TXND5_DROME
ID TXND5_DROME Reviewed; 416 AA.
AC Q9VYV3; M9PGX2;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Thioredoxin domain-containing protein 5 homolog {ECO:0000305};
DE AltName: Full=Protein pretaporter {ECO:0000303|PubMed:19927123};
DE Flags: Precursor;
GN Name=prtp {ECO:0000312|FlyBase:FBgn0030329};
GN ORFNames=CG1837 {ECO:0000312|FlyBase:FBgn0030329};
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:AAK93133.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK93133.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAK93133.1};
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 [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19927123; DOI=10.1038/emboj.2009.343;
RA Kuraishi T., Nakagawa Y., Nagaosa K., Hashimoto Y., Ishimoto T., Moki T.,
RA Fujita Y., Nakayama H., Dohmae N., Shiratsuchi A., Yamamoto N., Ueda K.,
RA Yamaguchi M., Awasaki T., Nakanishi Y.;
RT "Pretaporter, a Drosophila protein serving as a ligand for Draper in the
RT phagocytosis of apoptotic cells.";
RL EMBO J. 28:3868-3878(2009).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=23337816;
RA Fujita Y., Nagaosa K., Shiratsuchi A., Nakanishi Y.;
RT "Role of NPxY motif in Draper-mediated apoptotic cell clearance in
RT Drosophila.";
RL Drug Discov. Ther. 6:291-297(2012).
RN [6] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=22158613; DOI=10.1074/jbc.m111.277921;
RA Okada R., Nagaosa K., Kuraishi T., Nakayama H., Yamamoto N., Nakagawa Y.,
RA Dohmae N., Shiratsuchi A., Nakanishi Y.;
RT "Apoptosis-dependent externalization and involvement in apoptotic cell
RT clearance of DmCaBP1, an endoplasmic reticulum protein of Drosophila.";
RL J. Biol. Chem. 287:3138-3146(2012).
CC -!- FUNCTION: Possesses thioredoxin activity (By similarity). Acts as a
CC ligand for Drpr and is required for the phagocytosis of apoptotic cells
CC (PubMed:19927123, PubMed:23337816). Binds to the extracellular region
CC of Drpr and augments Drpr tyrosine phosphorylation (PubMed:19927123,
CC PubMed:23337816). {ECO:0000250|UniProtKB:Q91W90,
CC ECO:0000269|PubMed:19927123, ECO:0000269|PubMed:23337816}.
CC -!- INTERACTION:
CC Q9VYV3; Q9W0A0: drpr; NbExp=3; IntAct=EBI-125861, EBI-107028;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:19927123}. Cell surface
CC {ECO:0000269|PubMed:19927123}. Note=Relocates from the endoplasmic
CC reticulum to the cell surface during apoptosis.
CC {ECO:0000269|PubMed:19927123}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000312|FlyBase:FBgn0030329}; Synonyms=B
CC {ECO:0000312|FlyBase:FBgn0030329}, C {ECO:0000312|FlyBase:FBgn0030329};
CC IsoId=Q9VYV3-1; Sequence=Displayed;
CC Name=D {ECO:0000312|FlyBase:FBgn0030329};
CC IsoId=Q9VYV3-2; Sequence=VSP_058568;
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo, larva, pupa and adult (at
CC protein level). {ECO:0000269|PubMed:19927123}.
CC -!- DISRUPTION PHENOTYPE: Reduced level of apoptotic cell phagocytosis
CC (PubMed:19927123). Loss of both Prtp and CaBP1 does not cause a further
CC decrease in the reduced level of phagocytosis seen in either Prtp-
CC lacking or CaBP1-lacking embryos (PubMed:22158613).
CC {ECO:0000269|PubMed:19927123, ECO:0000269|PubMed:22158613}.
CC -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC {ECO:0000255, ECO:0000255|RuleBase:RU004208}.
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DR EMBL; AE014298; AAF48082.2; -; Genomic_DNA.
DR EMBL; AE014298; ADV37665.1; -; Genomic_DNA.
DR EMBL; AE014298; ADV37666.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95303.1; -; Genomic_DNA.
DR EMBL; AY051709; AAK93133.1; -; mRNA.
DR RefSeq; NP_001188583.1; NM_001201654.2. [Q9VYV3-1]
DR RefSeq; NP_001188584.1; NM_001201655.2. [Q9VYV3-1]
DR RefSeq; NP_001259460.1; NM_001272531.1. [Q9VYV3-2]
DR RefSeq; NP_572742.1; NM_132514.3. [Q9VYV3-1]
DR AlphaFoldDB; Q9VYV3; -.
DR SMR; Q9VYV3; -.
DR IntAct; Q9VYV3; 13.
DR MINT; Q9VYV3; -.
DR STRING; 7227.FBpp0292397; -.
DR PaxDb; Q9VYV3; -.
DR PRIDE; Q9VYV3; -.
DR DNASU; 32124; -.
DR EnsemblMetazoa; FBtr0073551; FBpp0073396; FBgn0030329. [Q9VYV3-1]
DR EnsemblMetazoa; FBtr0303334; FBpp0292397; FBgn0030329. [Q9VYV3-1]
DR EnsemblMetazoa; FBtr0303335; FBpp0292398; FBgn0030329. [Q9VYV3-1]
DR EnsemblMetazoa; FBtr0332954; FBpp0305170; FBgn0030329. [Q9VYV3-2]
DR GeneID; 32124; -.
DR KEGG; dme:Dmel_CG1837; -.
DR UCSC; CG1837-RA; d. melanogaster. [Q9VYV3-1]
DR CTD; 32124; -.
DR FlyBase; FBgn0030329; prtp.
DR VEuPathDB; VectorBase:FBgn0030329; -.
DR eggNOG; KOG0191; Eukaryota.
DR GeneTree; ENSGT00940000156920; -.
DR InParanoid; Q9VYV3; -.
DR OMA; TKHQTLC; -.
DR PhylomeDB; Q9VYV3; -.
DR Reactome; R-DME-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; Q9VYV3; -.
DR BioGRID-ORCS; 32124; 0 hits in 1 CRISPR screen.
DR ChiTaRS; prtp; fly.
DR GenomeRNAi; 32124; -.
DR PRO; PR:Q9VYV3; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030329; Expressed in thoracico-abdominal ganglion (Drosophila) and 33 other tissues.
DR ExpressionAtlas; Q9VYV3; baseline and differential.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:FlyBase.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IBA:GO_Central.
DR GO; GO:0043277; P:apoptotic cell clearance; IMP:FlyBase.
DR GO; GO:2000427; P:positive regulation of apoptotic cell clearance; IMP:FlyBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 3.
DR SUPFAM; SSF52833; SSF52833; 3.
DR TIGRFAMs; TIGR01126; pdi_dom; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Endoplasmic reticulum; Phagocytosis;
KW Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..416
FT /note="Thioredoxin domain-containing protein 5 homolog"
FT /id="PRO_5007929564"
FT DOMAIN 26..145
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 150..272
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 293..412
FT /note="Thioredoxin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT MOTIF 413..416
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT DISULFID 65..68
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 194..197
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 331..334
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT VAR_SEQ 1..64
FT /note="MLTRSILSVAVCGLLLSPLLPITRASQEEDTGKQDKQFTVELDPETFDTAIA
FT GGNVFVKFFAPW -> M (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_058568"
SQ SEQUENCE 416 AA; 46650 MW; 806FB758CABF7266 CRC64;
MLTRSILSVA VCGLLLSPLL PITRASQEED TGKQDKQFTV ELDPETFDTA IAGGNVFVKF
FAPWCGHCKR IQPLWEQLAE IMNVDNPKVI IAKVDCTKHQ GLCATHQVTG YPTLRLFKLG
EEESVKFKGT RDLPAITDFI NKELSAPAEA DLGEVKREQV ENLNIGKVVD LTEDTFAKHV
STGNHFVKFF APWCSHCQRL APTWEDLAKE LIKEPTVTIS KIDCTQFRSI CQDFEVKGYP
TLLWIEDGKK IEKYSGARDL STLKTYVEKM VGVPLEKTAG EAGDEKVVIE EVAGEEDAAK
KLTPQQLTGE DEFDQAIAEG VAFIKFYAPW CGHCQKLQPT WEQLATETHQ AQSSVKIAKV
DCTAPENKQV CIDQQVEGYP TLFLYKNGQR QNEYEGSRSL PELQAYLKKF LGHDEL
