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1.C.50.1.2
The Alzheimer’s disease amyloid β-protein (Aβpeptide; precursor: App, γ-secretase) (42aas) (3-d structure is known from NMR spectroscopy (1Z0Q_A; Jang et al., 2007; Zheng et al., 2008)).  This peptide is derived from the amyloid βA4 protein isoform f (NP_001129602)) which forms variable oligomeric toxic pores leading to cytosolic calcium elevation and Alzheimer's disease (Demuro et al., 2011). The monomer of Ass1-42 normally activates type-1 insulin-like growth factor receptors and enhances glucose uptake in neurons and peripheral cells by promoting the translocation of the Glut3 glucose transporter from the cytosol to the plasma membrane (Giuffrida et al. 2015).

Accession Number:P05067
Protein Name:Amyloid beta A4 protein
Length:770
Molecular Weight:86943.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Membrane1 / Single-pass type I membrane protein2
Substrate ions

Cross database links:

Genevestigator: P05067
eggNOG: prNOG05256
DIP: DIP-574N
RefSeq: NP_000475.1    NP_001129601.1    NP_001129602.1    NP_958816.1    NP_958817.1   
Entrez Gene ID: 351   
Pfam: PF02177    PF10515    PF03494    PF00014   
Drugbank: Drugbank Link   
OMIM: 104300  phenotype
104760  gene+phenotype
605714  phenotype
KEGG: hsa:351   

Gene Ontology

GO:0030424 C:axon
GO:0009986 C:cell surface
GO:0005905 C:coated pit
GO:0043198 C:dendritic shaft
GO:0043197 C:dendritic spine
GO:0005576 C:extracellular region
GO:0005794 C:Golgi apparatus
GO:0005887 C:integral to plasma membrane
GO:0031093 C:platelet alpha granule lumen
GO:0033130 F:acetylcholine receptor binding
GO:0003677 F:DNA binding
GO:0008201 F:heparin binding
GO:0042802 F:identical protein binding
GO:0046872 F:metal ion binding
GO:0004867 F:serine-type endopeptidase inhibitor activity
GO:0008344 P:adult locomotory behavior
GO:0008088 P:axon cargo transport
GO:0016199 P:axon midline choice point recognition
GO:0007155 P:cell adhesion
GO:0006878 P:cellular copper ion homeostasis
GO:0048669 P:collateral sprouting in the absence of injury
GO:0016358 P:dendrite development
GO:0006897 P:endocytosis
GO:0030198 P:extracellular matrix organization
GO:0000085 P:G2 phase of mitotic cell cycle
GO:0035235 P:ionotropic glutamate receptor signaling pat...
GO:0007617 P:mating behavior
GO:0006378 P:mRNA polyadenylation
GO:0051402 P:neuron apoptosis
GO:0016322 P:neuron remodeling
GO:0007219 P:Notch signaling pathway
GO:0045931 P:positive regulation of mitotic cell cycle
GO:0006468 P:protein amino acid phosphorylation
GO:0007176 P:regulation of epidermal growth factor recep...
GO:0040014 P:regulation of multicellular organism growth
GO:0050803 P:regulation of synapse structure and activity
GO:0006417 P:regulation of translation
GO:0008542 P:visual learning

References (129)

[1] “The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor.”  Kang J.et.al.   2881207
[2] “A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors.”  Ponte P.et.al.   2893289
[3] “The PreA4(695) precursor protein of Alzheimer's disease A4 amyloid is encoded by 16 exons.”  Lemaire H.-G.et.al.   2783775
[4] “Genomic organization of the human amyloid beta-protein precursor gene.”  Yoshikai S.et.al.   2110105
[5] “”  Yoshikai S.et.al.   1908403
[6] “Identification and differential expression of a novel alternative splice isoform of the beta A4 amyloid precursor protein (APP) mRNA in leukocytes and brain microglial cells.”  Koenig G.et.al.   1587857
[7] “A novel method for making nested deletions and its application for sequencing of a 300 kb region of human APP locus.”  Hattori M.et.al.   9108164
[8] “Identification of a novel alternative splicing isoform of human amyloid precursor protein gene, APP639.”  Tang K.et.al.   12859342
[9] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[10] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[11] “A cDNA specifying the human amyloid beta precursor protein (ABPP) encodes a 95-kDa polypeptide.”  Schon E.A.et.al.   3140222
[12] “Characterization of the 5'-end region and the first two exons of the beta-protein precursor gene.”  La Fauci G.et.al.   2538123
[13] “Purification of protease nexin II from human fibroblasts.”  van Nostrand W.E.et.al.   3597385
[14] “Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.”  Gevaert K.et.al.   12665801
[15] “Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease.”  Tanzi R.E.et.al.   2893290
[16] “Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity.”  Kitaguchi N.et.al.   2893291
[17] “Molecular cloning of amyloid cDNA derived from mRNA of the Alzheimer disease brain: coding and noncoding regions of the fetal precursor mRNA are expressed in the cortex.”  Zain S.B.et.al.   2893379
[18] “Regulation of amyloid protein precursor (APP) binding to collagen and mapping of the binding sites on APP and collagen type I.”  Beher D.et.al.   8576160
[19] “A system for studying the effect(s) of familial Alzheimer disease mutations on the processing of the beta-amyloid peptide precursor.”  Denman R.B.et.al.   8476439
[20] “Alzheimer's disease amyloid peptide is encoded by two exons and shows similarity to soybean trypsin inhibitor.”  Johnstone E.M.et.al.   2675837
[21] “Novel amyloid precursor protein gene missense mutation (D678N) in probable familial Alzheimer's disease.”  Wakutani Y.et.al.   15201367
[22] “Beta-amyloid-(1-42) is a major component of cerebrovascular amyloid deposits: implications for the pathology of Alzheimer disease.”  Roher A.E.et.al.   8248178
[23] “Isolation and quantification of soluble Alzheimer's beta-peptide from biological fluids.”  Seubert P.et.al.   1406936
[24] “The amino acid sequence of neuritic plaque amyloid from a familial Alzheimer's disease patient.”  Wisniewski T.et.al.   8109908
[25] “Characterization of beta-amyloid peptide from human cerebrospinal fluid.”  Vigo-Pelfrey C.et.al.   8229004
[26] “Amyloid angiopathy of Alzheimer's disease: amino acid composition and partial sequence of a 4,200-dalton peptide isolated from cortical microvessels.”  Pardridge W.M.et.al.   3312495
[27] “Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease.”  Goldgaber D.et.al.   3810169
[28] “Amyloid beta protein gene: cDNA, mRNA distribution, and genetic linkage near the Alzheimer locus.”  Tanzi R.E.et.al.   2949367
[29] “BACE2, as a novel APP theta-secretase, is not responsible for the pathogenesis of Alzheimer's disease in Down syndrome.”  Sun X.et.al.   16816112
[30] “A novel mRNA of the A4 amyloid precursor gene coding for a possibly secreted protein.”  de Sauvage F.et.al.   2569763
[31] “Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides.”  Robakis N.K.et.al.   3035574
[32] “The chondroitin sulfate attachment site of appican is formed by splicing out exon 15 of the amyloid precursor gene.”  Pangalos M.N.et.al.   7737970
[33] “Alzheimer's disease amyloid beta peptide 25-35 inhibits lipid peroxidation as a result of its membrane interactions.”  Walter M.F.et.al.   9168929
[34] “Alzheimer's amyloid-beta as a preventive antioxidant for brain lipoproteins.”  Kontush A.et.al.   11775062
[35] “The secreted form of the Alzheimer's amyloid precursor protein with the Kunitz domain is protease nexin-II.”  Oltersdorf T.et.al.   2506449
[36] “Protease-specificity of Kunitz inhibitor domain of Alzheimer's disease amyloid protein precursor.”  Kido H.et.al.   1969731
[37] “A novel zinc(II) binding site modulates the function of the beta A4 amyloid protein precursor of Alzheimer's disease.”  Bush A.I.et.al.   8344894
[38] “Alzheimer amyloid protein precursor complexes with brain GTP-binding protein G(o).”  Nishimoto I.et.al.   8446172
[39] “The beta A4 amyloid precursor protein binding to copper.”  Hesse L.et.al.   7913895
[40] “A heparin-binding domain in the amyloid protein precursor of Alzheimer's disease is involved in the regulation of neurite outgrowth.”  Small D.H.et.al.   8158260
[41] “Familial Alzheimer's disease-linked mutations at Val717 of amyloid precursor protein are specific for the increased secretion of A beta 42(43).”  Maruyama K.et.al.   8886002
[42] “APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein.”  Chow N.et.al.   8626687
[43] “The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein.”  Borg J.-P.et.al.   8887653
[44] “Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein.”  Guenette S.Y.et.al.   8855266
[45] “Expression and analysis of heparin-binding regions of the amyloid precursor protein of Alzheimer's disease.”  Mok S.S.et.al.   9357988
[46] “An intracellular protein that binds amyloid-beta peptide and mediates neurotoxicity in Alzheimer's disease.”  Yan S.D.et.al.   9338779
[47] “PAT1, a microtubule-interacting protein, recognizes the basolateral sorting signal of amyloid precursor protein.”  Zheng P.et.al.   9843960
[48] “Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the A beta peptide of Alzheimer's disease.”  Liu S.T.et.al.   10413512
[49] “Methionine residue 35 is important in amyloid beta-peptide-associated free radical oxidative stress.”  Varadarajan S.et.al.   10535332
[50] “Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein.”  Tomita S.et.al.   9890987
[51] “Mutagenesis identifies new signals for beta-amyloid precursor protein endocytosis, turnover, and the generation of secreted fragments, including Abeta42.”  Perez R.G.et.al.   10383380
[52] “Cysteine 144 is a key residue in the copper reduction by the beta-amyloid precursor protein.”  Ruiz F.H.et.al.   10461923
[53] “Lipidation of apolipoprotein E influences its isoform-specific interaction with Alzheimer's amyloid beta peptides.”  Tokuda T.et.al.   10816430
[54] “Beta-amyloid(1-42) binds to alpha7 nicotinic acetylcholine receptor with high affinity. Implications for Alzheimer's disease pathology.”  Wang H.-Y.et.al.   10681545
[55] “Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor.”  Passer B.et.al.   12214090
[56] “Beta amyloid peptide (Abeta42) is internalized via the G-protein-coupled receptor FPRL1 and forms fibrillar aggregates in macrophages.”  Yazawa H.et.al.   11689470
[57] “Beta-amyloid peptide-induced apoptosis regulated by a novel protein containing a G protein activation module.”  Kajkowski E.M.et.al.   11278849
[58] “Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered structure containing superoxide dismutase-like subunits.”  Curtain C.C.et.al.   11274207
[59] “Homodimerization of amyloid precursor protein and its implication in the amyloidogenic pathway of Alzheimer's disease.”  Scheuermann S.et.al.   11438549
[60] “The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner.”  Kimberly W.T.et.al.   11544248
[61] “Fibulin-1 binds the amino-terminal head of beta-amyloid precursor protein and modulates its physiological function.”  Ohsawa I.et.al.   11238726
[62] “Direct interaction of soluble human recombinant tau protein with Abeta 1-42 results in tau aggregation and hyperphosphorylation by tau protein kinase II.”  Rank K.B.et.al.   11943163
[63] “Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein (APP).”  Scheinfeld M.H.et.al.   11724784
[64] “Contrasting species-dependent modulation of copper-mediated neurotoxicity by the Alzheimer's disease amyloid precursor protein.”  White A.R.et.al.   11784781
[65] “The galvanization of beta-amyloid in Alzheimer's disease.”  Bush A.I.et.al.   12032279
[66] “Amyloid-beta protein precursor (AbetaPP) intracellular domain-associated protein-1 proteins bind to AbetaPP and modulate its processing in an isoform-specific manner.”  Ghersi E.et.al.   15347684
[67] “Cell cycle-dependent regulation of the phosphorylation and metabolism of the Alzheimer amyloid precursor protein.”  Suzuki T.et.al.   8131745
[68] “Ectodomain phosphorylation of beta-amyloid precursor protein at two distinct cellular locations.”  Walter J.et.al.   8999878
[69] “Copper-binding amyloid precursor protein undergoes a site-specific fragmentation in the reduction of hydrogen peroxide.”  Multhaup G.et.al.   9585534
[70] “Involvement of caspases in proteolytic cleavage of Alzheimer's amyloid-beta precursor protein and amyloidogenic A beta peptide formation.”  Gervais F.G.et.al.   10319819
[71] “Role of phosphorylation of Alzheimer's amyloid precursor protein during neuronal differentiation.”  Ando K.et.al.   10341243
[72] “Phosphorylation of the beta-amyloid precursor protein at the cell surface by ectocasein kinases 1 and 2.”  Walter J.et.al.   10806211
[73] “A second cytotoxic proteolytic peptide derived from amyloid beta-protein precursor.”  Lu D.C.et.al.   10742146
[74] “Phosphorylation-dependent regulation of the interaction of amyloid precursor protein with Fe65 affects the production of beta-amyloid.”  Ando K.et.al.   11517218
[75] “Phosphorylation of thr(668) in the cytoplasmic domain of the Alzheimer's disease amyloid precursor protein by stress-activated protein kinase 1b (Jun N-terminal kinase-3).”  Standen C.L.et.al.   11146006
[76] “A novel epsilon-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing.”  Weidemann A.et.al.   11851430
[77] “Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc.”  Tarr P.E.et.al.   11877420
[78] “Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.”  Liu T.et.al.   16335952
[79] “Identification, transmembrane orientation and biogenesis of the amyloid A4 precursor of Alzheimer's disease.”  Dyrks T.et.al.   2900137
[80] “A cell biological perspective on Alzheimer's disease.”  Annaert W.et.al.   12142279
[81] “Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.”  Rikova K.et.al.   18083107
[82] “Regulation of FE65 nuclear translocation and function by amyloid beta-protein precursor in osmotically stressed cells.”  Nakaya T.et.al.   18468999
[83] “BRI3 inhibits amyloid precursor protein processing in a mechanistically distinct manner from its homologue dementia gene BRI2.”  Matsuda S.et.al.   19366692
[84] “An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells.”  Heibeck T.H.et.al.   19534553
[85] “APP binds DR6 to trigger axon pruning and neuron death via distinct caspases.”  Nikolaev A.et.al.   19225519
[86] “RAGE-mediated signaling contributes to intraneuronal transport of amyloid-{beta} and neuronal dysfunction.”  Takuma K.et.al.   19901339
[87] “X-ray crystal structure of the protease inhibitor domain of Alzheimer's amyloid beta-protein precursor.”  Hynes T.R.et.al.   2125487
[88] “Sequential NMR resonance assignment and structure determination of the Kunitz-type inhibitor domain of the Alzheimer's beta-amyloid precursor protein.”  Heald S.L.et.al.   1718421
[89] “Solution structure of residues 1-28 of the amyloid beta-peptide.”  Talafous J.et.al.   7516706
[90] “Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease.”  Sticht H.et.al.   7588758
[91] “Three-dimensional structures of the amyloid beta peptide (25-35) in membrane-mimicking environment.”  Kohno T.et.al.   8973180
[92] “Crystal structures of bovine chymotrypsin and trypsin complexed to the inhibitor domain of Alzheimer's amyloid beta-protein precursor (APPI) and basic pancreatic trypsin inhibitor (BPTI): engineering of inhibitors with altered specificities.”  Scheidig A.J.et.al.   9300481
[93] “Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?”  Coles M.et.al.   9693002
[94] “Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein.”  Rossjohn J.et.al.   10201399
[95] “Substitutions at codon 22 of Alzheimer's Abeta peptide induce diverse conformational changes and apoptotic effects in human cerebral endothelial cells.”  Miravalle L.et.al.   10821838
[96] “The Alzheimer's peptide a beta adopts a collapsed coil structure in water.”  Zhang S.et.al.   10940221
[97] “Solution structures in aqueous SDS micelles of two amyloid beta peptides of Abeta(1-28) mutated at the alpha-secretase cleavage site.”  Poulsen S.-A.et.al.   10940222
[98] “The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain.”  Wang Y.et.al.   15304215
[99] “Framing beta-amyloid.”  Hardy J.et.al.   1363811
[100] “Mutation of the Alzheimer's disease amyloid gene in hereditary cerebral hemorrhage, Dutch type.”  Levy E.et.al.   2111584
[101] “Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease.”  Goate A.et.al.   1671712
[102] “The 717Val-->Ile substitution in amyloid precursor protein is associated with familial Alzheimer's disease regardless of ethnic groups.”  Yoshioka K.et.al.   1908231
[103] “Mis-sense mutation Val->Ile in exon 17 of amyloid precursor protein gene in Japanese familial Alzheimer's disease.”  Naruse S.et.al.   1678058
[104] “Early-onset Alzheimer's disease caused by mutations at codon 717 of the beta-amyloid precursor protein gene.”  Chartier-Harlin M.-C.et.al.   1944558
[105] “A mutation in the amyloid precursor protein associated with hereditary Alzheimer's disease.”  Murrell J.R.et.al.   1925564
[106] “Linkage and mutational analysis of familial Alzheimer disease kindreds for the APP gene region.”  Kamino K.et.al.   1415269
[107] “Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the beta-amyloid precursor protein gene.”  Hendriks L.et.al.   1303239
[108] “A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N-terminus of beta-amyloid.”  Mullan M.et.al.   1302033
[109] “Mutation in codon 713 of the beta amyloid precursor protein gene presenting with schizophrenia.”  Jones C.T.et.al.   1307241
[110] “More missense in amyloid gene.”  Carter D.A.et.al.   1303275
[111] “Characterization of amyloid fibril beta-peptide in familial Alzheimer's disease with APP717 mutations.”  Liepnieks J.J.et.al.   8267572
[112] “Novel amyloid precursor protein gene mutation (codon 665Asp) in a patient with late-onset Alzheimer's disease.”  Peacock M.L.et.al.   8154870
[113] “Clinical characteristics in a kindred with early-onset Alzheimer's disease and their linkage to a G-->T change at position 2149 of the amyloid precursor protein gene.”  Farlow M.et.al.   8290042
[114] “A mutation in codon 717 of the amyloid precursor protein gene in an Australian family with Alzheimer's disease.”  Brooks W.S.et.al.   8577393
[115] “A new pathogenic mutation in the APP gene (I716V) increases the relative proportion of A beta 42(43).”  Eckman C.B.et.al.   9328472
[116] “Presenile Alzheimer dementia characterized by amyloid angiopathy and large amyloid core type senile plaques in the APP 692Ala-->Gly mutation.”  Cras P.et.al.   9754958
[117] “Unusual phenotypic alteration of beta amyloid precursor protein (betaAPP) maturation by a new Val-715 --> Met betaAPP-770 mutation responsible for probable early-onset Alzheimer's disease.”  Ancolio K.et.al.   10097173
[118] “High prevalence of pathogenic mutations in patients with early-onset dementia detected by sequence analyses of four different genes.”  Finckh U.et.al.   10631141
[119] “Novel Leu723Pro amyloid precursor protein mutation increases amyloid beta42(43) peptide levels and induces apoptosis.”  Kwok J.B.J.et.al.   10665499
[120] “Early-onset Alzheimer disease caused by a new mutation (V717L) in the amyloid precursor protein gene.”  Murrell J.R.et.al.   10867787
[121] “Nonfibrillar diffuse amyloid deposition due to a gamma(42)-secretase site mutation points to an essential role for N-truncated A beta(42) in Alzheimer's disease.”  Kumar-Singh S.et.al.   11063718
[122] “Novel amyloid precursor protein mutation in an Iowa family with dementia and severe cerebral amyloid angiopathy.”  Grabowski T.J.et.al.   11409420
[123] “In vitro studies of amyloid beta-protein fibril assembly and toxicity provide clues to the aetiology of Flemish variant (Ala692-->Gly) Alzheimer's disease.”  Walsh D.M.et.al.   11311152
[124] “The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Abeta protofibril formation.”  Nilsberth C.et.al.   11528419
[125] “An Iranian family with Alzheimer's disease caused by a novel APP mutation (Thr714Ala).”  Pasalar P.et.al.   12034808
[126] “Hemorrhagic stroke associated with the Iowa amyloid precursor protein mutation.”  Greenberg S.M.et.al.   12654973
[127] “A family with Alzheimer disease and strokes associated with A713T mutation of the APP gene.”  Rossi G.et.al.   15365148
[128] “A novel AbetaPP mutation exclusively associated with cerebral amyloid angiopathy.”  Obici L.et.al.   16178030
[129] “An African American family with early-onset Alzheimer disease and an APP (T714I) mutation.”  Edwards-Lee T.et.al.   15668448
Structure:
1AAP   1AMB   1AMC   1AML   1BA4   1BA6   1BJB   1BJC   1BRC   1CA0   [...more]

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Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MLPGLALLLL AAWTARALEV PTDGNAGLLA EPQIAMFCGR LNMHMNVQNG KWDSDPSGTK 
61:	TCIDTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHPH FVIPYRCLVG 
121:	EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR 
181:	GVEFVCCPLA EESDNVDSAD AEEDDSDVWW GGADTDYADG SEDKVVEVAE EEEVAEVEEE 
241:	EADDDEDDED GDEVEEEAEE PYEEATERTT SIATTTTTTT ESVEEVVREV CSEQAETGPC 
301:	RAMISRWYFD VTEGKCAPFF YGGCGGNRNN FDTEEYCMAV CGSAMSQSLL KTTQEPLARD 
361:	PVKLPTTAAS TPDAVDKYLE TPGDENEHAH FQKAKERLEA KHRERMSQVM REWEEAERQA 
421:	KNLPKADKKA VIQHFQEKVE SLEQEAANER QQLVETHMAR VEAMLNDRRR LALENYITAL 
481:	QAVPPRPRHV FNMLKKYVRA EQKDRQHTLK HFEHVRMVDP KKAAQIRSQV MTHLRVIYER 
541:	MNQSLSLLYN VPAVAEEIQD EVDELLQKEQ NYSDDVLANM ISEPRISYGN DALMPSLTET 
601:	KTTVELLPVN GEFSLDDLQP WHSFGADSVP ANTENEVEPV DARPAADRGL TTRPGSGLTN 
661:	IKTEEISEVK MDAEFRHDSG YEVHHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL 
721:	VMLKKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN