ERAP2_HUMAN
ID ERAP2_HUMAN Reviewed; 960 AA.
AC Q6P179; Q7Z5K1; Q8TD32; Q8WVJ4; Q9HBX2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Endoplasmic reticulum aminopeptidase 2;
DE EC=3.4.11.-;
DE AltName: Full=Leukocyte-derived arginine aminopeptidase;
DE Short=L-RAP;
GN Name=ERAP2; Synonyms=LRAP;
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] (ISOFORM 1), FUNCTION, ENZYME ACTIVITY,
RP SUBCELLULAR LOCATION, GLYCOSYLATION, TOPOLOGY, TISSUE SPECIFICITY, AND
RP VARIANT ASN-392.
RX PubMed=12799365; DOI=10.1074/jbc.m305076200;
RA Tanioka T., Hattori A., Masuda S., Nomura Y., Nakayama H., Mizutani S.,
RA Tsujimoto M.;
RT "Human leukocyte-derived arginine aminopeptidase. The third member of the
RT oxytocinase subfamily of aminopeptidases.";
RL J. Biol. Chem. 278:32275-32283(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION BY IFNG, AND VARIANT
RP ASN-392.
RX PubMed=15691326; DOI=10.1111/j.1742-4658.2004.04521.x;
RA Tanioka T., Hattori A., Mizutani S., Tsujimoto M.;
RT "Regulation of the human leukocyte-derived arginine
RT aminopeptidase/endoplasmic reticulum-aminopeptidase 2 gene by interferon-
RT gamma.";
RL FEBS J. 272:916-928(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Schomburg L.;
RT "Molecular characterization of aminopeptidase MAMS.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Skeletal muscle, and Skin;
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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [7]
RP FUNCTION, SUBUNIT, AND INDUCTION BY IFNG.
RX PubMed=15908954; DOI=10.1038/ni1208;
RA Saveanu L., Carroll O., Lindo V., Del Val M., Lopez D., Lepelletier Y.,
RA Greer F., Schomburg L., Fruci D., Niedermann G., van Endert P.M.;
RT "Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase
RT complexes in the endoplasmic reticulum.";
RL Nat. Immunol. 6:689-697(2005).
RN [8]
RP FUNCTION.
RX PubMed=16286653; DOI=10.1073/pnas.0500721102;
RA Chang S.-C., Momburg F., Bhutani N., Goldberg A.L.;
RT "The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I
RT peptides by a 'molecular ruler' mechanism.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:17107-17112(2005).
RN [9]
RP GENE REGULATION.
RX PubMed=16585582; DOI=10.4049/jimmunol.176.8.4869;
RA Fruci D., Ferracuti S., Limongi M.Z., Cunsolo V., Giorda E., Fraioli R.,
RA Sibilio L., Carroll O., Hattori A., van Endert P.M., Giacomini P.;
RT "Expression of endoplasmic reticulum aminopeptidases in EBV-B cell lines
RT from healthy donors and in leukemia/lymphoma, carcinoma, and melanoma cell
RT lines.";
RL J. Immunol. 176:4869-4879(2006).
RN [10]
RP ALTERNATIVE SPLICING.
RX PubMed=17332242; DOI=10.1182/blood-2006-11-057208;
RA Pinyol M., Bea S., Pla L., Ribrag V., Bosq J., Rosenwald A., Campo E.,
RA Jares P.;
RT "Inactivation of RB1 in mantle-cell lymphoma detected by nonsense-mediated
RT mRNA decay pathway inhibition and microarray analysis.";
RL Blood 109:5422-5429(2007).
RN [11]
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 [12]
RP X-RAY CRYSTALLOGRAPHY (3.08 ANGSTROMS) OF 3-960 IN COMPLEX WITH SUBSTRATE,
RP GLYCOSYLATION AT ASN-85; ASN-219; ASN-405 AND ASN-650, ACTIVE SITE,
RP ZINC-BINDING SITES, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=22106953; DOI=10.1021/bi201230p;
RA Birtley J.R., Saridakis E., Stratikos E., Mavridis I.M.;
RT "The crystal structure of human endoplasmic reticulum aminopeptidase 2
RT reveals the atomic basis for distinct roles in antigen processing.";
RL Biochemistry 51:286-295(2012).
CC -!- FUNCTION: Aminopeptidase that plays a central role in peptide trimming,
CC a step required for the generation of most HLA class I-binding
CC peptides. Peptide trimming is essential to customize longer precursor
CC peptides to fit them to the correct length required for presentation on
CC MHC class I molecules. Preferentially hydrolyzes the basic residues Arg
CC and Lys. {ECO:0000269|PubMed:12799365, ECO:0000269|PubMed:15908954,
CC ECO:0000269|PubMed:16286653}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterodimer with ERAP1. {ECO:0000269|PubMed:15908954,
CC ECO:0000269|PubMed:22106953}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12799365}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:12799365}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6P179-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P179-2; Sequence=VSP_030674, VSP_030675;
CC Name=3;
CC IsoId=Q6P179-3; Sequence=VSP_030671;
CC Name=4;
CC IsoId=Q6P179-4; Sequence=VSP_030672, VSP_030673;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in spleen
CC and leukocytes. {ECO:0000269|PubMed:12799365}.
CC -!- INDUCTION: By IFNG/IFN-gamma. {ECO:0000269|PubMed:15691326,
CC ECO:0000269|PubMed:15908954}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12799365,
CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:22106953}.
CC -!- MISCELLANEOUS: Defects in the expression of this gene may cause
CC improper antigen processing, possibly leading to favor tumor escape
CC from the immune surveillance.
CC -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR EMBL; AB109031; BAC78818.1; -; mRNA.
DR EMBL; AB163917; BAD90015.1; -; mRNA.
DR EMBL; AY028805; AAK37776.1; -; mRNA.
DR EMBL; AF191545; AAG28383.1; -; mRNA.
DR EMBL; CH471084; EAW96080.1; -; Genomic_DNA.
DR EMBL; BC065240; AAH65240.1; -; mRNA.
DR EMBL; BC017927; AAH17927.1; -; mRNA.
DR CCDS; CCDS4086.1; -. [Q6P179-1]
DR CCDS; CCDS87316.1; -. [Q6P179-4]
DR CCDS; CCDS87317.1; -. [Q6P179-3]
DR RefSeq; NP_001123612.1; NM_001130140.2. [Q6P179-1]
DR RefSeq; NP_001316158.1; NM_001329229.1. [Q6P179-3]
DR RefSeq; NP_001316162.1; NM_001329233.1. [Q6P179-4]
DR RefSeq; NP_071745.1; NM_022350.4. [Q6P179-1]
DR PDB; 3SE6; X-ray; 3.08 A; A/B=1-960.
DR PDB; 4E36; X-ray; 3.22 A; A/B=1-960.
DR PDB; 4JBS; X-ray; 2.79 A; A/B=3-960.
DR PDB; 5AB0; X-ray; 2.50 A; A/C=1-960.
DR PDB; 5AB2; X-ray; 2.73 A; A/B=1-960.
DR PDB; 5CU5; X-ray; 3.02 A; A/B=1-960.
DR PDB; 5J6S; X-ray; 2.80 A; A/B=1-960.
DR PDB; 5K1V; X-ray; 2.90 A; A/B=1-960.
DR PDB; 6EA4; X-ray; 2.45 A; A/B=1-960.
DR PDB; 7P7P; X-ray; 3.00 A; A/B=1-960.
DR PDB; 7PFS; X-ray; 2.70 A; A/B=1-960.
DR PDBsum; 3SE6; -.
DR PDBsum; 4E36; -.
DR PDBsum; 4JBS; -.
DR PDBsum; 5AB0; -.
DR PDBsum; 5AB2; -.
DR PDBsum; 5CU5; -.
DR PDBsum; 5J6S; -.
DR PDBsum; 5K1V; -.
DR PDBsum; 6EA4; -.
DR PDBsum; 7P7P; -.
DR PDBsum; 7PFS; -.
DR AlphaFoldDB; Q6P179; -.
DR SMR; Q6P179; -.
DR BioGRID; 122092; 20.
DR CORUM; Q6P179; -.
DR IntAct; Q6P179; 3.
DR STRING; 9606.ENSP00000400376; -.
DR BindingDB; Q6P179; -.
DR ChEMBL; CHEMBL5043; -.
DR GuidetoPHARMACOLOGY; 1567; -.
DR MEROPS; M01.024; -.
DR GlyConnect; 1204; 16 N-Linked glycans (7 sites).
DR GlyGen; Q6P179; 10 sites, 16 N-linked glycans (7 sites).
DR iPTMnet; Q6P179; -.
DR PhosphoSitePlus; Q6P179; -.
DR BioMuta; ERAP2; -.
DR DMDM; 166232401; -.
DR EPD; Q6P179; -.
DR jPOST; Q6P179; -.
DR MassIVE; Q6P179; -.
DR MaxQB; Q6P179; -.
DR PaxDb; Q6P179; -.
DR PeptideAtlas; Q6P179; -.
DR PRIDE; Q6P179; -.
DR ProteomicsDB; 66824; -. [Q6P179-1]
DR ProteomicsDB; 66825; -. [Q6P179-2]
DR ProteomicsDB; 66826; -. [Q6P179-3]
DR ProteomicsDB; 66827; -. [Q6P179-4]
DR Antibodypedia; 25082; 132 antibodies from 32 providers.
DR DNASU; 64167; -.
DR Ensembl; ENST00000379904.8; ENSP00000369235.4; ENSG00000164308.17. [Q6P179-3]
DR Ensembl; ENST00000437043.8; ENSP00000400376.3; ENSG00000164308.17. [Q6P179-1]
DR Ensembl; ENST00000510309.1; ENSP00000425758.1; ENSG00000164308.17. [Q6P179-4]
DR Ensembl; ENST00000513084.5; ENSP00000421849.1; ENSG00000164308.17. [Q6P179-2]
DR GeneID; 64167; -.
DR KEGG; hsa:64167; -.
DR MANE-Select; ENST00000437043.8; ENSP00000400376.3; NM_022350.5; NP_071745.1.
DR UCSC; uc003kmq.4; human. [Q6P179-1]
DR CTD; 64167; -.
DR DisGeNET; 64167; -.
DR GeneCards; ERAP2; -.
DR HGNC; HGNC:29499; ERAP2.
DR HPA; ENSG00000164308; Tissue enhanced (lymphoid).
DR MIM; 609497; gene.
DR neXtProt; NX_Q6P179; -.
DR OpenTargets; ENSG00000164308; -.
DR PharmGKB; PA162385208; -.
DR VEuPathDB; HostDB:ENSG00000164308; -.
DR eggNOG; KOG1046; Eukaryota.
DR GeneTree; ENSGT00940000162653; -.
DR HOGENOM; CLU_003705_0_1_1; -.
DR InParanoid; Q6P179; -.
DR OMA; KSTYRTH; -.
DR PhylomeDB; Q6P179; -.
DR TreeFam; TF300395; -.
DR BRENDA; 3.4.11.1; 2681.
DR BRENDA; 3.4.11.6; 2681.
DR PathwayCommons; Q6P179; -.
DR Reactome; R-HSA-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR SABIO-RK; Q6P179; -.
DR SignaLink; Q6P179; -.
DR BioGRID-ORCS; 64167; 8 hits in 1073 CRISPR screens.
DR ChiTaRS; ERAP2; human.
DR GenomeRNAi; 64167; -.
DR Pharos; Q6P179; Tchem.
DR PRO; PR:Q6P179; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q6P179; protein.
DR Bgee; ENSG00000164308; Expressed in buccal mucosa cell and 165 other tissues.
DR ExpressionAtlas; Q6P179; baseline and differential.
DR Genevisible; Q6P179; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:BHF-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004177; F:aminopeptidase activity; IDA:HGNC-UCL.
DR GO; GO:0004175; F:endopeptidase activity; EXP:Reactome.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:HGNC-UCL.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; TAS:HGNC-UCL.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
DR GO; GO:0043171; P:peptide catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.10.390.10; -; 1.
DR Gene3D; 2.60.40.1730; -; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR033528; ERAP2.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF239; PTHR11533:SF239; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; SSF63737; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Adaptive immunity; Alternative splicing; Aminopeptidase;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; Immunity;
KW Membrane; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..960
FT /note="Endoplasmic reticulum aminopeptidase 2"
FT /id="PRO_0000315719"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..40
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..960
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT ACT_SITE 371
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095,
FT ECO:0000269|PubMed:22106953"
FT BINDING 200
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22106953"
FT BINDING 334..338
FT /ligand="substrate"
FT BINDING 370
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT SITE 455
FT /note="Transition state stabilizer"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22106953"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22106953"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22106953"
FT CARBOHYD 650
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22106953"
FT DISULFID 421..460
FT /evidence="ECO:0000269|PubMed:22106953"
FT DISULFID 759..766
FT /evidence="ECO:0000269|PubMed:22106953"
FT VAR_SEQ 238..282
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030671"
FT VAR_SEQ 324..350
FT /note="DLIAIPDFAPGAMENWGLITYRETSLL -> GMFKFHIIVFIFAHKTCFDLF
FT PLSLSM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030672"
FT VAR_SEQ 351..960
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030673"
FT VAR_SEQ 525..532
FT /note="LAFLGENA -> VRIKRVTE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15691326"
FT /id="VSP_030674"
FT VAR_SEQ 533..960
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15691326"
FT /id="VSP_030675"
FT VARIANT 214
FT /note="P -> L (in dbSNP:rs3733905)"
FT /id="VAR_038285"
FT VARIANT 392
FT /note="K -> N (in dbSNP:rs2549782)"
FT /evidence="ECO:0000269|PubMed:12799365,
FT ECO:0000269|PubMed:15691326"
FT /id="VAR_038286"
FT VARIANT 411
FT /note="L -> R (in dbSNP:rs34261036)"
FT /id="VAR_051569"
FT VARIANT 669
FT /note="L -> Q (in dbSNP:rs17408150)"
FT /id="VAR_038287"
FT CONFLICT 129
FT /note="R -> K (in Ref. 5; AAH17927)"
FT /evidence="ECO:0000305"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:7P7P"
FT STRAND 71..85
FT /evidence="ECO:0007829|PDB:6EA4"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 90..103
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 116..123
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 161..171
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 173..185
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:5AB0"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:6EA4"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 218..226
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:5J6S"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 272..277
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 290..296
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 297..314
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 320..330
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:6EA4"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 358..376
FT /evidence="ECO:0007829|PDB:6EA4"
FT TURN 378..380
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 381..385
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 390..407
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 413..428
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:5J6S"
FT HELIX 443..448
FT /evidence="ECO:0007829|PDB:6EA4"
FT TURN 452..455
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 456..469
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 471..485
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 492..500
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:5AB0"
FT STRAND 510..517
FT /evidence="ECO:0007829|PDB:5AB0"
FT HELIX 531..542
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 548..555
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 558..565
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:7PFS"
FT HELIX 575..581
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 588..596
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 601..605
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 607..613
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 621..624
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 625..627
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 632..635
FT /evidence="ECO:0007829|PDB:6EA4"
FT TURN 636..638
FT /evidence="ECO:0007829|PDB:5J6S"
FT HELIX 639..650
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 651..653
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 656..671
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 673..675
FT /evidence="ECO:0007829|PDB:4E36"
FT HELIX 677..683
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 684..689
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 693..713
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 716..729
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 731..735
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 739..741
FT /evidence="ECO:0007829|PDB:5AB0"
FT HELIX 745..760
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 764..780
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 788..790
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 791..798
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 802..814
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 818..828
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 834..846
FT /evidence="ECO:0007829|PDB:6EA4"
FT STRAND 848..850
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 852..854
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 855..863
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 866..878
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 880..886
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 892..902
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 908..923
FT /evidence="ECO:0007829|PDB:6EA4"
FT HELIX 930..960
FT /evidence="ECO:0007829|PDB:6EA4"
SQ SEQUENCE 960 AA; 110462 MW; 261EFC06870D644E CRC64;
MFHSSAMVNS HRKPMFNIHR GFYCLTAILP QICICSQFSV PSSYHFTEDP GAFPVATNGE
RFPWQELRLP SVVIPLHYDL FVHPNLTSLD FVASEKIEVL VSNATQFIIL HSKDLEITNA
TLQSEEDSRY MKPGKELKVL SYPAHEQIAL LVPEKLTPHL KYYVAMDFQA KLGDGFEGFY
KSTYRTLGGE TRILAVTDFE PTQARMAFPC FDEPLFKANF SIKIRRESRH IALSNMPKVK
TIELEGGLLE DHFETTVKMS TYLVAYIVCD FHSLSGFTSS GVKVSIYASP DKRNQTHYAL
QASLKLLDFY EKYFDIYYPL SKLDLIAIPD FAPGAMENWG LITYRETSLL FDPKTSSASD
KLWVTRVIAH ELAHQWFGNL VTMEWWNDIW LKEGFAKYME LIAVNATYPE LQFDDYFLNV
CFEVITKDSL NSSRPISKPA ETPTQIQEMF DEVSYNKGAC ILNMLKDFLG EEKFQKGIIQ
YLKKFSYRNA KNDDLWSSLS NSCLESDFTS GGVCHSDPKM TSNMLAFLGE NAEVKEMMTT
WTLQKGIPLL VVKQDGCSLR LQQERFLQGV FQEDPEWRAL QERYLWHIPL TYSTSSSNVI
HRHILKSKTD TLDLPEKTSW VKFNVDSNGY YIVHYEGHGW DQLITQLNQN HTLLRPKDRV
GLIHDVFQLV GAGRLTLDKA LDMTYYLQHE TSSPALLEGL SYLESFYHMM DRRNISDISE
NLKRYLLQYF KPVIDRQSWS DKGSVWDRML RSALLKLACD LNHAPCIQKA AELFSQWMES
SGKLNIPTDV LKIVYSVGAQ TTAGWNYLLE QYELSMSSAE QNKILYALST SKHQEKLLKL
IELGMEGKVI KTQNLAALLH AIARRPKGQQ LAWDFVRENW THLLKKFDLG SYDIRMIISG
TTAHFSSKDK LQEVKLFFES LEAQGSHLDI FQTVLETITK NIKWLEKNLP TLRTWLMVNT
