PDIA6_DROME
ID PDIA6_DROME Reviewed; 433 AA.
AC Q9V438;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Protein disulfide-isomerase A6 homolog {ECO:0000305};
DE EC=5.3.4.1 {ECO:0000250|UniProtKB:Q15084};
DE AltName: Full=Calcium-binding protein 1 {ECO:0000312|FlyBase:FBgn0025678};
DE Short=DmCaBP1 {ECO:0000303|PubMed:9770267};
DE Flags: Precursor;
GN Name=CaBP1 {ECO:0000312|FlyBase:FBgn0025678};
GN ORFNames=CG5809 {ECO:0000312|FlyBase:FBgn0025678};
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:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9770267;
RX DOI=10.1002/(sici)1520-6408(1998)23:2<104::aid-dvg2>3.0.co;2-a;
RA Li Y., Musacchio M., Finkelstein R.;
RT "A homologue of the calcium-binding disulfide isomerase CaBP1 is expressed
RT in the developing CNS of Drosophila melanogaster.";
RL Dev. Genet. 23:104-110(1998).
RN [2] {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 [3] {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 [4] {ECO:0000312|EMBL:AAL28897.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28897.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL28897.1};
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 [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH DRPR, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND IDENTIFICATION BY MASS SPECTROMETRY.
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: Binds to both apoptotic cells and phagocytes and promotes
CC Drpr-dependent phagocytosis of apoptotic cells.
CC {ECO:0000269|PubMed:22158613}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.;
CC EC=5.3.4.1; Evidence={ECO:0000250|UniProtKB:Q15084};
CC -!- SUBUNIT: Interacts with Drpr (via extracellular region).
CC {ECO:0000269|PubMed:22158613}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:22158613}. Cell surface
CC {ECO:0000269|PubMed:22158613}. Note=Relocates from the endoplasmic
CC reticulum to the cell surface during apoptosis.
CC {ECO:0000269|PubMed:22158613}.
CC -!- TISSUE SPECIFICITY: In the blastoderm embryo, expression starts at the
CC anterior and posterior poles and later appears as broad stripes.
CC Following gastrulation, expressed in midline precursor cells and the
CC posterior head with low levels present throughout the embryo. During
CC germ band extension, weak dorsoventral stripes of expression are
CC evident. Midline expression begins and is retained throughout
CC embryogenesis in clusters of cells in each segment in the central
CC nervous system. At least some of the midline expression occurs in VUM
CC neurons. {ECO:0000269|PubMed:9770267}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development from embryo to
CC adult. {ECO:0000269|PubMed:22158613}.
CC -!- DISRUPTION PHENOTYPE: Reduced levels of phagocytosis. Loss of both
CC CaBP1 and Prtp does not cause a further decrease in the reduced level
CC of phagocytosis seen in either CaBP1-lacking or Prtp-lacking embryos.
CC {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; AE014134; AAF53532.1; -; Genomic_DNA.
DR EMBL; AE014134; AHN54493.1; -; Genomic_DNA.
DR EMBL; AY061349; AAL28897.1; -; mRNA.
DR RefSeq; NP_001285979.1; NM_001299050.1.
DR RefSeq; NP_609792.1; NM_135948.4.
DR AlphaFoldDB; Q9V438; -.
DR SMR; Q9V438; -.
DR IntAct; Q9V438; 6.
DR STRING; 7227.FBpp0080395; -.
DR GlyGen; Q9V438; 1 site.
DR PaxDb; Q9V438; -.
DR PRIDE; Q9V438; -.
DR DNASU; 34976; -.
DR EnsemblMetazoa; FBtr0080837; FBpp0080395; FBgn0025678.
DR EnsemblMetazoa; FBtr0345544; FBpp0311643; FBgn0025678.
DR GeneID; 34976; -.
DR KEGG; dme:Dmel_CG5809; -.
DR UCSC; CG5809-RA; d. melanogaster.
DR CTD; 9478; -.
DR FlyBase; FBgn0025678; CaBP1.
DR VEuPathDB; VectorBase:FBgn0025678; -.
DR eggNOG; KOG0191; Eukaryota.
DR GeneTree; ENSGT00940000155646; -.
DR HOGENOM; CLU_030311_0_0_1; -.
DR InParanoid; Q9V438; -.
DR OMA; DDIWLVE; -.
DR OrthoDB; 840943at2759; -.
DR PhylomeDB; Q9V438; -.
DR Reactome; R-DME-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DME-8957275; Post-translational protein phosphorylation.
DR SignaLink; Q9V438; -.
DR BioGRID-ORCS; 34976; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34976; -.
DR PRO; PR:Q9V438; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0025678; Expressed in male reproductive gland and 28 other tissues.
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:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISS:FlyBase.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:2000427; P:positive regulation of apoptotic cell clearance; IDA:FlyBase.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IBA:GO_Central.
DR InterPro; IPR005788; Disulphide_isomerase.
DR InterPro; IPR044569; PDIA6-like.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR45815; PTHR45815; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR SUPFAM; SSF52833; SSF52833; 3.
DR TIGRFAMs; TIGR01126; pdi_dom; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 2.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase;
KW Phagocytosis; Redox-active center; Reference proteome; Repeat; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..433
FT /note="Protein disulfide-isomerase A6 homolog"
FT /id="PRO_5007929183"
FT DOMAIN 20..119
FT /note="Thioredoxin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DOMAIN 120..267
FT /note="Thioredoxin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 405..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 430..433
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 419..433
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 55
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 58
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 186
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 189
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 55..58
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 186..189
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
SQ SEQUENCE 433 AA; 46752 MW; 1A1C8A04A801AAFD CRC64;
MRQLASILLL AFVVGSVSAF YSPSDGVVEL TPSNFDREVL KDDAIWVVEF YAPWCGHCQS
LVPEYKKLAK ALKGVVKVGS VNADADSTLS GQFGVRGFPT IKIFGANKKS PTDYNGQRTA
KAIAEAALAE VKKKVQGVLG GGGGSSSGGS GSSSGDDVIE LTEDNFDKLV LNSDDIWLVE
FFAPWCGHCK NLAPEWAKAA KELKGKVKLG ALDATAHQSK AAEYNVRGYP TIKFFPAGSK
RASDAQEYDG GRTASDIVSW ASDKHVANVP APELIEIINE STFETACEGK PLCVVSVLPH
ILDCDAKCRN KFLDTLRTLG EKFKQKQWGW AWAEGGQQLA LEESLEVGGF GYPAMAVVNF
KKMKFSVLKG SFSKDGINEF LRDISYGRGH TAPVRGAKKP AIVSVDPWDG KDGQLPTEED
IDLSDIDLDK DEL
