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   27-MAR-2024, entry version 194.
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; 36.
DR   IntAct; Q9UHL4; 31.
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   GlyCosmos; Q9UHL4; 6 sites, 6 glycans.
DR   GlyGen; Q9UHL4; 6 sites, 10 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; 9606-ENSP00000360635; -.
DR   PeptideAtlas; Q9UHL4; -.
DR   ProteomicsDB; 84375; -.
DR   Pumba; Q9UHL4; -.
DR   Antibodypedia; 18905; 316 antibodies from 33 providers.
DR   DNASU; 29952; -.
DR   Ensembl; ENST00000371579.7; ENSP00000360635.2; ENSG00000176978.15.
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   AGR; HGNC:14892; -.
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; ELYMPMS; -.
DR   OrthoDB; 5488375at2759; -.
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; 30 hits in 1156 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 170 other cell types or tissues.
DR   ExpressionAtlas; Q9UHL4; baseline and differential.
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:0070008; F:serine-type exopeptidase activity; IEA:InterPro.
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; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 1.20.120.980; Serine carboxypeptidase S28, SKS domain; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR008758; Peptidase_S28.
DR   InterPro; IPR042269; Ser_carbopepase_S28_SKS.
DR   PANTHER; PTHR11010:SF107; DIPEPTIDYL PEPTIDASE 2; 1.
DR   PANTHER; PTHR11010; PROTEASE S28 PRO-X CARBOXYPEPTIDASE-RELATED; 1.
DR   Pfam; PF05577; Peptidase_S28; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   Genevisible; Q9UHL4; HS.
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
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