ID   MESD_DROME              Reviewed;         180 AA.
AC   Q8T9B6; A1Z712;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=LDLR chaperone boca;
DE   Flags: Precursor;
GN   Name=boca; ORFNames=CG30498;
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, INTERACTION WITH ARROW AND YOLKLESS, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF TRP-49.
RX   PubMed=12581524; DOI=10.1016/s0092-8674(02)01279-5;
RA   Culi J., Mann R.S.;
RT   "Boca, an endoplasmic reticulum protein required for wingless signaling and
RT   trafficking of LDL receptor family members in Drosophila.";
RL   Cell 112:343-354(2003).
CC   -!- FUNCTION: Chaperone specifically assisting the folding of beta-
CC       propeller/EGF modules within the family of low-density lipoprotein
CC       receptors (LDLRs). Acts as a modulator of the Wg pathway, since some
CC       LDLRs are coreceptors for the canonical Wnt pathway.
CC       {ECO:0000269|PubMed:12581524}.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with Arrow and Yolkless.
CC       {ECO:0000250, ECO:0000269|PubMed:12581524}.
CC   -!- INTERACTION:
CC       Q8T9B6; Q8T9B6: boca; NbExp=3; IntAct=EBI-15914860, EBI-15914860;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-
CC       ProRule:PRU10138, ECO:0000269|PubMed:12581524}.
CC   -!- DOMAIN: The LDLR maturation activity resides in the N- and C-terminal
CC       unstructured regions. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MESD family. {ECO:0000305}.
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DR   EMBL; AE013599; AAF59229.2; -; Genomic_DNA.
DR   EMBL; AY069840; AAL39985.1; -; mRNA.
DR   EMBL; BT044294; ACH92359.1; -; mRNA.
DR   RefSeq; NP_724578.1; NM_165541.2.
DR   PDB; 3OFE; X-ray; 2.29 A; A/B=88-172.
DR   PDB; 3OFF; X-ray; 2.00 A; A=89-172.
DR   PDBsum; 3OFE; -.
DR   PDBsum; 3OFF; -.
DR   AlphaFoldDB; Q8T9B6; -.
DR   SMR; Q8T9B6; -.
DR   BioGRID; 71878; 76.
DR   DIP; DIP-59112N; -.
DR   ELM; Q8T9B6; -.
DR   IntAct; Q8T9B6; 3.
DR   STRING; 7227.FBpp0088027; -.
DR   PaxDb; 7227-FBpp0088027; -.
DR   DNASU; 48986; -.
DR   EnsemblMetazoa; FBtr0088953; FBpp0088027; FBgn0004132.
DR   GeneID; 48986; -.
DR   KEGG; dme:Dmel_CG30498; -.
DR   UCSC; CG30498-RA; d. melanogaster.
DR   AGR; FB:FBgn0004132; -.
DR   CTD; 48986; -.
DR   FlyBase; FBgn0004132; boca.
DR   VEuPathDB; VectorBase:FBgn0004132; -.
DR   eggNOG; KOG4357; Eukaryota.
DR   GeneTree; ENSGT00390000000993; -.
DR   HOGENOM; CLU_111621_1_0_1; -.
DR   InParanoid; Q8T9B6; -.
DR   OMA; DTITKLW; -.
DR   OrthoDB; 2880079at2759; -.
DR   PhylomeDB; Q8T9B6; -.
DR   BioGRID-ORCS; 48986; 0 hits in 1 CRISPR screen.
DR   EvolutionaryTrace; Q8T9B6; -.
DR   GenomeRNAi; 48986; -.
DR   PRO; PR:Q8T9B6; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0004132; Expressed in eye disc (Drosophila) and 22 other cell types or tissues.
DR   GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
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; IDA:FlyBase.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEP:FlyBase.
DR   GO; GO:0006457; P:protein folding; IMP:FlyBase.
DR   GO; GO:0006612; P:protein targeting to membrane; IMP:FlyBase.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   DisProt; DP02312; -.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 6.10.250.640; -; 1.
DR   InterPro; IPR019330; MESD.
DR   PANTHER; PTHR17600:SF2; LRP CHAPERONE MESD; 1.
DR   PANTHER; PTHR17600; MESODERM DEVELOPMENT CANDIDATE 2; 1.
DR   Pfam; PF10185; Mesd; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   Genevisible; Q8T9B6; DM.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Endoplasmic reticulum; Reference proteome; Signal;
KW   Wnt signaling pathway.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..180
FT                   /note="LDLR chaperone boca"
FT                   /id="PRO_0000385021"
FT   REGION          48..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          93..166
FT                   /note="Structured core"
FT                   /evidence="ECO:0000250"
FT   MOTIF           177..180
FT                   /note="Prevents secretion from ER"
FT   MUTAGEN         49
FT                   /note="W->R: In boca1; induces lethality."
FT                   /evidence="ECO:0000269|PubMed:12581524"
FT   CONFLICT        15
FT                   /note="L -> V (in Ref. 3; AAL39985)"
FT                   /evidence="ECO:0000305"
FT   STRAND          94..103
FT                   /evidence="ECO:0007829|PDB:3OFF"
FT   HELIX           106..122
FT                   /evidence="ECO:0007829|PDB:3OFF"
FT   STRAND          127..133
FT                   /evidence="ECO:0007829|PDB:3OFF"
FT   STRAND          136..143
FT                   /evidence="ECO:0007829|PDB:3OFF"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:3OFF"
FT   HELIX           147..154
FT                   /evidence="ECO:0007829|PDB:3OFF"
FT   STRAND          160..165
FT                   /evidence="ECO:0007829|PDB:3OFF"
FT   STRAND          168..171
FT                   /evidence="ECO:0007829|PDB:3OFF"
SQ   SEQUENCE   180 AA;  21002 MW;  B51E057C901A6546 CRC64;
     MQTRLVLLLL ALTPLVLAKK FKEEEKPAWA KKDIRDYSEA DLERLLDQWE EDEEPLEDDE
     LPEHLRPQPK LDLSNLDSKS PEDLLKVSKK GRTLMTFVSV TGNPTREESD TITKLWQTSL
     WNNHIQAERY MVDDNRAIFL FKDGTQAWDA KDFLIEQERC KGVTIENKEY PGVNAKKDEL
//