Q8T9B6 (MESD_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
LDLR chaperone boca

Gene names

Name:	boca
ORF Names:	CG30498

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	180 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Chaperone specifically assisting the folding of beta-propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). Acts as a modulator of the Wg pathway, since some LDLRs are coreceptors for the canonical Wnt pathway. Ref.4
Subunit structure	Monomer By similarity. Interacts with Arrow and Yolkless. Ref.4
Subcellular location	Endoplasmic reticulum Ref.4.
Domain	The LDLR maturation activity resides in the N- and C-terminal unstructured regions By similarity.
Sequence similarities	Belongs to the MESD family.

Ontologies

Keywords
Biological process	Wnt signaling pathway
Cellular component	Endoplasmic reticulum
Domain	Signal
Molecular function	Chaperone
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ER to Golgi vesicle-mediated transport Inferred from expression pattern Ref.4. Source: FlyBase Wnt receptor signaling pathway Inferred from mutant phenotype Ref.4. Source: FlyBase low-density lipoprotein receptor particle metabolic process Inferred from mutant phenotype Ref.4. Source: FlyBase oogenesis Inferred from mutant phenotype Ref.4. Source: FlyBase proboscis development Inferred from mutant phenotype Ref.4. Source: FlyBase protein targeting to membrane Inferred from mutant phenotype Ref.4. Source: FlyBase
Cellular_component	apical part of cell Inferred from direct assay Ref.4. Source: FlyBase endoplasmic reticulum lumen Inferred from direct assay Ref.4. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Potential

Chain

19 – 180

162

LDLR chaperone boca

PRO_0000385021

Regions

Region

93 – 166

74

Structured core By similarity

Motif

177 – 180

4

Prevents secretion from ER

Experimental info

Mutagenesis

49

1

W → R in boca1; induces lethality. Ref.4

Sequence conflict

15

1

L → V in AAL39985. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

180

Helix Strand Turn

Details...

Beta strand

94 – 103

10

Helix

106 – 122

17

Beta strand

127 – 133

7

Beta strand

136 – 143

8

Helix

144 – 146

3

Helix

147 – 154

8

Beta strand

160 – 165

6

Beta strand

168 – 171

4

Sequences

	Sequence		Length	Mass (Da)
	Q8T9B6 [UniParc]. Last modified September 22, 2009. Version 2. Checksum: B51E057C901A6546	FASTA	180	21,002
	10 20 30 40 50 60 MQTRLVLLLL ALTPLVLAKK FKEEEKPAWA KKDIRDYSEA DLERLLDQWE EDEEPLEDDE 70 80 90 100 110 120 LPEHLRPQPK LDLSNLDSKS PEDLLKVSKK GRTLMTFVSV TGNPTREESD TITKLWQTSL 130 140 150 160 170 180 WNNHIQAERY MVDDNRAIFL FKDGTQAWDA KDFLIEQERC KGVTIENKEY PGVNAKKDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[4]	"Boca, an endoplasmic reticulum protein required for wingless signaling and trafficking of LDL receptor family members in Drosophila." Culi J., Mann R.S. Cell 112:343-354(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ARROW AND YOLKLESS, SUBCELLULAR LOCATION, MUTAGENESIS OF TRP-49.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE013599 Genomic DNA. Translation: AAF59229.2.
AY069840 mRNA. Translation: AAL39985.1.
BT044294 mRNA. Translation: ACH92359.1.

RefSeq

NP_724578.1. NM_165541.2.

UniGene

Dm.14878.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3OFE	X-ray	2.29	A/B	88-172	[»]
3OFF	X-ray	2.00	A	89-172	[»]

ProteinModelPortal

Q8T9B6.

SMR

Q8T9B6. Positions 31-172.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59112N.

STRING

7227.FBpp0088027.

Proteomic databases

PaxDb

Q8T9B6.

PRIDE

Q8T9B6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0088953; FBpp0088027; FBgn0004132.

GeneID

48986.

KEGG

dme:Dmel_CG30498.

UCSC

CG30498-RA. d. melanogaster.

Organism-specific databases

CTD

48986.

FlyBase

FBgn0004132. boca.

Phylogenomic databases

eggNOG

NOG286690.

GeneTree

ENSGT00390000000993.

InParanoid

Q8T9B6.

OMA

SLWNNHI.

OrthoDB

EOG4V6X06.

PhylomeDB

Q8T9B6.

Gene expression databases

Bgee

Q8T9B6.

Family and domain databases

InterPro

IPR019330. Mesoderm_development_cand-2.
[Graphical view]

Pfam

PF10185. Mesd. 1 hit.
[Graphical view]

PROSITE

PS00014. ER_TARGET. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q8T9B6.

GenomeRNAi

48986.

NextBio

839609.

Entry information

Entry name

MESD_DROME

Accession

Primary (citable) accession number: Q8T9B6
Secondary accession number(s): A1Z712

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 22, 2009
Last sequence update:	September 22, 2009
Last modified:	May 29, 2013
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project