PERF_MOUSE
ID PERF_MOUSE Reviewed; 554 AA.
AC P10820;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Perforin-1;
DE Short=P1;
DE AltName: Full=Cytolysin;
DE AltName: Full=Lymphocyte pore-forming protein;
DE Flags: Precursor;
GN Name=Prf1; Synonyms=Pfp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2783549; DOI=10.1016/s0006-291x(89)80168-8;
RA Kwon B.S., Wakulchik M., Liu C.C., Persechini P.M., Trapani J.A., Haq A.K.,
RA Kim Y., Young J.D.-E.;
RT "The structure of the mouse lymphocyte pore-forming protein perforin.";
RL Biochem. Biophys. Res. Commun. 158:1-10(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2303785; DOI=10.1084/jem.171.2.545;
RA Trapani J.A., Kwon B.S., Kozak C.A., Chintamaneni C., Young J.D.,
RA Dupont B.;
RT "Genomic organization of the mouse pore-forming protein (perforin) gene and
RT localization to chromosome 10. Similarities to and differences from C9.";
RL J. Exp. Med. 171:545-557(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=3261391; DOI=10.1038/334525a0;
RA Shinkai Y., Takio K., Okumura K.;
RT "Homology of perforin to the ninth component of complement (C9).";
RL Nature 334:525-527(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=2783486; DOI=10.1073/pnas.86.1.247;
RA Lowrey D.M., Aebischer Y., Olsen K., Lichtenheld M., Rupp F.,
RA Hengartner H., Podack E.R.;
RT "Cloning, analysis, and expression of murine perforin 1 cDNA, a component
RT of cytolytic T-cell granules with homology to complement component C9.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:247-251(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Mueller C., Lowin B., Tschopp J.;
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-117.
RC STRAIN=BALB/cJ;
RX PubMed=1401900;
RA Lichtenheld M.G., Podack E.R.;
RT "Structure and function of the murine perforin promoter and upstream
RT region. Reciprocal gene activation or silencing in perforin positive and
RT negative cells.";
RL J. Immunol. 149:2619-2626(1992).
RN [7]
RP PROTEIN SEQUENCE OF 21-52; 76-96; 160-187; 255-278; 312-328; 400-420 AND
RP 439-464.
RX PubMed=3190678; DOI=10.1016/s0006-291x(88)80905-7;
RA Persechini P.M., Young J.D.-E.;
RT "The primary structure of the lymphocyte pore-forming protein perforin:
RT partial amino acid sequencing and determination of isoelectric point.";
RL Biochem. Biophys. Res. Commun. 156:740-745(1988).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=2040805;
RA Ojcius D.M., Zheng L.M., Sphicas E.C., Zychlinsky A., Young J.D.-E.;
RT "Subcellular localization of perforin and serine esterase in lymphokine-
RT activated killer cells and cytotoxic T cells by immunogold labeling.";
RL J. Immunol. 146:4427-4432(1991).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=8164737; DOI=10.1038/369031a0;
RA Kagi D., Ledermann B., Burki K., Seiler P., Odermatt B., Olsen K.J.,
RA Podack E.R., Zinkernagel R.M., Hengartner H.;
RT "Cytotoxicity mediated by T cells and natural killer cells is greatly
RT impaired in perforin-deficient mice.";
RL Nature 369:31-37(1994).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=7526382; DOI=10.1073/pnas.91.23.10854;
RA Walsh C.M., Matloubian M., Liu C.C., Ueda R., Kurahara C.G.,
RA Christensen J.L., Huang M.T., Young J.D., Ahmed R., Clark W.R.;
RT "Immune function in mice lacking the perforin gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:10854-10858(1994).
RN [11]
RP SUBUNIT, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-191;
RP ARG-213 AND GLU-343.
RX PubMed=19446473; DOI=10.1016/j.immuni.2009.03.016;
RA Baran K., Dunstone M., Chia J., Ciccone A., Browne K.A., Clarke C.J.P.,
RA Lukoyanova N., Saibil H., Whisstock J.C., Voskoboinik I., Trapani J.A.;
RT "The molecular basis for perforin oligomerization and transmembrane pore
RT assembly.";
RL Immunity 30:684-695(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 21-554 OF MUTANT GLU-213 IN
RP COMPLEX WITH CALCIUM, COFACTOR, ELECTRON MICROSCOPY OF PORE COMPLEX,
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, GLYCOSYLATION AT ASN-204,
RP DISULFIDE BONDS, AND CALCIUM-BINDING.
RX PubMed=21037563; DOI=10.1038/nature09518;
RA Law R.H., Lukoyanova N., Voskoboinik I., Caradoc-Davies T.T., Baran K.,
RA Dunstone M.A., D'Angelo M.E., Orlova E.V., Coulibaly F., Verschoor S.,
RA Browne K.A., Ciccone A., Kuiper M.J., Bird P.I., Trapani J.A., Saibil H.R.,
RA Whisstock J.C.;
RT "The structural basis for membrane binding and pore formation by lymphocyte
RT perforin.";
RL Nature 468:447-451(2010).
CC -!- FUNCTION: Plays a key role in secretory granule-dependent cell death,
CC and in defense against virus-infected or neoplastic cells
CC (PubMed:19446473, PubMed:21037563, PubMed:3261391, PubMed:7526382,
CC PubMed:8164737). Can insert into the membrane of target cells in its
CC calcium-bound form, oligomerize and form large pores (PubMed:19446473,
CC PubMed:21037563, PubMed:3261391, PubMed:7526382, PubMed:8164737).
CC Promotes cytolysis and apoptosis of target cells by facilitating the
CC uptake of cytotoxic granzymes (PubMed:19446473, PubMed:21037563,
CC PubMed:3261391, PubMed:7526382, PubMed:8164737).
CC {ECO:0000269|PubMed:19446473, ECO:0000269|PubMed:21037563,
CC ECO:0000269|PubMed:3261391, ECO:0000269|PubMed:7526382,
CC ECO:0000269|PubMed:8164737}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041,
CC ECO:0000269|PubMed:21037563};
CC -!- SUBUNIT: Monomer, as soluble protein. Homooligomer. Oligomerization is
CC required for pore formation. {ECO:0000269|PubMed:19446473,
CC ECO:0000269|PubMed:21037563}.
CC -!- SUBCELLULAR LOCATION: Cytolytic granule {ECO:0000269|PubMed:2040805,
CC ECO:0000269|PubMed:8164737}. Secreted {ECO:0000269|PubMed:2040805,
CC ECO:0000269|PubMed:3261391}. Cell membrane
CC {ECO:0000269|PubMed:19446473, ECO:0000269|PubMed:21037563}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:19446473,
CC ECO:0000269|PubMed:21037563}. Endosome lumen
CC {ECO:0000250|UniProtKB:P14222}. Note=Stored in cytolytic granules of
CC cytolytic T-lymphocytes and secreted into the cleft between T-
CC lymphocyte and target cell (PubMed:2040805, PubMed:8164737). May be
CC taken up via endocytosis involving clathrin-coated vesicles and
CC accumulate in a first time in large early endosomes (By similarity).
CC Inserts into the cell membrane of target cells and forms pores.
CC Membrane insertion and pore formation requires a major conformation
CC change (PubMed:19446473, PubMed:21037563).
CC {ECO:0000250|UniProtKB:P14222, ECO:0000269|PubMed:19446473,
CC ECO:0000269|PubMed:2040805, ECO:0000269|PubMed:21037563,
CC ECO:0000269|PubMed:8164737}.
CC -!- TISSUE SPECIFICITY: Detected in cytotoxic T-lymphocytes and natural
CC killer cells. {ECO:0000269|PubMed:2040805, ECO:0000269|PubMed:2783486,
CC ECO:0000269|PubMed:3261391}.
CC -!- DOMAIN: The C2 domain mediates calcium-dependent binding to lipid
CC membranes. A subsequent conformation change leads to membrane insertion
CC of beta-hairpin structures and pore formation. The pore is formed by
CC transmembrane beta-strands. {ECO:0000269|PubMed:21037563}.
CC -!- PTM: N-glycosylated. The glycosylation sites are facing the interior of
CC the pore. {ECO:0000269|PubMed:21037563}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, but die of virus
CC infections that are normally efficiently dealt with by the immune
CC system. They cannot eliminate lymphocytic choriomeningitis virus, but
CC die of the infection. Young mice are abnormally susceptible to mouse
CC hepatitis virus. Cytolytic activity towards tumor cells and transplants
CC is also severely reduced. {ECO:0000269|PubMed:7526382,
CC ECO:0000269|PubMed:8164737}.
CC -!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Our hollow architecture
CC - Issue 126 of February 2011;
CC URL="https://web.expasy.org/spotlight/back_issues/126";
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DR EMBL; M23182; AAA39910.1; -; mRNA.
DR EMBL; X51340; CAA35721.1; -; Genomic_DNA.
DR EMBL; X51446; CAA35721.1; JOINED; Genomic_DNA.
DR EMBL; X12760; CAA31251.1; -; mRNA.
DR EMBL; J04148; AAA39909.1; -; mRNA.
DR EMBL; X60165; CAA42731.1; -; mRNA.
DR EMBL; M95527; AAB01574.1; -; Genomic_DNA.
DR CCDS; CCDS23875.1; -.
DR PIR; JL0146; A31300.
DR RefSeq; NP_035203.3; NM_011073.3.
DR RefSeq; XP_006513433.1; XM_006513370.3.
DR PDB; 3NSJ; X-ray; 2.75 A; A=21-554.
DR PDB; 4Y1S; X-ray; 1.61 A; A=410-535.
DR PDB; 4Y1T; X-ray; 2.67 A; A=410-535.
DR PDB; 5UG6; X-ray; 2.00 A; A=410-535.
DR PDB; 5UG7; X-ray; 1.80 A; A=410-535.
DR PDB; 7PAG; EM; 4.00 A; A=21-554.
DR PDBsum; 3NSJ; -.
DR PDBsum; 4Y1S; -.
DR PDBsum; 4Y1T; -.
DR PDBsum; 5UG6; -.
DR PDBsum; 5UG7; -.
DR PDBsum; 7PAG; -.
DR AlphaFoldDB; P10820; -.
DR SMR; P10820; -.
DR BioGRID; 202128; 2.
DR DIP; DIP-59218N; -.
DR STRING; 10090.ENSMUSP00000041483; -.
DR GlyGen; P10820; 3 sites.
DR iPTMnet; P10820; -.
DR PhosphoSitePlus; P10820; -.
DR SwissPalm; P10820; -.
DR EPD; P10820; -.
DR MaxQB; P10820; -.
DR PaxDb; P10820; -.
DR PRIDE; P10820; -.
DR ProteomicsDB; 287675; -.
DR Antibodypedia; 3723; 602 antibodies from 44 providers.
DR DNASU; 18646; -.
DR Ensembl; ENSMUST00000035419; ENSMUSP00000041483; ENSMUSG00000037202.
DR Ensembl; ENSMUST00000219375; ENSMUSP00000151354; ENSMUSG00000037202.
DR GeneID; 18646; -.
DR KEGG; mmu:18646; -.
DR UCSC; uc007ffv.2; mouse.
DR CTD; 5551; -.
DR MGI; MGI:97551; Prf1.
DR VEuPathDB; HostDB:ENSMUSG00000037202; -.
DR eggNOG; ENOG502RQWS; Eukaryota.
DR GeneTree; ENSGT00530000063725; -.
DR HOGENOM; CLU_039516_2_0_1; -.
DR InParanoid; P10820; -.
DR OMA; LCKNALQ; -.
DR OrthoDB; 360042at2759; -.
DR PhylomeDB; P10820; -.
DR TreeFam; TF330498; -.
DR BioGRID-ORCS; 18646; 1 hit in 73 CRISPR screens.
DR EvolutionaryTrace; P10820; -.
DR PRO; PR:P10820; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P10820; protein.
DR Bgee; ENSMUSG00000037202; Expressed in gastrula and 37 other tissues.
DR ExpressionAtlas; P10820; baseline and differential.
DR Genevisible; P10820; MM.
DR GO; GO:0044194; C:cytolytic granule; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031904; C:endosome lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0022829; F:wide pore channel activity; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0007623; P:circadian rhythm; ISO:MGI.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0002357; P:defense response to tumor cell; IMP:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0002418; P:immune response to tumor cell; IMP:UniProtKB.
DR GO; GO:0001771; P:immunological synapse formation; ISO:MGI.
DR GO; GO:0051712; P:positive regulation of killing of cells of another organism; ISO:MGI.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0001913; P:T cell mediated cytotoxicity; IDA:MGI.
DR CDD; cd04032; C2_Perforin; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR020864; MACPF.
DR InterPro; IPR020863; MACPF_CS.
DR InterPro; IPR037300; Perforin-1_C2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF01823; MACPF; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00457; MACPF; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00279; MACPF_1; 1.
DR PROSITE; PS51412; MACPF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell membrane; Cytolysis; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Endosome; Glycoprotein; Lysosome;
KW Membrane; Metal-binding; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane beta strand.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:3190678,
FT ECO:0000269|PubMed:3261391"
FT CHAIN 21..554
FT /note="Perforin-1"
FT /id="PRO_0000023610"
FT DOMAIN 26..374
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT DOMAIN 375..407
FT /note="EGF-like"
FT DOMAIN 395..513
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21037563"
FT BINDING 483
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21037563"
FT BINDING 484
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21037563"
FT BINDING 485
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21037563"
FT BINDING 488
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21037563"
FT BINDING 490
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21037563"
FT SITE 213
FT /note="Important for oligomerization"
FT /evidence="ECO:0000269|PubMed:19446473"
FT SITE 343
FT /note="Important for oligomerization"
FT /evidence="ECO:0000269|PubMed:19446473"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21037563"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 22..75
FT /evidence="ECO:0000269|PubMed:21037563"
FT DISULFID 30..72
FT /evidence="ECO:0000269|PubMed:21037563"
FT DISULFID 101..175
FT /evidence="ECO:0000269|PubMed:21037563"
FT DISULFID 241..407
FT /evidence="ECO:0000269|PubMed:21037563"
FT DISULFID 376..392
FT /evidence="ECO:0000269|PubMed:21037563"
FT DISULFID 380..394
FT /evidence="ECO:0000269|PubMed:21037563"
FT DISULFID 396..406
FT /evidence="ECO:0000269|PubMed:21037563"
FT DISULFID 496..509
FT /evidence="ECO:0000269|PubMed:21037563"
FT DISULFID 524..533
FT /evidence="ECO:0000269|PubMed:21037563"
FT MUTAGEN 191
FT /note="D->K,V: Loss of cytotoxicity."
FT /evidence="ECO:0000269|PubMed:19446473"
FT MUTAGEN 191
FT /note="D->S: Strongly decreased cytotoxicity."
FT /evidence="ECO:0000269|PubMed:19446473"
FT MUTAGEN 213
FT /note="R->E,L: Strongly decreased cytotoxicity."
FT /evidence="ECO:0000269|PubMed:19446473"
FT MUTAGEN 343
FT /note="E->R: Strongly decreased cytotoxicity."
FT /evidence="ECO:0000269|PubMed:19446473"
FT CONFLICT 3
FT /note="T -> M (in Ref. 3; CAA31251)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="R -> P (in Ref. 4; AAA39909)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="G -> A (in Ref. 3; CAA31251 and 5; CAA42731)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="D -> E (in Ref. 4; AAA39909)"
FT /evidence="ECO:0000305"
FT CONFLICT 543..550
FT /note="GDPPGNRS -> EILQETAC (in Ref. 4; AAA39909)"
FT /evidence="ECO:0000305"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:3NSJ"
FT HELIX 27..31
FT /evidence="ECO:0007829|PDB:3NSJ"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:3NSJ"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3NSJ"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:3NSJ"
FT TURN 78..82
FT /evidence="ECO:0007829|PDB:3NSJ"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:3NSJ"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:3NSJ"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:3NSJ"
FT HELIX 113..121
FT /evidence="ECO:0007829|PDB:3NSJ"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:3NSJ"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:3NSJ"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:3NSJ"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:3NSJ"
FT STRAND 166..182
FT /evidence="ECO:0007829|PDB:3NSJ"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:3NSJ"
FT HELIX 208..218
FT /evidence="ECO:0007829|PDB:3NSJ"
FT STRAND 220..239
FT /evidence="ECO:0007829|PDB:3NSJ"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:3NSJ"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:3NSJ"
FT HELIX 273..284
FT /evidence="ECO:0007829|PDB:3NSJ"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:3NSJ"
FT STRAND 298..305
FT /evidence="ECO:0007829|PDB:3NSJ"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:3NSJ"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:3NSJ"
FT HELIX 321..330
FT /evidence="ECO:0007829|PDB:3NSJ"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:3NSJ"
FT STRAND 336..344
FT /evidence="ECO:0007829|PDB:3NSJ"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:3NSJ"
FT HELIX 355..369
FT /evidence="ECO:0007829|PDB:3NSJ"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:3NSJ"
FT STRAND 394..397
FT /evidence="ECO:0007829|PDB:3NSJ"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:3NSJ"
FT HELIX 404..406
FT /evidence="ECO:0007829|PDB:3NSJ"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:3NSJ"
FT STRAND 412..424
FT /evidence="ECO:0007829|PDB:4Y1S"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:5UG7"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:4Y1S"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:4Y1S"
FT STRAND 464..470
FT /evidence="ECO:0007829|PDB:4Y1S"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:4Y1S"
FT STRAND 477..483
FT /evidence="ECO:0007829|PDB:4Y1S"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:5UG7"
FT STRAND 491..498
FT /evidence="ECO:0007829|PDB:4Y1S"
FT STRAND 502..510
FT /evidence="ECO:0007829|PDB:4Y1S"
FT STRAND 512..524
FT /evidence="ECO:0007829|PDB:4Y1S"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:3NSJ"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:3NSJ"
SQ SEQUENCE 554 AA; 62081 MW; 9E5964CE9FE8A0D8 CRC64;
MATCLFLLGL FLLLPRPVPA PCYTATRSEC KQKHKFVPGV WMAGEGMDVT TLRRSGSFPV
NTQRFLRPDR TCTLCKNSLM RDATQRLPVA ITHWRPHSSH CQRNVAAAKV HSTEGVAREA
AANINNDWRV GLDVNPRPEA NMRASVAGSH SKVANFAAEK TYQDQYNFNS DTVECRMYSF
RLVQKPPLHL DFKKALRALP RNFNSSTEHA YHRLISSYGT HFITAVDLGG RISVLTALRT
CQLTLNGLTA DEVGDCLNVE AQVSIGAQAS VSSEYKACEE KKKQHKMATS FHQTYRERHV
EVLGGPLDST HDLLFGNQAT PEQFSTWTAS LPSNPGLVDY SLEPLHTLLE EQNPKREALR
QAISHYIMSR ARWQNCSRPC RSGQHKSSHD SCQCECQDSK VTNQDCCPRQ RGLAHLVVSN
FRAEHLWGDY TTATDAYLKV FFGGQEFRTG VVWNNNNPRW TDKMDFENVL LSTGGPLRVQ
VWDADYGWDD DLLGSCDRSP HSGFHEVTCE LNHGRVKFSY HAKCLPHLTG GTCLEYAPQG
LLGDPPGNRS GAVW
