PGPSA_DROME
ID PGPSA_DROME Reviewed; 203 AA.
AC Q9VYX7;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Peptidoglycan-recognition protein SA;
DE EC=3.4.17.13 {ECO:0000269|PubMed:15361936};
DE AltName: Full=Protein semmelweis;
DE Flags: Precursor;
GN Name=PGRP-SA; Synonyms=seml; ORFNames=CG11709;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP PGN-BINDING, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11106397; DOI=10.1073/pnas.97.25.13772;
RA Werner T., Liu G., Kang D., Ekengren S., Steiner H., Hultmark D.;
RT "A family of peptidoglycan recognition proteins in the fruit fly Drosophila
RT melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:13772-13777(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DI7, Draveil, KY024, KY038, Loua, Monty5, P.bourg, S30, Tahiti,
RC Texas, and ZW141;
RX PubMed=14738318; DOI=10.1007/s00239-003-2506-6;
RA Jiggins F.M., Hurst G.D.D.;
RT "The evolution of parasite recognition genes in the innate immune system:
RT purifying selection on Drosophila melanogaster peptidoglycan recognition
RT proteins.";
RL J. Mol. Evol. 57:598-605(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-80.
RX PubMed=11742401; DOI=10.1038/414756a;
RA Michel T., Reichhart J.-M., Hoffmann J.A., Royet J.;
RT "Drosophila Toll is activated by Gram-positive bacteria through a
RT circulating peptidoglycan recognition protein.";
RL Nature 414:756-759(2001).
RN [7]
RP INDUCTION.
RX PubMed=12032070; DOI=10.1093/emboj/21.11.2568;
RA De Gregorio E., Spellman P.T., Tzou P., Rubin G.M., Lemaitre B.;
RT "The Toll and Imd pathways are the major regulators of the immune response
RT in Drosophila.";
RL EMBO J. 21:2568-2579(2002).
RN [8]
RP FUNCTION.
RX PubMed=14684822; DOI=10.1126/science.1085432;
RA Gobert V., Gottar M., Matskevich A.A., Rutschmann S., Royet J., Belvin M.,
RA Hoffmann J.A., Ferrandon D.;
RT "Dual activation of the Drosophila toll pathway by two pattern recognition
RT receptors.";
RL Science 302:2126-2130(2003).
RN [9]
RP FUNCTION.
RX PubMed=14722090; DOI=10.1074/jbc.m313324200;
RA Pili-Floury S., Leulier F., Takahashi K., Saigo K., Samain E., Ueda R.,
RA Lemaitre B.;
RT "In vivo RNA interference analysis reveals an unexpected role for GNBP1 in
RT the defense against Gram-positive bacterial infection in Drosophila
RT adults.";
RL J. Biol. Chem. 279:12848-12853(2004).
RN [10]
RP FUNCTION.
RX PubMed=15448690; DOI=10.1038/ni1123;
RA Bischoff V., Vignal C., Boneca I.G., Michel T., Hoffmann J.A., Royet J.;
RT "Function of the Drosophila pattern-recognition receptor PGRP-SD in the
RT detection of Gram-positive bacteria.";
RL Nat. Immunol. 5:1175-1180(2004).
RN [11]
RP FUNCTION.
RX PubMed=16399077; DOI=10.1016/j.devcel.2005.11.013;
RA Jang I.H., Chosa N., Kim S.H., Nam H.J., Lemaitre B., Ochiai M.,
RA Kambris Z., Brun S., Hashimoto C., Ashida M., Brey P.T., Lee W.J.;
RT "A Spatzle-processing enzyme required for toll signaling activation in
RT Drosophila innate immunity.";
RL Dev. Cell 10:45-55(2006).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 27-203, AND DISULFIDE BONDS.
RX PubMed=15223330; DOI=10.1016/j.jmb.2004.04.077;
RA Reiser J.-B., Teyton L., Wilson I.A.;
RT "Crystal structure of the Drosophila peptidoglycan recognition protein
RT (PGRP)-SA at 1.56 A resolution.";
RL J. Mol. Biol. 340:909-917(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP DISULFIDE BONDS, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-37;
RP HIS-68; 70-VAL-THR-71; CYS-74; 96-ASP--ASN-98; 90-TYR-HIS-91; SER-101;
RP TYR-126; ILE-180; THR-182 AND SER-184.
RX PubMed=15361936; DOI=10.1371/journal.pbio.0020277;
RA Chang C.-I., Pili-Floury S., Herve M., Parquet C., Chelliah Y.,
RA Lemaitre B., Mengin-Lecreulx D., Deisenhofer J.;
RT "A Drosophila pattern recognition receptor contains a peptidoglycan docking
RT groove and unusual L,D-carboxypeptidase activity.";
RL PLoS Biol. 2:1293-1302(2004).
CC -!- FUNCTION: Peptidoglycan-recognition protein that plays a key role in
CC innate immunity by binding to peptidoglycans (PGN) of Gram-positive
CC bacteria and activating the Toll pathway upstream of spz activating
CC enzyme SPE (PubMed:11106397, PubMed:16399077, PubMed:15448690). Has no
CC activity against Gram-negative bacteria and fungi (PubMed:11742401).
CC Shows some partial redundancy with PRPGP-SD in Gram-positive bacteria
CC recognition (PubMed:11742401, PubMed:15448690). May act by forming a
CC complex with GNBP1 that activates the proteolytic cleavage of Spatzle
CC and the subsequent activation of Toll pathway (PubMed:14684822,
CC PubMed:14722090, PubMed:11742401). Binds to diaminopimelic acid-type
CC tetrapeptide PGN (DAP-type PGN) and lysine-type PGN (Lys-type PGN)
CC (PubMed:15361936). Has some L,D-carboxypeptidase activity for DAP-type
CC PGN, which are specific to prokaryotes, but not for Lys-type PGN
CC (PubMed:15361936). {ECO:0000269|PubMed:11742401,
CC ECO:0000269|PubMed:14684822, ECO:0000269|PubMed:14722090,
CC ECO:0000269|PubMed:15361936, ECO:0000269|PubMed:15448690,
CC ECO:0000269|PubMed:16399077}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-
CC glutamyl-6-carboxy-L-lysyl-D-alanine = D-alanine + N-acetyl-D-
CC glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl;
CC Xref=Rhea:RHEA:48688, ChEBI:CHEBI:15377, ChEBI:CHEBI:57416,
CC ChEBI:CHEBI:90762, ChEBI:CHEBI:90763; EC=3.4.17.13;
CC Evidence={ECO:0000269|PubMed:15361936};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21.4 uM for GlcNAc-MurNAc(anhydro)-L-Ala-gamma-D-Glu-meso-DAP-D-
CC Ala {ECO:0000269|PubMed:15361936};
CC -!- INTERACTION:
CC Q9VYX7; Q9NHB0: GNBP1; NbExp=4; IntAct=EBI-15721239, EBI-15721168;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11742401}.
CC Note=Secreted in hemolymph.
CC -!- TISSUE SPECIFICITY: In larvae, it is expressed in fat body. Also
CC expressed in uninduced hemocytes and mbn-2 cells.
CC {ECO:0000269|PubMed:11106397, ECO:0000269|PubMed:11742401}.
CC -!- INDUCTION: Strongly up-regulated by PGN from B.subtilis. Regulated by
CC both imd/Relish and Toll pathways. {ECO:0000269|PubMed:11106397,
CC ECO:0000269|PubMed:12032070}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000305}.
CC -!- CAUTION: Although suggested, the interaction with GNBP1 has not been
CC experimentally demonstrated. {ECO:0000305|PubMed:14684822}.
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DR EMBL; AF207540; AAG23734.1; -; Genomic_DNA.
DR EMBL; AF207541; AAG23735.1; -; mRNA.
DR EMBL; AJ556551; CAD89116.1; -; Genomic_DNA.
DR EMBL; AJ556552; CAD89117.1; -; Genomic_DNA.
DR EMBL; AJ556553; CAD89118.1; -; Genomic_DNA.
DR EMBL; AJ556554; CAD89119.1; -; Genomic_DNA.
DR EMBL; AJ556555; CAD89120.1; -; Genomic_DNA.
DR EMBL; AJ556556; CAD89121.1; -; Genomic_DNA.
DR EMBL; AJ556557; CAD89122.1; -; Genomic_DNA.
DR EMBL; AJ556558; CAD89123.1; -; Genomic_DNA.
DR EMBL; AJ556559; CAD89124.1; -; Genomic_DNA.
DR EMBL; AJ556560; CAD89125.1; -; Genomic_DNA.
DR EMBL; AJ556561; CAD89126.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48056.1; -; Genomic_DNA.
DR EMBL; AY075293; AAL68160.1; -; mRNA.
DR RefSeq; NP_001285128.1; NM_001298199.1.
DR RefSeq; NP_572727.1; NM_132499.3.
DR PDB; 1S2J; X-ray; 2.20 A; A/B=1-203.
DR PDB; 1SXR; X-ray; 1.56 A; A/B=27-203.
DR PDBsum; 1S2J; -.
DR PDBsum; 1SXR; -.
DR AlphaFoldDB; Q9VYX7; -.
DR SMR; Q9VYX7; -.
DR BioGRID; 58509; 2.
DR DIP; DIP-60775N; -.
DR IntAct; Q9VYX7; 7.
DR STRING; 7227.FBpp0073358; -.
DR PaxDb; Q9VYX7; -.
DR DNASU; 32099; -.
DR EnsemblMetazoa; FBtr0073509; FBpp0073358; FBgn0030310.
DR EnsemblMetazoa; FBtr0340296; FBpp0309257; FBgn0030310.
DR GeneID; 32099; -.
DR KEGG; dme:Dmel_CG11709; -.
DR CTD; 32099; -.
DR FlyBase; FBgn0030310; PGRP-SA.
DR VEuPathDB; VectorBase:FBgn0030310; -.
DR eggNOG; ENOG502S2KY; Eukaryota.
DR HOGENOM; CLU_037559_3_0_1; -.
DR InParanoid; Q9VYX7; -.
DR OMA; RFVVIHH; -.
DR OrthoDB; 1110472at2759; -.
DR PhylomeDB; Q9VYX7; -.
DR Reactome; R-DME-6803157; Antimicrobial peptides.
DR BioGRID-ORCS; 32099; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; Q9VYX7; -.
DR GenomeRNAi; 32099; -.
DR PRO; PR:Q9VYX7; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030310; Expressed in seminal fluid secreting gland and 22 other tissues.
DR ExpressionAtlas; Q9VYX7; baseline and differential.
DR Genevisible; Q9VYX7; DM.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0106415; F:muramoyltetrapeptide carboxypeptidase activity; IDA:FlyBase.
DR GO; GO:0032500; F:muramyl dipeptide binding; IDA:FlyBase.
DR GO; GO:0038187; F:pattern recognition receptor activity; IMP:FlyBase.
DR GO; GO:0042834; F:peptidoglycan binding; IDA:FlyBase.
DR GO; GO:0016019; F:peptidoglycan immune receptor activity; TAS:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; NAS:UniProtKB.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR GO; GO:0006965; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-positive bacteria; IMP:UniProtKB.
DR GO; GO:0045752; P:positive regulation of Toll signaling pathway; IMP:FlyBase.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0032494; P:response to peptidoglycan; IMP:FlyBase.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; -; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR017331; Peptidoglycan_recognition.
DR InterPro; IPR015510; PGRP.
DR InterPro; IPR006619; PGRP_domain_met/bac.
DR PANTHER; PTHR11022; PTHR11022; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR PIRSF; PIRSF037945; PGRPs; 1.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; SSF55846; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Immunity; Innate immunity; Protease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:11106397"
FT CHAIN 27..203
FT /note="Peptidoglycan-recognition protein SA"
FT /id="PRO_0000023906"
FT DOMAIN 59..186
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT REGION 87..90
FT /note="Peptidoglycan binding"
FT /evidence="ECO:0000305"
FT REGION 97..102
FT /note="Peptidoglycan binding"
FT /evidence="ECO:0000305"
FT SITE 182
FT /note="Interacts with peptidoglycan"
FT /evidence="ECO:0000305"
FT DISULFID 37..160
FT DISULFID 74..80
FT MUTAGEN 37
FT /note="C->A: Does not affect activation of Toll pathway."
FT /evidence="ECO:0000269|PubMed:15361936"
FT MUTAGEN 68
FT /note="H->A: Abolishes L,D-carboxypeptidase activity on
FT DAP-type PGN."
FT /evidence="ECO:0000269|PubMed:15361936"
FT MUTAGEN 70..71
FT /note="VT->AA: Strongly reduces PGN-binding and activation
FT of Toll pathway."
FT /evidence="ECO:0000269|PubMed:15361936"
FT MUTAGEN 74
FT /note="C->A: Abolishes activation of Toll pathway."
FT /evidence="ECO:0000269|PubMed:15361936"
FT MUTAGEN 80
FT /note="C->Y: In seml; induces susceptibility to Gram-
FT positive bacterial infection."
FT /evidence="ECO:0000269|PubMed:11742401"
FT MUTAGEN 90..91
FT /note="YH->AA: Strongly reduces PGN-binding and activation
FT of Toll pathway."
FT /evidence="ECO:0000269|PubMed:15361936"
FT MUTAGEN 96..98
FT /note="DFN->AAA: Strongly reduces PGN-binding and
FT activation of Toll pathway."
FT /evidence="ECO:0000269|PubMed:15361936"
FT MUTAGEN 101
FT /note="S->A: Increases PGN-binding and activation of Toll
FT pathway."
FT /evidence="ECO:0000269|PubMed:15361936"
FT MUTAGEN 126
FT /note="Y->A: Strongly reduces PGN-binding and activation of
FT Toll pathway."
FT /evidence="ECO:0000269|PubMed:15361936"
FT MUTAGEN 180
FT /note="I->A: Strongly reduces PGN-binding."
FT /evidence="ECO:0000269|PubMed:15361936"
FT MUTAGEN 182
FT /note="T->Y: Abolishes PGN-binding and activation of Toll
FT pathway."
FT /evidence="ECO:0000269|PubMed:15361936"
FT MUTAGEN 184
FT /note="S->A,C: Abolishes PGN-binding and activation of Toll
FT pathway. Abolishes L,D-carboxypeptidase activity on DAP-
FT type PGN."
FT /evidence="ECO:0000269|PubMed:15361936"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:1SXR"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:1SXR"
FT HELIX 76..93
FT /evidence="ECO:0007829|PDB:1SXR"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:1SXR"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:1SXR"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1SXR"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:1SXR"
FT STRAND 132..139
FT /evidence="ECO:0007829|PDB:1SXR"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1SXR"
FT HELIX 148..163
FT /evidence="ECO:0007829|PDB:1SXR"
FT STRAND 166..175
FT /evidence="ECO:0007829|PDB:1SXR"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1SXR"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1S2J"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:1SXR"
SQ SEQUENCE 203 AA; 22260 MW; D200A6EA79C66731 CRC64;
MQPVRFGSPW IMAIGLVLLL LAFVSAGKSR QRSPANCPTI KLKRQWGGKP SLGLHYQVRP
IRYVVIHHTV TGECSGLLKC AEILQNMQAY HQNELDFNDI SYNFLIGNDG IVYEGTGWGL
RGAHTYGYNA IGTGIAFIGN FVDKLPSDAA LQAAKDLLAC GVQQGELSED YALIAGSQVI
STQSPGLTLY NEIQEWPHWL SNP
