DNPEP_HUMAN
ID DNPEP_HUMAN Reviewed; 485 AA.
AC Q9ULA0; Q9BW44; Q9NUV5; Q9NV55;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Aspartyl aminopeptidase {ECO:0000305};
DE EC=3.4.11.21 {ECO:0000269|PubMed:9632644};
GN Name=DNPEP {ECO:0000312|HGNC:HGNC:2981}; Synonyms=ASPEP, DAP;
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], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9632644; DOI=10.1074/jbc.273.26.15961;
RA Wilk S., Wilk E., Magnusson R.P.;
RT "Purification, characterization, and cloning of a cytosolic aspartyl
RT aminopeptidase.";
RL J. Biol. Chem. 273:15961-15970(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-213, AND IDENTIFICATION BY
RP 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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 11-478 IN COMPLEX WITH SUBSTRATE
RP ANALOG, ZINC-BINDING SITES, SUBSTRATE-BINDING SITES, AND SUBUNIT.
RX PubMed=22720794; DOI=10.1186/1472-6807-12-14;
RA Chaikuad A., Pilka E.S., Riso A.D., Delft F.V., Kavanagh K.L.,
RA Venien-Bryan C., Oppermann U., Yue W.W.;
RT "Structure of human aspartyl aminopeptidase complexed with substrate
RT analogue: insight into catalytic mechanism, substrate specificity and M18
RT peptidase family.";
RL BMC Struct. Biol. 12:14-14(2012).
CC -!- FUNCTION: Aminopeptidase with specificity towards an acidic amino acid
CC at the N-terminus. Likely to play an important role in intracellular
CC protein and peptide metabolism. {ECO:0000269|PubMed:9632644}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal aspartate or glutamate from a
CC peptide, with a preference for aspartate.; EC=3.4.11.21;
CC Evidence={ECO:0000269|PubMed:9632644};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:9632644};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:9632644};
CC -!- ACTIVITY REGULATION: One of the zinc ions is readily exchangeable with
CC other divalent cations such as manganese, which strongly stimulates the
CC enzymatic activity. {ECO:0000250}.
CC -!- SUBUNIT: Tetrahedron-shaped homododecamer built from six homodimers.
CC {ECO:0000269|PubMed:22720794}.
CC -!- INTERACTION:
CC Q9ULA0; Q9ULA0: DNPEP; NbExp=4; IntAct=EBI-748356, EBI-748356;
CC Q9ULA0; Q8TBB1: LNX1; NbExp=7; IntAct=EBI-748356, EBI-739832;
CC Q9ULA0; Q00013: MPP1; NbExp=6; IntAct=EBI-748356, EBI-711788;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9632644}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULA0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULA0-2; Sequence=VSP_060753;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9632644}.
CC -!- SIMILARITY: Belongs to the peptidase M18 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD01211.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH00653.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91903.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF005050; AAD01211.2; ALT_INIT; mRNA.
DR EMBL; AK001777; BAA91903.1; ALT_FRAME; mRNA.
DR EMBL; AK001977; BAA92014.1; -; mRNA.
DR EMBL; AC053503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000653; AAH00653.2; ALT_INIT; mRNA.
DR CCDS; CCDS42823.1; -. [Q9ULA0-1]
DR RefSeq; NP_001306049.1; NM_001319120.1.
DR RefSeq; NP_036232.2; NM_012100.3. [Q9ULA0-1]
DR PDB; 4DYO; X-ray; 2.20 A; A=11-478.
DR PDBsum; 4DYO; -.
DR AlphaFoldDB; Q9ULA0; -.
DR SMR; Q9ULA0; -.
DR BioGRID; 117093; 102.
DR IntAct; Q9ULA0; 21.
DR MINT; Q9ULA0; -.
DR STRING; 9606.ENSP00000273075; -.
DR BindingDB; Q9ULA0; -.
DR ChEMBL; CHEMBL2761; -.
DR DrugBank; DB00142; Glutamic acid.
DR GuidetoPHARMACOLOGY; 1559; -.
DR MEROPS; M18.002; -.
DR iPTMnet; Q9ULA0; -.
DR PhosphoSitePlus; Q9ULA0; -.
DR BioMuta; DNPEP; -.
DR DMDM; 17367145; -.
DR EPD; Q9ULA0; -.
DR jPOST; Q9ULA0; -.
DR MassIVE; Q9ULA0; -.
DR MaxQB; Q9ULA0; -.
DR PaxDb; Q9ULA0; -.
DR PeptideAtlas; Q9ULA0; -.
DR PRIDE; Q9ULA0; -.
DR ProteomicsDB; 84965; -.
DR Antibodypedia; 34327; 207 antibodies from 28 providers.
DR DNASU; 23549; -.
DR Ensembl; ENST00000273075.9; ENSP00000273075.4; ENSG00000123992.20. [Q9ULA0-1]
DR GeneID; 23549; -.
DR KEGG; hsa:23549; -.
DR MANE-Select; ENST00000273075.9; ENSP00000273075.4; NM_012100.4; NP_036232.2.
DR UCSC; uc002vle.3; human. [Q9ULA0-1]
DR CTD; 23549; -.
DR DisGeNET; 23549; -.
DR GeneCards; DNPEP; -.
DR HGNC; HGNC:2981; DNPEP.
DR HPA; ENSG00000123992; Low tissue specificity.
DR MIM; 611367; gene.
DR neXtProt; NX_Q9ULA0; -.
DR OpenTargets; ENSG00000123992; -.
DR PharmGKB; PA27448; -.
DR VEuPathDB; HostDB:ENSG00000123992; -.
DR eggNOG; KOG2596; Eukaryota.
DR GeneTree; ENSGT00390000003164; -.
DR InParanoid; Q9ULA0; -.
DR OMA; GPILKVN; -.
DR PhylomeDB; Q9ULA0; -.
DR TreeFam; TF300487; -.
DR BRENDA; 3.4.11.21; 2681.
DR PathwayCommons; Q9ULA0; -.
DR SignaLink; Q9ULA0; -.
DR BioGRID-ORCS; 23549; 15 hits in 1084 CRISPR screens.
DR ChiTaRS; DNPEP; human.
DR GeneWiki; DNPEP; -.
DR GenomeRNAi; 23549; -.
DR Pharos; Q9ULA0; Tchem.
DR PRO; PR:Q9ULA0; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9ULA0; protein.
DR Bgee; ENSG00000123992; Expressed in left testis and 203 other tissues.
DR ExpressionAtlas; Q9ULA0; baseline and differential.
DR Genevisible; Q9ULA0; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0004177; F:aminopeptidase activity; TAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006518; P:peptide metabolic process; TAS:ProtInc.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.250.10; -; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; PTHR28570; 1.
DR Pfam; PF02127; Peptidase_M18; 1.
DR PRINTS; PR00932; AMINO1PTASE.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Aminopeptidase;
KW Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein;
KW Protease; Reference proteome; Zinc.
FT CHAIN 1..485
FT /note="Aspartyl aminopeptidase"
FT /id="PRO_0000173451"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22720794"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22720794"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22720794"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22720794"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22720794"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22720794"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22720794"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22720794"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22720794"
FT BINDING 384
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22720794"
FT BINDING 391
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22720794"
FT BINDING 450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:22720794"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..10
FT /note="Missing (in isoform 2)"
FT /id="VSP_060753"
FT CONFLICT 2
FT /note="S -> C (in Ref. 2; BAA91903)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="E -> V (in Ref. 2; BAA92014)"
FT /evidence="ECO:0000305"
FT HELIX 18..36
FT /evidence="ECO:0007829|PDB:4DYO"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:4DYO"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 109..120
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 123..133
FT /evidence="ECO:0007829|PDB:4DYO"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 144..153
FT /evidence="ECO:0007829|PDB:4DYO"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:4DYO"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:4DYO"
FT TURN 183..187
FT /evidence="ECO:0007829|PDB:4DYO"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:4DYO"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:4DYO"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:4DYO"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:4DYO"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:4DYO"
FT HELIX 273..289
FT /evidence="ECO:0007829|PDB:4DYO"
FT TURN 293..298
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 301..309
FT /evidence="ECO:0007829|PDB:4DYO"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:4DYO"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:4DYO"
FT HELIX 342..346
FT /evidence="ECO:0007829|PDB:4DYO"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:4DYO"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:4DYO"
FT TURN 387..390
FT /evidence="ECO:0007829|PDB:4DYO"
FT HELIX 395..408
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:4DYO"
FT HELIX 427..435
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:4DYO"
FT STRAND 451..458
FT /evidence="ECO:0007829|PDB:4DYO"
FT HELIX 459..478
FT /evidence="ECO:0007829|PDB:4DYO"
FT MOD_RES Q9ULA0-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 485 AA; 53410 MW; 522180921D0FBFA9 CRC64;
MSGHSPTRGA MQVAMNGKAR KEAVQTAAKE LLKFVNRSPS PFHAVAECRN RLLQAGFSEL
KETEKWNIKP ESKYFMTRNS STIIAFAVGG QYVPGNGFSL IGAHTDSPCL RVKRRSRRSQ
VGFQQVGVET YGGGIWSTWF DRDLTLAGRV IVKCPTSGRL EQQLVHVERP ILRIPHLAIH
LQRNINENFG PNTEMHLVPI LATAIQEELE KGTPEPGPLN AVDERHHSVL MSLLCAHLGL
SPKDIVEMEL CLADTQPAVL GGAYDEFIFA PRLDNLHSCF CALQALIDSC AGPGSLATEP
HVRMVTLYDN EEVGSESAQG AQSLLTELVL RRISASCQHP TAFEEAIPKS FMISADMAHA
VHPNYLDKHE ENHRPLFHKG PVIKVNSKQR YASNAVSEAL IREVANKVKV PLQDLMVRND
TPCGTTIGPI LASRLGLRVL DLGSPQLAMH SIREMACTTG VLQTLTLFKG FFELFPSLSH
NLLVD
