PGPLC_DROME
ID PGPLC_DROME Reviewed; 520 AA.
AC Q9GNK5; Q1EBX6; Q7YW58; Q8T5Q2; Q9VSV9;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Peptidoglycan-recognition protein LC;
DE AltName: Full=Immune response deficient 7 protein;
GN Name=PGRP-LC; Synonyms=ird7, PGRPLC; ORFNames=CG4432;
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 {ECO:0000312|EMBL:AAG23733.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; X AND Y), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Berkeley {ECO:0000269|PubMed:11106397}, and
RC Canton-S {ECO:0000269|PubMed:11106397};
RC TISSUE=Embryo {ECO:0000269|PubMed:11106397},
RC Head {ECO:0000269|PubMed:11106397}, Larva {ECO:0000269|PubMed:11106397},
RC and Pupae {ECO:0000269|PubMed:11106397};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM X), FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Berkeley {ECO:0000269|PubMed:11872802};
RC TISSUE=Larva {ECO:0000269|PubMed:11872802}, and
RC Pupae {ECO:0000269|PubMed:11872802};
RX PubMed=11872802; DOI=10.1126/science.1070216;
RA Choe K.-M., Werner T., Stoeven S., Hultmark D., Anderson K.V.;
RT "Requirement for a peptidoglycan recognition protein (PGRP) in Relish
RT activation and antibacterial immune responses in Drosophila.";
RL Science 296:359-362(2002).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM Y), AND FUNCTION (ISOFORMS A; X AND Y).
RC STRAIN=Canton-S {ECO:0000312|EMBL:AAQ16306.1};
RX PubMed=12777387; DOI=10.1074/jbc.c300184200;
RA Werner T., Borge-Renberg K., Mellroth P., Steiner H., Hultmark D.;
RT "Functional diversity of the Drosophila PGRP-LC gene cluster in the
RT response to lipopolysaccharide and peptidoglycan.";
RL J. Biol. Chem. 278:26319-26322(2003).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [5] {ECO:0000305}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [6] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM X).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Larva {ECO:0000269|PubMed:12537569}, and
RC Pupae {ECO:0000269|PubMed:12537569};
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM X).
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22022271; DOI=10.1371/journal.ppat.1002319;
RA Akhouayri I., Turc C., Royet J., Charroux B.;
RT "Toll-8/Tollo negatively regulates antimicrobial response in the Drosophila
RT respiratory epithelium.";
RL PLoS Pathog. 7:E1002319-E1002319(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 355-520, DISULFIDE BOND, AND
RP FUNCTION (ISOFORMS A AND X).
RX PubMed=16006509; DOI=10.1073/pnas.0504547102;
RA Chang C.-I., Ihara K., Chelliah Y., Mengin-Lecreulx D., Wakatsuki S.,
RA Deisenhofer J.;
RT "Structure of the ectodomain of Drosophila peptidoglycan-recognition
RT protein LCa suggests a molecular mechanism for pattern recognition.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:10279-10284(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 355-520 IN COMPLEX WITH
RP PEPTIDOGLYCAN FRAGMENT, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-389 AND
RP ASN-515.
RX PubMed=16556841; DOI=10.1126/science.1123056;
RA Chang C.-I., Chelliah Y., Borek D., Mengin-Lecreulx D., Deisenhofer J.;
RT "Structure of tracheal cytotoxin in complex with a heterodimeric pattern-
RT recognition receptor.";
RL Science 311:1761-1764(2006).
CC -!- FUNCTION: Major activator of the imd/Relish pathway and is likely to
CC encode a pattern recognition molecule for the humoral immune response
CC (PubMed:11872802, PubMed:22022271). Required for Relish processing and
CC nuclear translocation following proteolytic cleavage (PubMed:11872802).
CC Involved in the response to lipopolysaccharide (LPS) and peptidoglycan
CC of Gram-negative bacteria (PubMed:11872802). The different isoforms
CC probably display different recognition capabilities to various
CC microbial patterns (PubMed:12777387, PubMed:16006509).
CC {ECO:0000269|PubMed:11872802, ECO:0000269|PubMed:12777387,
CC ECO:0000269|PubMed:16006509, ECO:0000269|PubMed:22022271}.
CC -!- FUNCTION: [Isoform a]: Mediates the response to LPS and Gram-negative
CC bacteria. {ECO:0000269|PubMed:12777387, ECO:0000269|PubMed:16006509}.
CC -!- FUNCTION: [Isoform x]: Mediates the response to LPS, peptidoglycan and
CC Gram-negative bacteria. {ECO:0000269|PubMed:12777387,
CC ECO:0000269|PubMed:16006509}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11106397,
CC ECO:0000269|PubMed:11872802}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:11106397, ECO:0000269|PubMed:11872802}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000269|PubMed:11106397}; Synonyms=B
CC {ECO:0000269|PubMed:11106397};
CC IsoId=Q9GNK5-1; Sequence=Displayed;
CC Name=x {ECO:0000269|PubMed:11872802}; Synonyms=A
CC {ECO:0000269|PubMed:11872802};
CC IsoId=Q9GNK5-2; Sequence=VSP_050759;
CC Name=y {ECO:0000269|PubMed:12777387}; Synonyms=C
CC {ECO:0000269|PubMed:12777387};
CC IsoId=Q9GNK5-3; Sequence=VSP_050760;
CC -!- TISSUE SPECIFICITY: Expressed in the fat body and hemocytes.
CC {ECO:0000269|PubMed:11106397}.
CC -!- DEVELOPMENTAL STAGE: Expressed during larval and pupal stages.
CC {ECO:0000269|PubMed:11872802}.
CC -!- DISRUPTION PHENOTYPE: Larvae infected with Gram-negative bacteria fail
CC to induce tracheal expression of the antimicrobial peptide gene Drs.
CC {ECO:0000269|PubMed:22022271}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {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; AF207539; AAG23733.1; -; mRNA.
DR EMBL; AF500096; AAM18530.1; -; mRNA.
DR EMBL; AY327466; AAQ16306.1; -; mRNA.
DR EMBL; AE014296; AAF50302.3; -; Genomic_DNA.
DR EMBL; AE014296; AAN11957.1; -; Genomic_DNA.
DR EMBL; AE014296; AAS65052.1; -; Genomic_DNA.
DR EMBL; AY119048; AAM50908.1; -; mRNA.
DR EMBL; BT025958; ABG02202.1; -; mRNA.
DR RefSeq; NP_001163396.1; NM_001169925.1. [Q9GNK5-2]
DR RefSeq; NP_001246693.1; NM_001259764.1. [Q9GNK5-1]
DR RefSeq; NP_648298.1; NM_140041.4. [Q9GNK5-1]
DR RefSeq; NP_729468.2; NM_168324.4. [Q9GNK5-2]
DR RefSeq; NP_996030.1; NM_206308.4.
DR PDB; 1Z6I; X-ray; 2.50 A; A=355-520.
DR PDB; 2F2L; X-ray; 2.10 A; A=355-520, X=418-434.
DR PDBsum; 1Z6I; -.
DR PDBsum; 2F2L; -.
DR AlphaFoldDB; Q9GNK5; -.
DR SMR; Q9GNK5; -.
DR BioGRID; 64460; 89.
DR IntAct; Q9GNK5; 3.
DR MINT; Q9GNK5; -.
DR STRING; 7227.FBpp0088492; -.
DR GlyGen; Q9GNK5; 2 sites.
DR iPTMnet; Q9GNK5; -.
DR PaxDb; Q9GNK5; -.
DR DNASU; 39063; -.
DR EnsemblMetazoa; FBtr0089490; FBpp0088491; FBgn0035976. [Q9GNK5-2]
DR EnsemblMetazoa; FBtr0089491; FBpp0088492; FBgn0035976. [Q9GNK5-1]
DR EnsemblMetazoa; FBtr0300290; FBpp0289518; FBgn0035976. [Q9GNK5-2]
DR EnsemblMetazoa; FBtr0308349; FBpp0300668; FBgn0035976. [Q9GNK5-1]
DR GeneID; 39063; -.
DR KEGG; dme:Dmel_CG4432; -.
DR CTD; 39063; -.
DR FlyBase; FBgn0035976; PGRP-LC.
DR VEuPathDB; VectorBase:FBgn0035976; -.
DR eggNOG; ENOG502S2KY; Eukaryota.
DR InParanoid; Q9GNK5; -.
DR OMA; TEMSQCP; -.
DR PhylomeDB; Q9GNK5; -.
DR Reactome; R-DME-209171; Peptidoglycans (PGN) bind to a peptidoglycan recognition protein receptor, PGRP-LC/LE. [Q9GNK5-2]
DR Reactome; R-DME-209266; Peptidoglycan bound PGRP-LC/LE oligomerises.
DR Reactome; R-DME-214397; Assembly of the PGN:PGRP-LC/LE receptor 'signalling complex'.
DR Reactome; R-DME-214399; Activated IkappaB kinase (IKK) complex, Phospho IRD5:KEY dimer, phosphorylates REL in the PGN:PGRP-LC/LE receptor 'signalling complex'.
DR Reactome; R-DME-214411; REL binds to DREDD in the PGN:PGRP-LC/LE receptor 'signalling complex'.
DR Reactome; R-DME-214416; Phosphorylated REL is cleaved by and dissociates from DREDD.
DR BioGRID-ORCS; 39063; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; Q9GNK5; -.
DR GenomeRNAi; 39063; -.
DR PRO; PR:Q9GNK5; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035976; Expressed in saliva-secreting gland and 23 other tissues.
DR ExpressionAtlas; Q9GNK5; baseline and differential.
DR Genevisible; Q9GNK5; DM.
DR GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0098793; C:presynapse; IDA:FlyBase.
DR GO; GO:0001875; F:lipopolysaccharide immune receptor activity; IMP:FlyBase.
DR GO; GO:0042834; F:peptidoglycan binding; IDA:FlyBase.
DR GO; GO:0016019; F:peptidoglycan immune receptor activity; IMP:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0019731; P:antibacterial humoral response; IMP:FlyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:FlyBase.
DR GO; GO:0051607; P:defense response to virus; IMP:FlyBase.
DR GO; GO:0006955; P:immune response; IMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IDA:FlyBase.
DR GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IMP:FlyBase.
DR GO; GO:0006964; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IMP:FlyBase.
DR GO; GO:0002920; P:regulation of humoral immune response; IMP:FlyBase.
DR GO; GO:0035007; P:regulation of melanization defense response; IMP:FlyBase.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:FlyBase.
DR GO; GO:0009617; P:response to bacterium; 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; IPR015510; PGRP.
DR InterPro; IPR006619; PGRP_domain_met/bac.
DR PANTHER; PTHR11022; PTHR11022; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; SSF55846; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein; Immunity;
KW Innate immunity; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..520
FT /note="Peptidoglycan-recognition protein LC"
FT /id="PRO_0000220624"
FT TOPO_DOM 1..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..520
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 412..490
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000255"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16556841"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16556841"
FT DISULFID 390..396
FT /evidence="ECO:0000269|PubMed:16006509,
FT ECO:0000269|PubMed:16556841"
FT VAR_SEQ 324..520
FT /note="SKIRDDDDYRQNIPINSTIDLDNIGGGLILRFVERQQWLAQPPQKEIPDLEL
FT PVGLVIALPTNSENCSTQAICVLRVRLLQTYDIESSQKCDIAYNFLIGGDGNVYVGRGW
FT NKMGAHMNNINYDSQSLSFAYIGSFKTIQPSAKQLSVTRLLLERGVKLGKIAPSYRFTA
FT SSKLMPSVTDFKADALYASFANWTHWS -> TDLDVIDNSTLVILKVAEWGGRPAKRML
FT DAQQLPINRVVISHTAAEGCESREVCSARVNVVQSFHMDSWGWDHIGYNFLVGGDGRVY
FT EGRGWDYVGAHTKGYNRGSIGISFIGTFTTRKPNERQLEACQLLLQEGVRLKKLTTNYR
FT LYGHRQLSATESPGEELYKIIKKWPHWSHEI (in isoform x)"
FT /evidence="ECO:0000303|PubMed:11106397,
FT ECO:0000303|PubMed:11872802, ECO:0000303|PubMed:12537569,
FT ECO:0000303|Ref.7"
FT /id="VSP_050759"
FT VAR_SEQ 324..520
FT /note="SKIRDDDDYRQNIPINSTIDLDNIGGGLILRFVERQQWLAQPPQKEIPDLEL
FT PVGLVIALPTNSENCSTQAICVLRVRLLQTYDIESSQKCDIAYNFLIGGDGNVYVGRGW
FT NKMGAHMNNINYDSQSLSFAYIGSFKTIQPSAKQLSVTRLLLERGVKLGKIAPSYRFTA
FT SSKLMPSVTDFKADALYASFANWTHWS -> TNDPEIHVDGKLVVISIKGWGGMPTRGN
FT LKPLKLPVSKVIISETPPEICTTQDSCSYWTRVTQSRHMDTFNWSQVGYNFLVGGDGRI
FT YEGRGWNYMGDHTRDNNNNSIGITFLGTFRRQEPTPKSLEACQLLIAQGVRLKKLKPDY
FT QLLGHRQITGTLMPGEELYRIIQTWNNWYNLTKTWPDLHMTQ (in isoform y)"
FT /evidence="ECO:0000303|PubMed:11106397,
FT ECO:0000303|PubMed:12777387"
FT /id="VSP_050760"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:2F2L"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:2F2L"
FT STRAND 375..384
FT /evidence="ECO:0007829|PDB:2F2L"
FT HELIX 393..409
FT /evidence="ECO:0007829|PDB:2F2L"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:2F2L"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:2F2L"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:2F2L"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:2F2L"
FT HELIX 444..447
FT /evidence="ECO:0007829|PDB:2F2L"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:2F2L"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:2F2L"
FT HELIX 466..481
FT /evidence="ECO:0007829|PDB:2F2L"
FT STRAND 484..493
FT /evidence="ECO:0007829|PDB:2F2L"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:2F2L"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:2F2L"
FT HELIX 507..511
FT /evidence="ECO:0007829|PDB:2F2L"
FT TURN 512..515
FT /evidence="ECO:0007829|PDB:2F2L"
FT CONFLICT Q9GNK5-3:338
FT /note="I -> V (in Ref. 4; AAS65052)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9GNK5-3:355
FT /note="L -> F (in Ref. 4; AAS65052)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9GNK5-3:373
FT /note="T -> K (in Ref. 3; AAQ16306)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 56046 MW; 3215F8380857DFC1 CRC64;
MPFSNETEMS QCSNAKRRVN DPLTGPKNCS TSSTDSGVIL NDNVAAFRPE KETKDRGTGE
GQFQSKSEEK TESKRISVEH TVNITTENVG KTSSPAVSIR STTISVVSID DNAIDSSSID
SDSEAEAEDY TVQKLGHQVT YPPNSSHLRD LNQGLTVISR HVAPGEAAVP PPNPLEAGIV
AKQILNGNLA VATPTSPAGG ATQGIGSIAL TNSTDVTFGD KHFYEGPVTI QQFLIDNRDK
WKPGEGPAGG QDNPAFNGGP STNGSAPGSK HEDPAQTPPI CPFLPNTVGR KAVTVTVVFV
TLTFLLGIVL ATTTNLFGKT LNQSKIRDDD DYRQNIPINS TIDLDNIGGG LILRFVERQQ
WLAQPPQKEI PDLELPVGLV IALPTNSENC STQAICVLRV RLLQTYDIES SQKCDIAYNF
LIGGDGNVYV GRGWNKMGAH MNNINYDSQS LSFAYIGSFK TIQPSAKQLS VTRLLLERGV
KLGKIAPSYR FTASSKLMPS VTDFKADALY ASFANWTHWS
