DPP2_HUMAN
ID DPP2_HUMAN Reviewed; 492 AA.
AC Q9UHL4; A8K7U7; Q5VSF1; Q969X4;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Dipeptidyl peptidase 2;
DE EC=3.4.14.2;
DE AltName: Full=Dipeptidyl aminopeptidase II;
DE AltName: Full=Dipeptidyl peptidase 7;
DE AltName: Full=Dipeptidyl peptidase II;
DE Short=DPP II;
DE AltName: Full=Quiescent cell proline dipeptidase;
DE Flags: Precursor;
GN Name=DPP7; Synonyms=DPP2, QPP;
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], PARTIAL PROTEIN SEQUENCE, AND VARIANT GLY-89.
RX PubMed=10567372; DOI=10.1074/jbc.274.48.34053;
RA Underwood R., Chiravuri M., Lee H., Schmitz T., Kabcenell A.K., Yardley Y.,
RA Huber B.T.;
RT "Sequence, purification, and cloning of an intracellular serine protease,
RT quiescent cell proline dipeptidase.";
RL J. Biol. Chem. 274:34053-34058(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Synovial cell;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-89.
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 [5]
RP CHARACTERIZATION.
RX PubMed=11067927; DOI=10.4049/jimmunol.165.10.5695;
RA Chiravuri M., Agarraberes F., Mathieu S.L., Lee H., Huber B.T.;
RT "Vesicular localization and characterization of a novel post-proline-
RT cleaving aminodipeptidase, quiescent cell proline dipeptidase.";
RL J. Immunol. 165:5695-5702(2000).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50 AND ASN-315.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 28-492, PARTIAL PROTEIN SEQUENCE,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION,
RP TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15487984; DOI=10.1042/bj20041156;
RA Maes M.B., Lambeir A.M., Gilany K., Senten K., Van der Veken P.,
RA Leiting B., Augustyns K., Scharpe S., De Meester I.;
RT "Kinetic investigation of human dipeptidyl peptidase II (DPPII)-mediated
RT hydrolysis of dipeptide derivatives and its identification as quiescent
RT cell proline dipeptidase (QPP)/dipeptidyl peptidase 7 (DPP7).";
RL Biochem. J. 386:315-324(2005).
CC -!- FUNCTION: Plays an important role in the degradation of some
CC oligopeptides. {ECO:0000269|PubMed:15487984}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially
CC when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially
CC tripeptides.; EC=3.4.14.2; Evidence={ECO:0000269|PubMed:15487984};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. Has low activity at pH 7 and is inactive at pH 8.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15487984}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:15487984}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:15487984}. Secreted
CC {ECO:0000269|PubMed:15487984}.
CC -!- TISSUE SPECIFICITY: Detected in seminal plasma (at protein level).
CC {ECO:0000269|PubMed:15487984}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15487984,
CC ECO:0000269|PubMed:19159218}.
CC -!- SIMILARITY: Belongs to the peptidase S28 family. {ECO:0000305}.
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DR EMBL; AF154502; AAF12747.1; -; mRNA.
DR EMBL; AK292112; BAF84801.1; -; mRNA.
DR EMBL; AL929554; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011907; AAH11907.1; -; mRNA.
DR EMBL; BC016961; AAH16961.1; -; mRNA.
DR CCDS; CCDS7030.1; -.
DR PIR; S77568; S77568.
DR RefSeq; NP_037511.2; NM_013379.2.
DR PDB; 3JYH; X-ray; 2.19 A; A/B/C/D=28-492.
DR PDB; 3N0T; X-ray; 2.45 A; A/B/C/D=28-492.
DR PDB; 4EBB; X-ray; 2.00 A; A/B=27-492.
DR PDBsum; 3JYH; -.
DR PDBsum; 3N0T; -.
DR PDBsum; 4EBB; -.
DR AlphaFoldDB; Q9UHL4; -.
DR SMR; Q9UHL4; -.
DR BioGRID; 118989; 31.
DR IntAct; Q9UHL4; 29.
DR MINT; Q9UHL4; -.
DR STRING; 9606.ENSP00000360635; -.
DR BindingDB; Q9UHL4; -.
DR ChEMBL; CHEMBL3976; -.
DR DrugCentral; Q9UHL4; -.
DR GuidetoPHARMACOLOGY; 1605; -.
DR ESTHER; human-DPP7; Prolylcarboxypeptidase.
DR MEROPS; S28.002; -.
DR GlyConnect; 1176; 6 N-Linked glycans (2 sites).
DR GlyGen; Q9UHL4; 6 sites, 6 N-linked glycans (2 sites).
DR iPTMnet; Q9UHL4; -.
DR PhosphoSitePlus; Q9UHL4; -.
DR BioMuta; DPP7; -.
DR DMDM; 212276510; -.
DR CPTAC; CPTAC-1304; -.
DR EPD; Q9UHL4; -.
DR jPOST; Q9UHL4; -.
DR MassIVE; Q9UHL4; -.
DR MaxQB; Q9UHL4; -.
DR PaxDb; Q9UHL4; -.
DR PeptideAtlas; Q9UHL4; -.
DR PRIDE; Q9UHL4; -.
DR ProteomicsDB; 84375; -.
DR Antibodypedia; 18905; 297 antibodies from 33 providers.
DR DNASU; 29952; -.
DR Ensembl; ENST00000371579.7; ENSP00000360635.2; ENSG00000176978.14.
DR GeneID; 29952; -.
DR KEGG; hsa:29952; -.
DR MANE-Select; ENST00000371579.7; ENSP00000360635.2; NM_013379.3; NP_037511.2.
DR UCSC; uc004clh.4; human.
DR CTD; 29952; -.
DR DisGeNET; 29952; -.
DR GeneCards; DPP7; -.
DR HGNC; HGNC:14892; DPP7.
DR HPA; ENSG00000176978; Low tissue specificity.
DR MIM; 610537; gene.
DR neXtProt; NX_Q9UHL4; -.
DR OpenTargets; ENSG00000176978; -.
DR PharmGKB; PA27469; -.
DR VEuPathDB; HostDB:ENSG00000176978; -.
DR eggNOG; KOG2183; Eukaryota.
DR GeneTree; ENSGT00940000159838; -.
DR HOGENOM; CLU_020959_0_0_1; -.
DR InParanoid; Q9UHL4; -.
DR OMA; IKGGAHH; -.
DR OrthoDB; 555765at2759; -.
DR PhylomeDB; Q9UHL4; -.
DR TreeFam; TF314414; -.
DR BRENDA; 3.4.14.2; 2681.
DR PathwayCommons; Q9UHL4; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9UHL4; -.
DR BioGRID-ORCS; 29952; 15 hits in 1076 CRISPR screens.
DR ChiTaRS; DPP7; human.
DR EvolutionaryTrace; Q9UHL4; -.
DR GeneWiki; DPP7; -.
DR GenomeRNAi; 29952; -.
DR Pharos; Q9UHL4; Tchem.
DR PRO; PR:Q9UHL4; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9UHL4; protein.
DR Bgee; ENSG00000176978; Expressed in adenohypophysis and 168 other tissues.
DR ExpressionAtlas; Q9UHL4; baseline and differential.
DR Genevisible; Q9UHL4; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0031982; C:vesicle; IDA:CACAO.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc.
DR GO; GO:1905146; P:lysosomal protein catabolic process; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.980; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR008758; Peptidase_S28.
DR InterPro; IPR042269; Ser_carbopepase_S28_SKS.
DR Pfam; PF05577; Peptidase_S28; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cleavage on pair of basic residues;
KW Cytoplasmic vesicle; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Lysosome; Protease; Reference proteome; Secreted; Serine protease; Signal;
KW Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..25
FT /evidence="ECO:0000255"
FT /id="PRO_0000027314"
FT CHAIN 26..492
FT /note="Dipeptidyl peptidase 2"
FT /id="PRO_0000027315"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 418
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT ACT_SITE 443
FT /note="Charge relay system"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 89
FT /note="A -> G (in dbSNP:rs10747049)"
FT /evidence="ECO:0000269|PubMed:10567372,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_047087"
FT CONFLICT 71
FT /note="I -> T (in Ref. 1; AAF12747)"
FT /evidence="ECO:0000305"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:4EBB"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:4EBB"
FT STRAND 52..60
FT /evidence="ECO:0007829|PDB:4EBB"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:4EBB"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:4EBB"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 131..148
FT /evidence="ECO:0007829|PDB:4EBB"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:4EBB"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:4EBB"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 200..210
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 214..233
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:4EBB"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 252..271
FT /evidence="ECO:0007829|PDB:4EBB"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 288..297
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 302..314
FT /evidence="ECO:0007829|PDB:4EBB"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:3JYH"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 342..351
FT /evidence="ECO:0007829|PDB:4EBB"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:4EBB"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 375..386
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 394..399
FT /evidence="ECO:0007829|PDB:4EBB"
FT STRAND 409..415
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:4EBB"
FT STRAND 430..438
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:4EBB"
FT HELIX 456..476
FT /evidence="ECO:0007829|PDB:4EBB"
SQ SEQUENCE 492 AA; 54341 MW; 6C3EDECA90FA7583 CRC64;
MGSAPWAPVL LLALGLRGLQ AGARRAPDPG FQERFFQQRL DHFNFERFGN KTFPQRFLVS
DRFWVRGEGP IFFYTGNEGD VWAFANNSAF VAELAAERGA LLVFAEHRYY GKSLPFGAQS
TQRGHTELLT VEQALADFAE LLRALRRDLG AQDAPAIAFG GSYGGMLSAY LRMKYPHLVA
GALAASAPVL AVAGLGDSNQ FFRDVTADFE GQSPKCTQGV REAFRQIKDL FLQGAYDTVR
WEFGTCQPLS DEKDLTQLFM FARNAFTVLA MMDYPYPTDF LGPLPANPVK VGCDRLLSEA
QRITGLRALA GLVYNASGSE HCYDIYRLYH SCADPTGCGT GPDARAWDYQ ACTEINLTFA
SNNVTDMFPD LPFTDELRQR YCLDTWGVWP RPDWLLTSFW GGDLRAASNI IFSNGNLDPW
AGGGIRRNLS ASVIAVTIQG GAHHLDLRAS HPEDPASVVE ARKLEATIIG EWVKAARREQ
QPALRGGPRL SL
