MPEG1_HUMAN
ID MPEG1_HUMAN Reviewed; 716 AA.
AC Q2M385; Q2M1T6; Q8TEF8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Macrophage-expressed gene 1 protein;
DE Short=Macrophage gene 1 protein;
DE Short=Mpg-1;
DE AltName: Full=Perforin-2 {ECO:0000303|PubMed:23753625};
DE Short=P-2 {ECO:0000303|PubMed:23753625};
DE Flags: Precursor;
GN Name=MPEG1;
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 [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-552.
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=7888681;
RA Spilsbury K., O'Mara M.-A., Wu W.M., Rowe P.B., Symonds G., Takayama Y.;
RT "Isolation of a novel macrophage-specific gene by differential cDNA
RT analysis.";
RL Blood 85:1620-1629(1995).
RN [5]
RP FUNCTION.
RX PubMed=23753625; DOI=10.1128/iai.00497-13;
RA Fields K.A., McCormack R., de Armas L.R., Podack E.R.;
RT "Perforin-2 restricts growth of Chlamydia trachomatis in macrophages.";
RL Infect. Immun. 81:3045-3054(2013).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=26402460; DOI=10.7554/elife.06508;
RA McCormack R.M., de Armas L.R., Shiratsuchi M., Fiorentino D.G.,
RA Olsson M.L., Lichtenheld M.G., Morales A., Lyapichev K., Gonzalez L.E.,
RA Strbo N., Sukumar N., Stojadinovic O., Plano G.V., Munson G.P.,
RA Tomic-Canic M., Kirsner R.S., Russell D.G., Podack E.R.;
RT "Perforin-2 is essential for intracellular defense of parenchymal cells and
RT phagocytes against pathogenic bacteria.";
RL Elife 4:E06508-E06508(2015).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING, AND
RP INDUCTION.
RX PubMed=28705375; DOI=10.1016/j.cellimm.2017.07.001;
RA Xiong P., Shiratsuchi M., Matsushima T., Liao J., Tanaka E., Nakashima Y.,
RA Takayanagi R., Ogawa Y.;
RT "Regulation of expression and trafficking of perforin-2 by LPS and TNF-
RT alpha.";
RL Cell. Immunol. 320:1-10(2017).
RN [8]
RP INVOLVEMENT IN IMD77, VARIANTS IMD77 ALA-73; 398-GLN--ALA-716 DEL AND
RP THR-405, VARIANT SER-316, CHARACTERIZATION OF VARIANTS IMD77 ALA-73;
RP 398-GLN--ALA-716 DEL AND THR-405, CHARACTERIZATION OF VARIANT SER-316, AND
RP FUNCTION.
RX PubMed=28422754; DOI=10.1172/jci.insight.89635;
RA McCormack R.M., Szymanski E.P., Hsu A.P., Perez E., Olivier K.N.,
RA Fisher E., Goodhew E.B., Podack E.R., Holland S.M.;
RT "MPEG1/perforin-2 mutations in human pulmonary nontuberculous mycobacterial
RT infections.";
RL JCI Insight 2:0-0(2017).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=30609079; DOI=10.1111/exd.13870;
RA Strbo N., Pastar I., Romero L., Chen V., Vujanac M., Sawaya A.P., Jozic I.,
RA Ferreira A.D.F., Wong L.L., Head C., Stojadinovic O., Garcia D.,
RA O'Neill K., Drakulich S., Taller S., Kirsner R.S., Tomic-Canic M.;
RT "Single cell analyses reveal specific distribution of anti-bacterial
RT molecule Perforin-2 in human skin and its modulation by wounding and
RT Staphylococcus aureus infection.";
RL Exp. Dermatol. 28:225-232(2019).
RN [10]
RP VARIANT IMD77 430-TYR--ALA-716 DEL, CHARACTERIZATION OF VARIANT IMD77
RP 430-TYR--ALA-716 DEL, AND FUNCTION.
RX PubMed=33224153; DOI=10.3389/fimmu.2020.601584;
RA Merselis L.C., Jiang S.Y., Nelson S.F., Lee H., Prabaker K.K., Baker J.L.,
RA Munson G.P., Butte M.J.;
RT "MPEG1/Perforin-2 Haploinsufficiency Associated Polymicrobial Skin
RT Infections and Considerations for Interferon-gamma Therapy.";
RL Front. Immunol. 11:601584-601584(2020).
CC -!- FUNCTION: Plays a key role in the innate immune response following
CC bacterial infection by inserting into the bacterial surface to form
CC pores (By similarity). By breaching the surface of phagocytosed
CC bacteria, allows antimicrobial effectors to enter the bacterial
CC periplasmic space and degrade bacterial proteins such as superoxide
CC dismutase sodC which contributes to bacterial virulence (By
CC similarity). Shows antibacterial activity against a wide spectrum of
CC Gram-positive, Gram-negative and acid-fast bacteria (PubMed:23753625,
CC PubMed:26402460, PubMed:30609079, PubMed:28422754, PubMed:33224153).
CC Reduces the viability of the intracytosolic pathogen L.monocytogenes by
CC inhibiting acidification of the phagocytic vacuole of host cells which
CC restricts bacterial translocation from the vacuole to the cytosol (By
CC similarity). Required for the antibacterial activity of reactive oxygen
CC species and nitric oxide (By similarity).
CC {ECO:0000250|UniProtKB:A1L314, ECO:0000269|PubMed:23753625,
CC ECO:0000269|PubMed:26402460, ECO:0000269|PubMed:28422754,
CC ECO:0000269|PubMed:30609079, ECO:0000269|PubMed:33224153}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:28705375}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Bacterial infection induces translocation of the
CC cytoplasmic vesicles to bacterium-containing phagocytic vesicles and
CC fusing of the vesicles. {ECO:0000269|PubMed:28705375}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000269|PubMed:28705375}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PRF2a {ECO:0000303|PubMed:28705375};
CC IsoId=Q2M385-1; Sequence=Displayed;
CC Name=2; Synonyms=PRF2b {ECO:0000303|PubMed:28705375};
CC IsoId=Q2M385-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Expressed constitutively in a variety of cell types
CC including macrophages, natural killer cells, neutrophils, keratinocytes
CC and monocytes (PubMed:26402460, PubMed:28705375, PubMed:7888681). In
CC skin, expressed in both hematopoietic and non-hematopoietic cells with
CC expression detected in a variety of cell types including keratinocytes,
CC fibroblasts and endothelial cells (PubMed:30609079).
CC {ECO:0000269|PubMed:26402460, ECO:0000269|PubMed:28705375,
CC ECO:0000269|PubMed:30609079, ECO:0000269|PubMed:7888681}.
CC -!- INDUCTION: By wounding; increased levels are observed in hematopoietic
CC cells 48 hours after wounding (PubMed:30609079). Following wounding,
CC repressed by infection with S.aureus (PubMed:30609079). Isoform 1: By
CC lipopolysaccharide and TNF (PubMed:28705375). Isoform 2: By
CC lipopolysaccharide and TNF (PubMed:28705375).
CC {ECO:0000269|PubMed:28705375, ECO:0000269|PubMed:30609079}.
CC -!- PTM: Monoubiquitinated in response to bacterial infection;
CC ubiquitination is required for vesicular localization and antibacterial
CC activity and can be blocked by bacterial cell cycle inhibiting factor
CC (cif) (By similarity). {ECO:0000250|UniProtKB:A1L314}.
CC -!- DISEASE: Immunodeficiency 77 (IMD77) [MIM:619223]: An autosomal
CC dominant disorder characterized by recurrent, persistent bacterial and
CC fungal infections with multiple unusual organisms. Skin and pulmonary
CC infections are the most common. Patient macrophages show impaired
CC killing of intracellular bacteria and organisms, including non-
CC tubercular mycobacteria, Pseudomonas, Candida, and Aspergillus.
CC {ECO:0000269|PubMed:28422754, ECO:0000269|PubMed:33224153}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 2]: Lacks the C-terminal transmembrane domain.
CC {ECO:0000269|PubMed:28705375}.
CC -!- SIMILARITY: Belongs to the MPEG1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB84992.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK074166; BAB84992.1; ALT_INIT; mRNA.
DR EMBL; CH471076; EAW73839.1; -; Genomic_DNA.
DR EMBL; BC104997; AAI04998.1; -; mRNA.
DR EMBL; BC112230; AAI12231.1; -; mRNA.
DR CCDS; CCDS41650.1; -. [Q2M385-1]
DR RefSeq; NP_001034485.1; NM_001039396.1. [Q2M385-1]
DR PDB; 6U23; EM; 3.49 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=18-653.
DR PDB; 6U2J; EM; 2.37 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=18-653.
DR PDB; 6U2K; EM; 2.93 A; B=18-653.
DR PDB; 6U2L; EM; 2.83 A; A/AA/B/BB/C/CC/D/DD/E/EE/F/FF/G/GG/H/HH/I/II/J/JJ/K/KK/L/LL/M/MM/N/NN/O/OO=18-653.
DR PDB; 6U2W; EM; 3.63 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=18-653.
DR PDBsum; 6U23; -.
DR PDBsum; 6U2J; -.
DR PDBsum; 6U2K; -.
DR PDBsum; 6U2L; -.
DR PDBsum; 6U2W; -.
DR AlphaFoldDB; Q2M385; -.
DR SMR; Q2M385; -.
DR BioGRID; 128608; 3.
DR IntAct; Q2M385; 3.
DR STRING; 9606.ENSP00000354335; -.
DR BindingDB; Q2M385; -.
DR ChEMBL; CHEMBL3414409; -.
DR TCDB; 1.C.39.14.1; the membrane attack complex/perforin (macpf) family.
DR GlyGen; Q2M385; 6 sites.
DR iPTMnet; Q2M385; -.
DR PhosphoSitePlus; Q2M385; -.
DR BioMuta; MPEG1; -.
DR DMDM; 121941470; -.
DR jPOST; Q2M385; -.
DR MassIVE; Q2M385; -.
DR MaxQB; Q2M385; -.
DR PaxDb; Q2M385; -.
DR PeptideAtlas; Q2M385; -.
DR PRIDE; Q2M385; -.
DR ProteomicsDB; 61365; -.
DR Antibodypedia; 21299; 94 antibodies from 21 providers.
DR DNASU; 219972; -.
DR Ensembl; ENST00000361050.4; ENSP00000354335.3; ENSG00000197629.6. [Q2M385-1]
DR GeneID; 219972; -.
DR KEGG; hsa:219972; -.
DR MANE-Select; ENST00000361050.4; ENSP00000354335.3; NM_001039396.2; NP_001034485.1.
DR UCSC; uc001nnu.5; human. [Q2M385-1]
DR CTD; 219972; -.
DR DisGeNET; 219972; -.
DR GeneCards; MPEG1; -.
DR HGNC; HGNC:29619; MPEG1.
DR HPA; ENSG00000197629; Tissue enhanced (lymphoid).
DR MalaCards; MPEG1; -.
DR MIM; 610390; gene.
DR MIM; 619223; phenotype.
DR neXtProt; NX_Q2M385; -.
DR OpenTargets; ENSG00000197629; -.
DR PharmGKB; PA164723088; -.
DR VEuPathDB; HostDB:ENSG00000197629; -.
DR eggNOG; ENOG502QRKR; Eukaryota.
DR GeneTree; ENSGT00390000008048; -.
DR HOGENOM; CLU_023578_1_0_1; -.
DR InParanoid; Q2M385; -.
DR OMA; FTRPPLM; -.
DR OrthoDB; 235876at2759; -.
DR PhylomeDB; Q2M385; -.
DR TreeFam; TF331165; -.
DR PathwayCommons; Q2M385; -.
DR SignaLink; Q2M385; -.
DR BioGRID-ORCS; 219972; 6 hits in 1057 CRISPR screens.
DR GenomeRNAi; 219972; -.
DR Pharos; Q2M385; Tchem.
DR PRO; PR:Q2M385; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q2M385; protein.
DR Bgee; ENSG00000197629; Expressed in monocyte and 158 other tissues.
DR Genevisible; Q2M385; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0035915; P:pore formation in membrane of another organism; ISS:UniProtKB.
DR InterPro; IPR020864; MACPF.
DR InterPro; IPR039707; MPEG1.
DR PANTHER; PTHR31463; PTHR31463; 1.
DR Pfam; PF01823; MACPF; 1.
DR SMART; SM00457; MACPF; 1.
DR PROSITE; PS51412; MACPF_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antibiotic; Antimicrobial;
KW Cytoplasmic vesicle; Disease variant; Glycoprotein; Immunity;
KW Innate immunity; Membrane; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..716
FT /note="Macrophage-expressed gene 1 protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000324143"
FT TOPO_DOM 18..655
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 656..676
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 677..716
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..345
FT /note="MACPF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00745"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 73
FT /note="T -> A (in IMD77; unknown pathological significance;
FT decreased defense response to bacterium;
FT dbSNP:rs143527301)"
FT /evidence="ECO:0000269|PubMed:28422754"
FT /id="VAR_085655"
FT VARIANT 316
FT /note="P -> S (decreased defense response to bacterium;
FT dbSNP:rs11229878)"
FT /evidence="ECO:0000269|PubMed:28422754"
FT /id="VAR_085656"
FT VARIANT 398..716
FT /note="Missing (in IMD77; decreased defense response to
FT bacterium)"
FT /evidence="ECO:0000269|PubMed:28422754"
FT /id="VAR_085657"
FT VARIANT 405
FT /note="P -> T (in IMD77; unknown pathological significance;
FT decreased defense response to bacterium;
FT dbSNP:rs200420254)"
FT /evidence="ECO:0000269|PubMed:28422754"
FT /id="VAR_085658"
FT VARIANT 430..716
FT /note="Missing (in IMD77; decreased defense response to
FT bacterium)"
FT /evidence="ECO:0000269|PubMed:33224153"
FT /id="VAR_085659"
FT VARIANT 467
FT /note="A -> T (in dbSNP:rs544864)"
FT /id="VAR_051200"
FT VARIANT 552
FT /note="P -> L (in dbSNP:rs7926933)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_051201"
FT VARIANT 694
FT /note="Q -> R (in dbSNP:rs17153442)"
FT /id="VAR_051202"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:6U2J"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:6U2J"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:6U23"
FT STRAND 84..97
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:6U2J"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:6U2J"
FT TURN 121..129
FT /evidence="ECO:0007829|PDB:6U2J"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 145..161
FT /evidence="ECO:0007829|PDB:6U2J"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:6U2J"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 202..222
FT /evidence="ECO:0007829|PDB:6U2J"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:6U2J"
FT HELIX 233..249
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:6U23"
FT HELIX 261..269
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 270..281
FT /evidence="ECO:0007829|PDB:6U2J"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:6U2J"
FT TURN 295..298
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 301..309
FT /evidence="ECO:0007829|PDB:6U2J"
FT HELIX 310..313
FT /evidence="ECO:0007829|PDB:6U2J"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:6U2J"
FT HELIX 324..343
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:6U2J"
FT TURN 396..400
FT /evidence="ECO:0007829|PDB:6U2J"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:6U2K"
FT STRAND 416..419
FT /evidence="ECO:0007829|PDB:6U2K"
FT STRAND 424..431
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 448..464
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 473..476
FT /evidence="ECO:0007829|PDB:6U2K"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:6U23"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:6U2J"
FT TURN 490..492
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 502..505
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 507..509
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 511..514
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 518..520
FT /evidence="ECO:0007829|PDB:6U23"
FT HELIX 521..524
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:6U23"
FT STRAND 554..556
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 562..565
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 575..578
FT /evidence="ECO:0007829|PDB:6U2J"
FT TURN 582..584
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 608..614
FT /evidence="ECO:0007829|PDB:6U2J"
FT TURN 615..618
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 619..622
FT /evidence="ECO:0007829|PDB:6U2J"
FT TURN 625..627
FT /evidence="ECO:0007829|PDB:6U2J"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:6U2K"
FT HELIX 635..645
FT /evidence="ECO:0007829|PDB:6U2J"
SQ SEQUENCE 716 AA; 78587 MW; C863E3AF2029A0AA CRC64;
MNNFRATILF WAAAAWAKSG KPSGEMDEVG VQKCKNALKL PVLEVLPGGG WDNLRNVDMG
RVMELTYSNC RTTEDGQYII PDEIFTIPQK QSNLEMNSEI LESWANYQSS TSYSINTELS
LFSKVNGKFS TEFQRMKTLQ VKDQAITTRV QVRNLVYTVK INPTLELSSG FRKELLDISD
RLENNQTRMA TYLAELLVLN YGTHVTTSVD AGAALIQEDH LRASFLQDSQ SSRSAVTASA
GLAFQNTVNF KFEENYTSQN VLTKSYLSNR TNSRVQSIGG VPFYPGITLQ AWQQGITNHL
VAIDRSGLPL HFFINPNMLP DLPGPLVKKV SKTVETAVKR YYTFNTYPGC TDLNSPNFNF
QANTDDGSCE GKMTNFSFGG VYQECTQLSG NRDVLLCQKL EQKNPLTGDF SCPSGYSPVH
LLSQIHEEGY NHLECHRKCT LLVFCKTVCE DVFQVAKAEF RAFWCVASSQ VPENSGLLFG
GLFSSKSINP MTNAQSCPAG YFPLRLFENL KVCVSQDYEL GSRFAVPFGG FFSCTVGNPL
VDPAISRDLG APSLKKCPGG FSQHPALISD GCQVSYCVKS GLFTGGSLPP ARLPPFTRPP
LMSQAATNTV IVTNSENARS WIKDSQTHQW RLGEPIELRR AMNVIHGDGG GLSGGAAAGV
TVGVTTILAV VITLAIYGTR KFKKKAYQAI EERQSLVPGT AATGDTTYQE QGQSPA
