PDB:4ATM"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:1UTC"
SQ SEQUENCE 695 AA; 76257 MW; 78B4F75AB75BA357 CRC64;
MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE AEGTRLQREL
RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE KCDVLWEDFH QKLVDGSLLT
LDTYLGQFPD IKNRIAKRSR KLVDYDSARH HLEALQSSKR KDESRISKAE EEFQKAQKVF
EEFNVDLQEE LPSLWSRRVG FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD
KAFTIQGAPS DSGPLRIAKT PSPPEEPSPL PSPTASPNHT LAPASPAPAR PRSPSQTRKG
PPVPPLPKVT PTKELQQENI ISFFEDNFVP EISVTTPSQN EVPEVKKEET LLDLDFDPFK
PEVTPAGSAG VTHSPMSQTL PWDLWTTSTD LVQPASGGSF NGFTQPQDTS LFTMQTDQSM
ICNLAESEQA PPTEPKAEEP LAAVTPAVGL DLGMDTRAEE PVEEAVIIPG ADADAAVGTL
VSAAEGAPGE EAEAEKATVP AGEGVSLEEA KIGTETTEGA ESAQPEAEEL EATVPQEKVI
PSVVIEPASN HEEEGENEIT IGAEPKETTE DAAPPGPTSE TPELATEQKP IQDPQPTPSA
PAMGAADQLA SAREASQELP PGFLYKVETL HDFEAANSDE LTLQRGDVVL VVPSDSEADQ
DAGWLVGVKE SDWLQYRDLA TYKGLFPENF TRRLD
