BARA1_DROME
ID BARA1_DROME Reviewed; 257 AA.
AC C0HLZ9; Q7KR65; Q7KR66; Q8ML70; Q8ML71;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 1.
DT 03-AUG-2022, entry version 2.
DE RecName: Full=Baramicin A1 {ECO:0000303|PubMed:34432851};
DE Contains:
DE RecName: Full=Immune-induced peptide 24 {ECO:0000303|PubMed:34432851};
DE Short=DIM-24 {ECO:0000305|PubMed:9736738};
DE Short=DIM24 {ECO:0000303|PubMed:9736738};
DE Short=IM24 {ECO:0000303|PubMed:34432851};
DE Contains:
DE RecName: Full=Immune-induced peptide 10 {ECO:0000303|PubMed:34432851};
DE Short=DIM-10 {ECO:0000305|PubMed:9736738};
DE Short=DIM10 {ECO:0000303|PubMed:9736738};
DE Short=IM10 {ECO:0000303|PubMed:34432851};
DE Contains:
DE RecName: Full=Immune-induced peptide 12 {ECO:0000303|PubMed:34432851};
DE Short=DIM-12 {ECO:0000305|PubMed:9736738};
DE Short=DIM12 {ECO:0000303|PubMed:9736738};
DE Short=IM12 {ECO:0000303|PubMed:34432851};
DE Contains:
DE RecName: Full=Immune-induced peptide 13 {ECO:0000303|PubMed:34432851};
DE Short=DIM-13 {ECO:0000305|PubMed:9736738};
DE Short=DIM13 {ECO:0000303|PubMed:9736738};
DE Short=IM13 {ECO:0000303|PubMed:34432851};
DE Contains:
DE RecName: Full=Immune-induced peptide 22 {ECO:0000303|PubMed:34432851};
DE Short=DIM-22 {ECO:0000305|PubMed:9736738};
DE Short=DIM22 {ECO:0000303|PubMed:9736738};
DE Short=IM22 {ECO:0000303|PubMed:34432851};
DE Contains:
DE RecName: Full=Immune-induced peptide 5 {ECO:0000303|PubMed:34432851};
DE Short=DIM-5 {ECO:0000305|PubMed:34432851};
DE Short=DIM5 {ECO:0000305|PubMed:34432851};
DE Short=IM5 {ECO:0000303|PubMed:34432851};
DE Contains:
DE RecName: Full=Immune-induced peptide 6 {ECO:0000303|PubMed:34432851};
DE Short=DIM-6 {ECO:0000305|PubMed:34432851};
DE Short=DIM6 {ECO:0000305|PubMed:34432851};
DE Short=IM6 {ECO:0000303|PubMed:34432851};
DE Contains:
DE RecName: Full=Immune-induced peptide 8 {ECO:0000303|PubMed:34432851};
DE Short=DIM-8 {ECO:0000305|PubMed:9736738};
DE Short=DIM8 {ECO:0000303|PubMed:9736738};
DE Short=IM8 {ECO:0000303|PubMed:34432851};
DE Flags: Precursor;
GN Name=BaraA1 {ECO:0000303|PubMed:34432851, ECO:0000312|FlyBase:FBgn0053470};
GN Synonyms=IMPPP {ECO:0000312|FlyBase:FBgn0053470};
GN ORFNames=CG33470 {ECO:0000312|FlyBase:FBgn0053470};
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|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:AAO41418.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO41418.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAO41418.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 22-117; 122-144; 149-171 AND 176-198, PYROGLUTAMATE
RP FORMATION AT GLN-22; GLN-122; GLN-149 AND GLN-176, AND MASS SPECTROMETRY.
RC STRAIN=Oregon-R {ECO:0000303|Ref.4}; TISSUE=Hemolymph {ECO:0000303|Ref.4};
RA Bulet P.;
RL Submitted (JUL-2000) to UniProtKB.
RN [5]
RP GENOME REANNOTATION.
RX PubMed=14709175; DOI=10.1186/gb-2003-5-1-r3;
RA Hild M., Beckmann B., Haas S.A., Koch B., Solovyev V., Busold C.,
RA Fellenberg K., Boutros M., Vingron M., Sauer F., Hoheisel J.D., Paro R.;
RT "An integrated gene annotation and transcriptional profiling approach
RT towards the full gene content of the Drosophila genome.";
RL Genome Biol. 5:R3.1-R3.17(2003).
RN [6] {ECO:0000305}
RP FUNCTION, INDUCTION BY BACTERIA, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Oregon-R {ECO:0000303|PubMed:9736738};
RC TISSUE=Hemolymph {ECO:0000303|PubMed:9736738};
RX PubMed=9736738; DOI=10.1073/pnas.95.19.11342;
RA Uttenweiler-Joseph S., Moniatte M., Lagueux M., van Dorsselaer A.,
RA Hoffmann J.A., Bulet P.;
RT "Differential display of peptides induced during the immune response of
RT Drosophila: a matrix-assisted laser desorption ionization time-of-flight
RT mass spectrometry study.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11342-11347(1998).
RN [7]
RP PROTEIN SEQUENCE OF 176-198, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PYROGLUTAMATE FORMATION AT
RP GLN-176.
RC TISSUE=Hemolymph {ECO:0000303|Ref.7};
RX DOI=10.1255/ejms.450;
RA Carte N., Cavusoglu N., Leize E., Dorsselaer A.V.;
RT "De novo sequencing by nano-electrospray multiple-stage tandem mass
RT spectrometry of an immune-induced peptide of Drosophila melanogaster.";
RL Eur. J. Mass Spectrom. 7:399-408(2001).
RN [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY BACTERIA, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hemolymph {ECO:0000303|PubMed:16510152};
RX PubMed=16510152; DOI=10.1016/j.jinsphys.2005.12.007;
RA Verleyen P., Baggerman G., D'Hertog W., Vierstraete E., Husson S.J.,
RA Schoofs L.;
RT "Identification of new immune induced molecules in the haemolymph of
RT Drosophila melanogaster by 2D-nanoLC MS/MS.";
RL J. Insect Physiol. 52:379-388(2006).
RN [9]
RP SYNTHESIS OF 122-144; 149-171 AND 176-198, FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INDUCTION BY BACTERIA, DISRUPTION PHENOTYPE,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PROTEOLYTIC PROCESSING.
RC STRAIN=Oregon-R {ECO:0000303|PubMed:34432851};
RC TISSUE=Hemolymph {ECO:0000303|PubMed:34432851};
RX PubMed=34432851; DOI=10.1371/journal.ppat.1009846;
RA Hanson M.A., Cohen L.B., Marra A., Iatsenko I., Wasserman S.A.,
RA Lemaitre B.;
RT "The Drosophila Baramicin polypeptide gene protects against fungal
RT infection.";
RL PLoS Pathog. 17:e1009846-e1009846(2021).
CC -!- FUNCTION: Secreted immune-induced peptides induced by Toll signaling
CC (PubMed:9736738, PubMed:34432851). Has a significant role in resistance
CC to infection by the entomopathogenic fungus B.bassiana R444 and weak
CC antifungal activity against M.rileyi PHP1705 (PubMed:34432851). In
CC adult males, activity appears to be important for neuromuscular
CC processes that mediate correct wing posture upon Toll activation
CC (PubMed:34432851). {ECO:0000269|PubMed:34432851,
CC ECO:0000269|PubMed:9736738}.
CC -!- SUBCELLULAR LOCATION: [Immune-induced peptide 24]: Secreted
CC {ECO:0000269|PubMed:34432851}.
CC -!- SUBCELLULAR LOCATION: [Immune-induced peptide 6]: Secreted
CC {ECO:0000269|PubMed:34432851}.
CC -!- SUBCELLULAR LOCATION: [Immune-induced peptide 12]: Secreted
CC {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851}.
CC -!- SUBCELLULAR LOCATION: [Immune-induced peptide 10]: Secreted
CC {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851,
CC ECO:0000269|PubMed:9736738}.
CC -!- SUBCELLULAR LOCATION: [Immune-induced peptide 5]: Secreted
CC {ECO:0000269|PubMed:34432851}.
CC -!- SUBCELLULAR LOCATION: [Immune-induced peptide 8]: Secreted
CC {ECO:0000269|PubMed:34432851}.
CC -!- SUBCELLULAR LOCATION: [Immune-induced peptide 13]: Secreted
CC {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851,
CC ECO:0000269|Ref.7}.
CC -!- SUBCELLULAR LOCATION: [Immune-induced peptide 22]: Secreted
CC {ECO:0000269|PubMed:34432851}.
CC -!- TISSUE SPECIFICITY: [Immune-induced peptide 24]: Hemolymph (at protein
CC level). {ECO:0000269|PubMed:34432851}.
CC -!- TISSUE SPECIFICITY: [Immune-induced peptide 6]: Hemolymph (at protein
CC level). {ECO:0000269|PubMed:34432851}.
CC -!- TISSUE SPECIFICITY: [Immune-induced peptide 12]: Hemolymph (at protein
CC level). {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851}.
CC -!- TISSUE SPECIFICITY: [Immune-induced peptide 10]: Hemolymph (at protein
CC level). {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851,
CC ECO:0000269|PubMed:9736738}.
CC -!- TISSUE SPECIFICITY: [Immune-induced peptide 5]: Hemolymph (at protein
CC level). {ECO:0000269|PubMed:34432851}.
CC -!- TISSUE SPECIFICITY: [Immune-induced peptide 8]: Hemolymph (at protein
CC level). {ECO:0000269|PubMed:34432851}.
CC -!- TISSUE SPECIFICITY: [Immune-induced peptide 13]: Hemolymph (at protein
CC level). {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851,
CC ECO:0000269|Ref.7}.
CC -!- TISSUE SPECIFICITY: [Immune-induced peptide 22]: Hemolymph (at protein
CC level). {ECO:0000269|PubMed:34432851}.
CC -!- INDUCTION: By bacterial infection (at protein level) (PubMed:9736738,
CC PubMed:16510152). Detected within 24 hours of infection
CC (PubMed:9736738). Up-regulated in the fat body following infection with
CC M.luteus, with expression levels increasing from 2 to 48 hours post
CC infection (PubMed:34432851). In adults, also up-regulated in the head
CC including the border of the eyes and the ocelli, and in the brain
CC tissue including the region posterior to the central brain furrow
CC (PubMed:34432851). Up-regulated in the wing veins, along the borders of
CC the thoracic pleura, and in the spermatheca of females
CC (PubMed:34432851). In larvae, induced in the brain tissue at the
CC posterior of the ventral nervous system (PubMed:34432851).
CC {ECO:0000269|PubMed:16510152, ECO:0000269|PubMed:34432851,
CC ECO:0000269|PubMed:9736738}.
CC -!- PTM: Proteolytically cleaved. {ECO:0000269|PubMed:34432851,
CC ECO:0000269|PubMed:9736738}.
CC -!- MASS SPECTROMETRY: [Immune-induced peptide 24]: Mass=10030.8;
CC Method=MALDI; Evidence={ECO:0000269|Ref.4};
CC -!- MASS SPECTROMETRY: [Immune-induced peptide 12]: Mass=2572.8;
CC Method=MALDI; Evidence={ECO:0000269|Ref.4};
CC -!- MASS SPECTROMETRY: [Immune-induced peptide 12]: Mass=2571.3;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:16510152};
CC -!- MASS SPECTROMETRY: [Immune-induced peptide 10]: Mass=2520.8;
CC Method=MALDI; Evidence={ECO:0000269|Ref.4};
CC -!- MASS SPECTROMETRY: [Immune-induced peptide 10]: Mass=2519.3;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:16510152};
CC -!- MASS SPECTROMETRY: [Immune-induced peptide 13]: Mass=2650.9;
CC Method=MALDI; Evidence={ECO:0000269|Ref.4};
CC -!- MASS SPECTROMETRY: [Immune-induced peptide 13]: Mass=2649.4;
CC Method=MALDI; Evidence={ECO:0000269|Ref.7};
CC -!- MASS SPECTROMETRY: [Immune-induced peptide 13]: Mass=2649.3;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:16510152};
CC -!- MASS SPECTROMETRY: [Immune-induced peptide 22]: Mass=5974.5;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:34432851};
CC -!- DISRUPTION PHENOTYPE: Viable with no obvious morphological defects,
CC however flies have an increased susceptibility to entomopathogenic
CC fungi (PubMed:34432851). Displays increased fungal load 48 hours after
CC infection with B.bassiana R444 spores resulting in a significant
CC decrease in survival (PubMed:34432851). Survival is also slightly
CC decreased following septic injury with M.rileyi PHP1705
CC (PubMed:34432851). Some adult males display an erect wing phenotype
CC upon infection with Gram-positive bacteria, fungi, and to a lesser
CC extent, Gram-negative bacteria and clean injury (PubMed:34432851).
CC Males also display the erect wing phenotype after injury with heat-
CC killed E.faecalis suggesting that the phenotype occurs due to Toll
CC activation and is not the result of infection (PubMed:34432851). No
CC effect on activation of the Toll or imd/NF-kappa-B signaling cascades
CC in response to microbial infection (PubMed:34432851). No significant
CC affect on lifespan, resistance to bacterial infection and survival
CC following clean injury (PubMed:34432851).
CC {ECO:0000269|PubMed:34432851}.
CC -!- MISCELLANEOUS: In some wild flies and common laboratory strains, the
CC BaraA locus has undergone a duplication event to produce two identical
CC paralogs, BaraA1 and BaraA2 (PubMed:34432851). However BaraA copy
CC number varies within these strains indicating that the duplication
CC event is recent and not fixed (PubMed:34432851).
CC {ECO:0000269|PubMed:34432851}.
CC -!- MISCELLANEOUS: The name 'Baramicin' derives from the Japanese idiom
CC Bara-Bara, meaning to break apart, and refers to the multiple peptides
CC produced from the precursor protein. {ECO:0000269|PubMed:34432851}.
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DR EMBL; AE013599; AAS64857.2; -; Genomic_DNA.
DR EMBL; AE013599; AAS64856.1; -; Genomic_DNA.
DR EMBL; BK003775; DAA02473.1; -; Genomic_DNA.
DR EMBL; BT003754; AAO41418.1; -; mRNA.
DR EnsemblMetazoa; FBtr0087654; FBpp0086780; FBgn0283462.
DR EnsemblMetazoa; FBtr0087656; FBpp0086782; FBgn0053470.
DR EnsemblMetazoa; FBtr0303099; FBpp0292218; FBgn0053470.
DR EnsemblMetazoa; FBtr0339757; FBpp0308804; FBgn0283462.
DR FlyBase; FBgn0053470; BaraA1.
DR Proteomes; UP000000803; Chromosome 2R.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antimicrobial; Cleavage on pair of basic residues;
KW Direct protein sequencing; Fungicide; Glycoprotein; Immunity;
KW Innate immunity; Pyrrolidone carboxylic acid; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..21
FT /evidence="ECO:0000269|Ref.4"
FT /id="PRO_0000021496"
FT PEPTIDE 22..117
FT /note="Immune-induced peptide 24"
FT /evidence="ECO:0000269|PubMed:34432851, ECO:0000269|Ref.4"
FT /id="PRO_0000021497"
FT PROPEP 118..121
FT /evidence="ECO:0000305|PubMed:34432851, ECO:0000305|Ref.4"
FT /id="PRO_0000021498"
FT PEPTIDE 122..144
FT /note="Immune-induced peptide 12"
FT /evidence="ECO:0000269|PubMed:16510152,
FT ECO:0000269|PubMed:34432851, ECO:0000269|Ref.4"
FT /id="PRO_0000021499"
FT PEPTIDE 122..139
FT /note="Immune-induced peptide 6"
FT /evidence="ECO:0000269|PubMed:34432851"
FT /id="PRO_0000455126"
FT PROPEP 145..148
FT /evidence="ECO:0000305|PubMed:34432851, ECO:0000305|Ref.4"
FT /id="PRO_0000021500"
FT PEPTIDE 149..171
FT /note="Immune-induced peptide 10"
FT /evidence="ECO:0000269|PubMed:16510152,
FT ECO:0000269|PubMed:34432851, ECO:0000269|Ref.4"
FT /id="PRO_0000021501"
FT PROPEP 172..175
FT /evidence="ECO:0000305|PubMed:34432851, ECO:0000305|Ref.4"
FT /id="PRO_0000021502"
FT PEPTIDE 176..198
FT /note="Immune-induced peptide 13"
FT /evidence="ECO:0000269|PubMed:16510152,
FT ECO:0000269|PubMed:34432851, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.7"
FT /id="PRO_0000021503"
FT PEPTIDE 176..196
FT /note="Immune-induced peptide 8"
FT /evidence="ECO:0000269|PubMed:34432851"
FT /id="PRO_0000455127"
FT PEPTIDE 176..192
FT /note="Immune-induced peptide 5"
FT /evidence="ECO:0000269|PubMed:34432851"
FT /id="PRO_0000455128"
FT PROPEP 199..204
FT /evidence="ECO:0000305|PubMed:34432851"
FT /id="PRO_0000455129"
FT PEPTIDE 205..257
FT /note="Immune-induced peptide 22"
FT /evidence="ECO:0000269|PubMed:34432851"
FT /id="PRO_0000455130"
FT REGION 95..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 122
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 149
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 176
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.4, ECO:0000269|Ref.7"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 257 AA; 28036 MW; 6080064ABCC1CC3D CRC64;
MKSFGLIALA ICGVICVAAE PQHTYDGRNG PHVFGSPGNQ VYIRGQNEGT YSVPGVGGQF
QNAPQRGEHV YTDEAGNTFV NRKNAGGPAS HTISGPNFSA KNLGPNGAKS VGIPQRARRS
PQFHVERPGR TVDVGNGGFY IQRGRRSPQL HVARPDRTVT IGNGGVYIQR SRRSPQFHVE
RPDRTVDFGN GGFSAQRFRR GINDARVQGE NFVARDDQAG IWDNNVSVWK RPDGRTVTID
RNGHTIVSGR GRPAQHY
