PPBI_HUMAN
ID PPBI_HUMAN Reviewed; 528 AA.
AC P09923; B2R7Y4; Q53S80; Q9UBV5; Q9UCL2;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Intestinal-type alkaline phosphatase;
DE Short=IAP;
DE Short=Intestinal alkaline phosphatase;
DE EC=3.1.3.1;
DE Flags: Precursor;
GN Name=ALPI;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3468508; DOI=10.1073/pnas.84.3.695;
RA Berger J., Garattini E., Hua J.-C., Udenfriend S.;
RT "Cloning and sequencing of human intestinal alkaline phosphatase cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:695-698(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3469665; DOI=10.1073/pnas.84.5.1234;
RA Henthorn P.S., Raducha M., Edwards Y.H., Weiss M.J., Slaughter C.,
RA Lafferty M.A., Harris H.;
RT "Nucleotide and amino acid sequences of human intestinal alkaline
RT phosphatase: close homology to placental alkaline phosphatase.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:1234-1238(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2841341; DOI=10.1016/s0021-9258(18)37886-4;
RA Henthorn P.S., Raducha M., Kadesch T., Weiss M.J., Harris H.;
RT "Sequence and characterization of the human intestinal alkaline phosphatase
RT gene.";
RL J. Biol. Chem. 263:12011-12019(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
RX PubMed=3697102; DOI=10.1093/nar/15.24.10599;
RA Millan J.L.;
RT "Promoter structure of the human intestinal alkaline phosphatase gene.";
RL Nucleic Acids Res. 15:10599-10599(1987).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
RX PubMed=3443302; DOI=10.1016/0378-1119(87)90235-6;
RA Knoll B.J., Rothblum K.N., Longley M.;
RT "Two gene duplication events in the evolution of the human heat-stable
RT alkaline phosphatases.";
RL Gene 60:267-276(1987).
RN [10]
RP PROTEIN SEQUENCE OF 20-58.
RX PubMed=3458202; DOI=10.1073/pnas.83.8.2368;
RA Hua J.-C., Berger J., Pan Y.C.E., Hulmes J.D., Udenfriend S.;
RT "Partial sequencing of human adult, human fetal, and bovine intestinal
RT alkaline phosphatases: comparison with the human placental and liver
RT isozymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:2368-2372(1986).
RN [11]
RP PROTEIN SEQUENCE OF 20-49.
RX PubMed=1458595;
RA Nishihara Y., Hayashi Y., Adachi T., Koyama I., Stigbrand T., Hirano K.;
RT "Chemical nature of intestinal-type alkaline phosphatase in human kidney.";
RL Clin. Chem. 38:2539-2542(1992).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Alkaline phosphatase that can hydrolyze various phosphate
CC compounds. {ECO:0000250|UniProtKB:P15693}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a phosphate monoester + H2O = an alcohol + phosphate;
CC Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1;
CC Evidence={ECO:0000250|UniProtKB:P15693, ECO:0000255|PROSITE-
CC ProRule:PRU10042};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P15693};
CC Note=Binds 1 Mg(2+) ion. {ECO:0000250|UniProtKB:P15693};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P15693};
CC Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:P15693};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P05186};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P15693}.
CC -!- INTERACTION:
CC P09923; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1052631, EBI-10171774;
CC P09923; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-1052631, EBI-10172052;
CC P09923; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-1052631, EBI-945833;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15693};
CC Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P15693}.
CC -!- MISCELLANEOUS: In most mammals there are four different isozymes:
CC placental (ALPP), germ cell (ALPG), intestinal (ALPI) and tissue non-
CC specific (liver/bone/kidney) (ALPL/TNAP).
CC -!- SIMILARITY: Belongs to the alkaline phosphatase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Alkaline phosphatase entry;
CC URL="https://en.wikipedia.org/wiki/Alkaline_phosphatase";
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DR EMBL; M15694; AAA51703.1; -; mRNA.
DR EMBL; M31008; AAA51704.1; -; mRNA.
DR EMBL; J03930; AAA98617.1; -; Genomic_DNA.
DR EMBL; AK313163; BAG35981.1; -; mRNA.
DR EMBL; AC068134; AAY24089.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70997.1; -; Genomic_DNA.
DR EMBL; BC132678; AAI32679.1; -; mRNA.
DR EMBL; Y00512; CAA68564.1; -; Genomic_DNA.
DR EMBL; M19161; AAA51705.1; -; Genomic_DNA.
DR CCDS; CCDS2492.1; -.
DR PIR; A31073; PAHUI.
DR RefSeq; NP_001622.2; NM_001631.4.
DR AlphaFoldDB; P09923; -.
DR SMR; P09923; -.
DR BioGRID; 106749; 87.
DR IntAct; P09923; 22.
DR MINT; P09923; -.
DR STRING; 9606.ENSP00000295463; -.
DR BindingDB; P09923; -.
DR ChEMBL; CHEMBL5573; -.
DR DrugBank; DB16349; Vicagrel.
DR DEPOD; ALPI; -.
DR GlyConnect; 11; 9 N-Linked glycans.
DR GlyGen; P09923; 4 sites, 17 N-linked glycans (1 site).
DR iPTMnet; P09923; -.
DR PhosphoSitePlus; P09923; -.
DR BioMuta; ALPI; -.
DR DMDM; 130744; -.
DR EPD; P09923; -.
DR jPOST; P09923; -.
DR MassIVE; P09923; -.
DR MaxQB; P09923; -.
DR PaxDb; P09923; -.
DR PeptideAtlas; P09923; -.
DR PRIDE; P09923; -.
DR ProteomicsDB; 52281; -.
DR Antibodypedia; 20217; 769 antibodies from 34 providers.
DR DNASU; 248; -.
DR Ensembl; ENST00000295463.4; ENSP00000295463.3; ENSG00000163295.5.
DR GeneID; 248; -.
DR KEGG; hsa:248; -.
DR MANE-Select; ENST00000295463.4; ENSP00000295463.3; NM_001631.5; NP_001622.2.
DR UCSC; uc002vst.4; human.
DR CTD; 248; -.
DR DisGeNET; 248; -.
DR GeneCards; ALPI; -.
DR HGNC; HGNC:437; ALPI.
DR HPA; ENSG00000163295; Tissue enriched (intestine).
DR MIM; 171740; gene.
DR neXtProt; NX_P09923; -.
DR OpenTargets; ENSG00000163295; -.
DR PharmGKB; PA24728; -.
DR VEuPathDB; HostDB:ENSG00000163295; -.
DR eggNOG; KOG4126; Eukaryota.
DR GeneTree; ENSGT00950000183063; -.
DR HOGENOM; CLU_008539_4_0_1; -.
DR InParanoid; P09923; -.
DR OMA; CANMQVA; -.
DR OrthoDB; 454880at2759; -.
DR PhylomeDB; P09923; -.
DR TreeFam; TF323513; -.
DR PathwayCommons; P09923; -.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-HSA-8935690; Digestion.
DR SABIO-RK; P09923; -.
DR SignaLink; P09923; -.
DR BioGRID-ORCS; 248; 12 hits in 1070 CRISPR screens.
DR ChiTaRS; ALPI; human.
DR GeneWiki; ALPI; -.
DR GenomeRNAi; 248; -.
DR Pharos; P09923; Tchem.
DR PRO; PR:P09923; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P09923; protein.
DR Bgee; ENSG00000163295; Expressed in jejunal mucosa and 27 other tissues.
DR ExpressionAtlas; P09923; baseline and differential.
DR Genevisible; P09923; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0004035; F:alkaline phosphatase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0002020; F:protease binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR CDD; cd16012; ALP; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR001952; Alkaline_phosphatase.
DR InterPro; IPR018299; Alkaline_phosphatase_AS.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR PANTHER; PTHR11596; PTHR11596; 1.
DR Pfam; PF00245; Alk_phosphatase; 1.
DR PRINTS; PR00113; ALKPHPHTASE.
DR SMART; SM00098; alkPPc; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Magnesium; Membrane;
KW Metal-binding; Reference proteome; Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1458595,
FT ECO:0000269|PubMed:3458202"
FT CHAIN 20..503
FT /note="Intestinal-type alkaline phosphatase"
FT /id="PRO_0000024037"
FT PROPEP 504..528
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000024038"
FT ACT_SITE 111
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10042"
FT BINDING 61
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P15693"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15693"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15693"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P15693"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 304
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P05186"
FT BINDING 330
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P15693"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15693"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15693"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15693"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15693"
FT BINDING 451
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15693"
FT LIPID 503
FT /note="GPI-anchor amidated aspartate"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 140..202
FT /evidence="ECO:0000250|UniProtKB:P15693"
FT DISULFID 486..493
FT /evidence="ECO:0000250|UniProtKB:P15693"
FT VARIANT 144
FT /note="R -> H (in dbSNP:rs7559279)"
FT /id="VAR_050524"
FT VARIANT 298
FT /note="H -> L (in dbSNP:rs1047223)"
FT /id="VAR_011816"
FT CONFLICT 347
FT /note="L -> V (in Ref. 2; AAA51703)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="I -> T (in Ref. 1; AAA51704)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="P -> L (in Ref. 2; AAA51703)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 528 AA; 56812 MW; 465306BEDF9F0B79 CRC64;
MQGPWVLLLL GLRLQLSLGV IPAEEENPAF WNRQAAEALD AAKKLQPIQK VAKNLILFLG
DGLGVPTVTA TRILKGQKNG KLGPETPLAM DRFPYLALSK TYNVDRQVPD SAATATAYLC
GVKANFQTIG LSAAARFNQC NTTRGNEVIS VMNRAKQAGK SVGVVTTTRV QHASPAGTYA
HTVNRNWYSD ADMPASARQE GCQDIATQLI SNMDIDVILG GGRKYMFPMG TPDPEYPADA
SQNGIRLDGK NLVQEWLAKH QGAWYVWNRT ELMQASLDQS VTHLMGLFEP GDTKYEIHRD
PTLDPSLMEM TEAALRLLSR NPRGFYLFVE GGRIDHGHHE GVAYQALTEA VMFDDAIERA
GQLTSEEDTL TLVTADHSHV FSFGGYTLRG SSIFGLAPSK AQDSKAYTSI LYGNGPGYVF
NSGVRPDVNE SESGSPDYQQ QAAVPLSSET HGGEDVAVFA RGPQAHLVHG VQEQSFVAHV
MAFAACLEPY TACDLAPPAC TTDAAHPVAA SLPLLAGTLL LLGASAAP
