ISG15_MOUSE
ID ISG15_MOUSE Reviewed; 161 AA.
AC Q64339; Q8K0H3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Ubiquitin-like protein ISG15;
DE AltName: Full=Interferon-induced 15 kDa protein;
DE AltName: Full=Interferon-induced 17 kDa protein;
DE Short=IP17;
DE AltName: Full=Ubiquitin cross-reactive protein;
DE Flags: Precursor;
GN Name=Isg15; Synonyms=G1p2, Ucrp;
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].
RC STRAIN=BALB/cJ;
RA Fahey D.;
RT "Nucleotide sequence and deduced amino acid sequence of a cDNA encoding an
RT interferon-induced mouse 15-KDa protein.";
RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Garlie N.K., Haas A.L., D'Cunha J., Schilling D., Knight E. Jr.,
RA Borden E.C.;
RT "Sequence differences between murine ISG15, human ISG15 and ubiquitin: a
RT functional divergence from ubiquitin.";
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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 PROTEIN SEQUENCE OF 9-30; 36-44 AND 89-106, AND CONJUGATION TO SERPINA3G.
RX PubMed=11859133; DOI=10.4049/jimmunol.168.5.2415;
RA Hamerman J.A., Hayashi F., Schroeder L.A., Gygi S.P., Haas A.L.,
RA Hampson L., Coughlin P., Aebersold R., Aderem A.;
RT "Serpin 2a is induced in activated macrophages and conjugates to a
RT ubiquitin homolog.";
RL J. Immunol. 168:2415-2423(2002).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, CHEMOTACTIC ACTIVITY, AND MASS SPECTROMETRY.
RX PubMed=12963022; DOI=10.1016/j.bbrc.2003.08.038;
RA Owhashi M., Taoka Y., Ishii K., Nakazawa S., Uemura H., Kambara H.;
RT "Identification of a ubiquitin family protein as a novel neutrophil
RT chemotactic factor.";
RL Biochem. Biophys. Res. Commun. 309:533-539(2003).
RN [6]
RP CONJUGATION TO JAK1; MAPK3 AND PLCG1.
RX PubMed=12582176; DOI=10.1074/jbc.m208435200;
RA Malakhov M.P., Kim K.I., Malakhova O.A., Jacobs B.S., Borden E.C.,
RA Zhang D.-E.;
RT "High-throughput immunoblotting. Ubiquitin-like protein ISG15 modifies key
RT regulators of signal transduction.";
RL J. Biol. Chem. 278:16608-16613(2003).
RN [7]
RP FUNCTION IN SINDBIS VIRUS RESTRICTION.
RX PubMed=16254333; DOI=10.1128/jvi.79.22.13974-13983.2005;
RA Lenschow D.J., Giannakopoulos N.V., Gunn L.J., Johnston C., O'Guin A.K.,
RA Schmidt R.E., Levine B., Virgin H.W. IV;
RT "Identification of interferon-stimulated gene 15 as an antiviral molecule
RT during Sindbis virus infection in vivo.";
RL J. Virol. 79:13974-13983(2005).
RN [8]
RP FUNCTION IN TRIM25 ISGYLATION.
RX PubMed=17222803; DOI=10.1016/j.bbrc.2006.12.210;
RA Zou W., Wang J., Zhang D.-E.;
RT "Negative regulation of ISG15 E3 ligase EFP through its autoISGylation.";
RL Biochem. Biophys. Res. Commun. 354:321-327(2007).
RN [9]
RP FUNCTION IN EIF4E2 ISGYLATION.
RX PubMed=17289916; DOI=10.1101/gad.1521607;
RA Okumura F., Zou W., Zhang D.E.;
RT "ISG15 modification of the eIF4E cognate 4EHP enhances cap structure-
RT binding activity of 4EHP.";
RL Genes Dev. 21:255-260(2007).
RN [10]
RP FUNCTION IN HHV-1; SV; INFLUENZA A AND B VIRUS RESTRICTION.
RX PubMed=17227866; DOI=10.1073/pnas.0607038104;
RA Lenschow D.J., Lai C., Frias-Staheli N., Giannakopoulos N.V., Lutz A.,
RA Wolff T., Osiak A., Levine B., Schmidt R.E., Garcia-Sastre A., Leib D.A.,
RA Pekosz A., Knobeloch K.P., Horak I., Virgin H.W. IV;
RT "IFN-stimulated gene 15 functions as a critical antiviral molecule against
RT influenza, herpes, and Sindbis viruses.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1371-1376(2007).
RN [11]
RP SUBUNIT, AND S-NITROSYLATION AT CYS-76 AND CYS-144.
RX PubMed=18606809; DOI=10.1074/jbc.m803795200;
RA Okumura F., Lenschow D.J., Zhang D.E.;
RT "Nitrosylation of ISG15 prevents the disulfide bond-mediated dimerization
RT of ISG15 and contributes to effective ISGylation.";
RL J. Biol. Chem. 283:24484-24488(2008).
RN [12]
RP FUNCTION IN DDX58 ISGYLATION.
RX PubMed=18057259; DOI=10.1128/jvi.01650-07;
RA Kim M.J., Hwang S.Y., Imaizumi T., Yoo J.Y.;
RT "Negative feedback regulation of RIG-I-mediated antiviral signaling by
RT interferon-induced ISG15 conjugation.";
RL J. Virol. 82:1474-1483(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP REVIEW.
RX PubMed=20946978; DOI=10.1016/j.cell.2010.09.033;
RA Skaug B., Chen Z.J.;
RT "Emerging role of ISG15 in antiviral immunity.";
RL Cell 143:187-190(2010).
RN [15]
RP FUNCTION IN STAT5A; MAPK1; PLC-GAMMA AND GLOBIN ISGYLATION.
RX PubMed=22022510; DOI=10.1371/journal.pone.0026068;
RA Maragno A.L., Pironin M., Alcalde H., Cong X., Knobeloch K.P., Tangy F.,
RA Zhang D.E., Ghysdael J., Quang C.T.;
RT "ISG15 modulates development of the erythroid lineage.";
RL PLoS ONE 6:E26068-E26068(2011).
RN [16]
RP FUNCTION.
RX PubMed=22028657; DOI=10.1371/journal.ppat.1002322;
RA Werneke S.W., Schilte C., Rohatgi A., Monte K.J., Michault A.,
RA Arenzana-Seisdedos F., Vanlandingham D.L., Higgs S., Fontanet A.,
RA Albert M.L., Lenschow D.J.;
RT "ISG15 is critical in the control of Chikungunya virus infection
RT independent of UbE1L mediated conjugation.";
RL PLoS Pathog. 7:E1002322-E1002322(2011).
RN [17]
RP FUNCTION.
RX PubMed=22859821; DOI=10.1126/science.1224026;
RA Bogunovic D., Byun M., Durfee L.A., Abhyankar A., Sanal O., Mansouri D.,
RA Salem S., Radovanovic I., Grant A.V., Adimi P., Mansouri N., Okada S.,
RA Bryant V.L., Kong X.F., Kreins A., Velez M.M., Boisson B., Khalilzadeh S.,
RA Ozcelik U., Darazam I.A., Schoggins J.W., Rice C.M., Al-Muhsen S., Behr M.,
RA Vogt G., Puel A., Bustamante J., Gros P., Huibregtse J.M., Abel L.,
RA Boisson-Dupuis S., Casanova J.L.;
RT "Mycobacterial disease and impaired IFN-gamma immunity in humans with
RT inherited ISG15 deficiency.";
RL Science 337:1684-1688(2012).
RN [18] {ECO:0007744|PDB:6YVA}
RP X-RAY CRYSTALLOGRAPHY (3.18 ANGSTROMS) OF 1-156 IN COMPLEX WITH SARS-COV-2
RP NON-STRUCTURAL PROTEIN 3, AND FUNCTION.
RX PubMed=32726803; DOI=10.1038/s41586-020-2601-5;
RA Shin D., Mukherjee R., Grewe D., Bojkova D., Baek K., Bhattacharya A.,
RA Schulz L., Widera M., Mehdipour A.R., Tascher G., Geurink P.P., Wilhelm A.,
RA van der Heden van Noort G.J., Ovaa H., Mueller S., Knobeloch K.P.,
RA Rajalingam K., Schulman B.A., Cinatl J., Hummer G., Ciesek S., Dikic I.;
RT "Papain-like protease regulates SARS-CoV-2 viral spread and innate
RT immunity.";
RL Nature 587:657-662(2020).
CC -!- FUNCTION: Ubiquitin-like protein which plays a key role in the innate
CC immune response to viral infection either via its conjugation to a
CC target protein (ISGylation) or via its action as a free or unconjugated
CC protein. ISGylation involves a cascade of enzymatic reactions involving
CC E1, E2, and E3 enzymes which catalyze the conjugation of ISG15 to a
CC lysine residue in the target protein. Its target proteins include
CC SERPINA3G/SPI2A, JAK1, MAPK3/ERK1, PLCG1, TRIM25, STAT5A, MAPK1/ERK2
CC and globin. Isgylation of the viral sensor IFIH1/MDA5 promotes
CC IFIH1/MDA5 oligomerization and triggers activation of innate immunity
CC against a range of viruses, including coronaviruses, flaviviruses and
CC picornaviruses. Can also isgylate: DDX58/RIG-I which inhibits its
CC function in antiviral signaling response, IRF3 which inhibits its
CC ubiquitination and degradation as well as EIF4E2 which enhances its cap
CC structure-binding activity and translation-inhibition activity.
CC Exhibits antiviral activity towards both DNA and RNA viruses, including
CC influenza A and B virus, sindbis virus (SV) and herpes simplex type-1
CC (HHV-1). Plays a significant role in the control of neonatal
CC Chikungunya virus (CHIKV) infection by acting as a putative
CC immunomodulator of pro-inflammatory cytokines. Protects mice against
CC the consequences of Chikungunya virus infection by down-regulating the
CC pathogenic cytokine response, often denoted as the cytokine storm.
CC Plays a role in erythroid differentiation. The secreted form of ISG15
CC can: induce natural killer cell proliferation, act as a chemotactic
CC factor for neutrophils and act as a IFN-gamma-inducing cytokine playing
CC an essential role in antimycobacterial immunity. The secreted form acts
CC through the integrin ITGAL/ITGB2 receptor to initiate activation of SRC
CC family tyrosine kinases including LYN, HCK and FGR which leads to
CC secretion of IFNG and IL10; the interaction is mediated by ITGAL (By
CC similarity). {ECO:0000250|UniProtKB:P05161,
CC ECO:0000269|PubMed:16254333, ECO:0000269|PubMed:17222803,
CC ECO:0000269|PubMed:17227866, ECO:0000269|PubMed:17289916,
CC ECO:0000269|PubMed:18057259, ECO:0000269|PubMed:22022510,
CC ECO:0000269|PubMed:22028657, ECO:0000269|PubMed:22859821,
CC ECO:0000269|PubMed:32726803}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts with,
CC and is conjugated to its targets by the UBE1L (E1 enzyme) and UBE2E2
CC (E2 enzyme) (By similarity). Interacts with NEDD4 (By similarity).
CC {ECO:0000250|UniProtKB:P05161}.
CC -!- INTERACTION:
CC Q64339; Q9WTV6: Usp18; NbExp=4; IntAct=EBI-8345781, EBI-9119995;
CC Q64339; PRO_0000422456 [K9N638]: 1a; Xeno; NbExp=2; IntAct=EBI-8345781, EBI-25635184;
CC Q64339; PRO_0000338257 [P0C6U8]: 1a; Xeno; NbExp=3; IntAct=EBI-8345781, EBI-25635190;
CC Q64339; PRO_0000037311 [P0C6X7]: rep; Xeno; NbExp=4; IntAct=EBI-8345781, EBI-25474079;
CC Q64339; PRO_0000449621 [P0DTD1]: rep; Xeno; NbExp=5; IntAct=EBI-8345781, EBI-25492388;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P05161}.
CC Secreted {ECO:0000250|UniProtKB:P05161}. Note=Exists in three distinct
CC states: free within the cell, released into the extracellular space, or
CC conjugated to target proteins. {ECO:0000250|UniProtKB:P05161}.
CC -!- INDUCTION: By type I interferons.
CC -!- DOMAIN: Both the Ubiquitin-like 1 and Ubiquitin-like 2 domains are
CC required for its efficient conjugation to cellular proteins. The two
CC domains play different roles in the ISGylation pathway: Ubiquitin-like
CC 2 domain is necessary for the first two steps allowing the linking of
CC ISG15 to the E1 and E2 enzymes while Ubiquitin-like 1 domain is
CC essential for the final, E3-mediated transfer of ISG15, from the E2 to
CC the Lys of the target protein. {ECO:0000250|UniProtKB:P05161}.
CC -!- PTM: S-nitrosylation decreases its dimerization, thereby increasing the
CC availability as well as the solubility of monomeric ISG15 for its
CC conjugation to cellular proteins. {ECO:0000269|PubMed:18606809}.
CC -!- PTM: Induced as an inactive, precursor protein that is cleaved by
CC specific proteases to expose the C-terminal diglycine (LRLRGG) motif.
CC This motif is essential not only for its conjugation to substrates but
CC also for its recognition by the relevant processing proteases (By
CC similarity). {ECO:0000250|UniProtKB:P05161}.
CC -!- MASS SPECTROMETRY: Mass=17015; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:12963022};
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DR EMBL; X56602; CAA39939.1; -; mRNA.
DR EMBL; U58202; AAB02697.1; -; Genomic_DNA.
DR EMBL; BC031424; AAH31424.1; -; mRNA.
DR EMBL; BC083156; AAH83156.1; -; mRNA.
DR CCDS; CCDS51405.1; -.
DR PIR; S26434; S26434.
DR RefSeq; NP_056598.2; NM_015783.3.
DR PDB; 5CHF; X-ray; 2.30 A; A/B/C/D/E=1-155.
DR PDB; 5CHV; X-ray; 3.00 A; C/D=1-155.
DR PDB; 5CHW; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=1-155.
DR PDB; 5JZE; X-ray; 2.47 A; B/D=79-154.
DR PDB; 5TL7; X-ray; 2.44 A; A/C=78-155.
DR PDB; 5TLA; X-ray; 3.24 A; A/B/C/D/E/F/G/H/I/J=1-150.
DR PDB; 6J62; X-ray; 2.49 A; A=1-153.
DR PDB; 6YVA; X-ray; 3.18 A; C=1-161.
DR PDBsum; 5CHF; -.
DR PDBsum; 5CHV; -.
DR PDBsum; 5CHW; -.
DR PDBsum; 5JZE; -.
DR PDBsum; 5TL7; -.
DR PDBsum; 5TLA; -.
DR PDBsum; 6J62; -.
DR PDBsum; 6YVA; -.
DR AlphaFoldDB; Q64339; -.
DR SMR; Q64339; -.
DR BioGRID; 782389; 37.
DR IntAct; Q64339; 8.
DR MINT; Q64339; -.
DR STRING; 10090.ENSMUSP00000082548; -.
DR iPTMnet; Q64339; -.
DR PhosphoSitePlus; Q64339; -.
DR SwissPalm; Q64339; -.
DR CPTAC; non-CPTAC-3583; -.
DR EPD; Q64339; -.
DR MaxQB; Q64339; -.
DR PaxDb; Q64339; -.
DR PRIDE; Q64339; -.
DR ProteomicsDB; 269337; -.
DR Antibodypedia; 809; 575 antibodies from 40 providers.
DR Ensembl; ENSMUST00000085425; ENSMUSP00000082548; ENSMUSG00000035692.
DR GeneID; 100038882; -.
DR KEGG; mmu:100038882; -.
DR UCSC; uc012dri.1; mouse.
DR CTD; 9636; -.
DR MGI; MGI:1855694; Isg15.
DR VEuPathDB; HostDB:ENSMUSG00000035692; -.
DR eggNOG; KOG0001; Eukaryota.
DR GeneTree; ENSGT00940000162007; -.
DR HOGENOM; CLU_010412_4_2_1; -.
DR InParanoid; Q64339; -.
DR OMA; QCTVFMN; -.
DR OrthoDB; 1367357at2759; -.
DR PhylomeDB; Q64339; -.
DR TreeFam; TF338379; -.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
DR Reactome; R-MMU-5656169; Termination of translesion DNA synthesis.
DR BioGRID-ORCS; 100038882; 1 hit in 75 CRISPR screens.
DR PRO; PR:Q64339; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q64339; protein.
DR Bgee; ENSMUSG00000035692; Expressed in bone marrow and 67 other tissues.
DR ExpressionAtlas; Q64339; baseline and differential.
DR Genevisible; Q64339; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0031386; F:protein tag; IDA:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0032020; P:ISG15-protein conjugation; IDA:UniProtKB.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IDA:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; ISO:MGI.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISS:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISS:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; ISS:UniProtKB.
DR GO; GO:0032461; P:positive regulation of protein oligomerization; ISS:UniProtKB.
DR GO; GO:0070585; P:protein localization to mitochondrion; ISS:UniProtKB.
DR GO; GO:0032649; P:regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR GO; GO:0034340; P:response to type I interferon; ISS:UniProtKB.
DR GO; GO:0009615; P:response to virus; ISS:UniProtKB.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00240; ubiquitin; 2.
DR SMART; SM00213; UBQ; 2.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Isopeptide bond; Reference proteome; Repeat;
KW S-nitrosylation; Secreted; Ubl conjugation pathway.
FT CHAIN 1..155
FT /note="Ubiquitin-like protein ISG15"
FT /id="PRO_0000035988"
FT PROPEP 156..161
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000035989"
FT DOMAIN 2..76
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 77..155
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 151..155
FT /note="Involved in the ligation of specific target
FT proteins"
FT /evidence="ECO:0000250"
FT MOTIF 150..155
FT /note="LRLRGG"
FT /evidence="ECO:0000250"
FT SITE 151
FT /note="Interacts with activating enzyme"
FT /evidence="ECO:0000250"
FT MOD_RES 76
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:18606809"
FT MOD_RES 144
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:18606809"
FT CROSSLNK 155
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CONFLICT 111..115
FT /note="QREQV -> SGTS (in Ref. 1; CAA39939 and 2; AAB02697)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:5CHW"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:6YVA"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:5CHW"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:5CHW"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:5CHW"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:5CHW"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5CHW"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:5CHW"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:5CHW"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5TL7"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:5CHW"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:5CHW"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:5CHW"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:5CHW"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:6J62"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:5TLA"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:5CHW"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:5CHW"
SQ SEQUENCE 161 AA; 17898 MW; 9C70D9A507979171 CRC64;
MAWDLKVKML GGNDFLVSVT NSMTVSELKK QIAQKIGVPA FQQRLAHQTA VLQDGLTLSS
LGLGPSSTVM LVVQNCSEPL SILVRNERGH SNIYEVFLTQ TVDTLKKKVS QREQVHEDQF
WLSFEGRPME DKELLGEYGL KPQCTVIKHL RLRGGGGDQC A
