Gene Dmel\Acp26Aa

Experimentally Determined Recombination Data

Location

Left of (cM)

Right of (cM)

Notes

Gene Model & Products

Please see the GBrowse view of Dmel\Acp26Aa for information on other features

To submit a correction to a gene model please use the Contact FlyBase form

Comments on Gene Model

Gene model reviewed during 5.51

Transcript Data

Annotated Transcripts

Name

FlyBase ID

RefSeq ID

Length (nt)

Associated CDS (aa)

Acp26Aa-RA

FBtr0079155

NM_057296

958

264

Additional Transcript Data & Comments

Reported size (kB)

0.9 (northern blot)

Comments

External Data

Crossreferences

Polypeptide Data

Annotated Polypeptides

Name

FlyBase ID

Predicted MW (kDa)

Length (aa)

Theoretical pI

RefSeq ID

GenBank protein

Acp26Aa-PA

FBpp0078786

29.6

264

9.31

NP_476644

AAF52298

Additional Polypeptide Data & Comments

Reported size (kDa)

264 (aa); 41, 37, 36 (kD observed); 29 (kD predicted)

41, 37, 33, 30, 28, 25 (kD observed)

29, 22 (kD observed)

Comments

Generated from the 30kD species by an N-terminal cleavage step in the female genital tract.

This putative cleavage product was not detected. It is thought to be generated from the 41kD product by an N-terminal cleavage step in the female genital tract.

The 41kD, 37kD and 36kD forms of Acp26Aa protein differ in the extent of glycosylation. The 36kD species is far less abundant than the other two. By tracking with region-specific antibodies, it was shown that the 41kD species is processed to 38kD, 33kD and finally to 28kD while the 37kD species is processed to 33kD, 30kD and finally 25kD in parallel processing pathways. These processing steps were shown to consist of stepwise cleavage events in the N-terminal half of the protein. The processing sites were mapped by CNBr mapping and by analysis of conserved cleav ge sites within several Drosophila species. Finally, it was found that accessory gland main cell secretions are necessary to process Acp26Aa protein in the female genital tract.

Three forms of Acp26Aa protein are present in the male accessory gland, 36, 37, and 41kD. The 37kD is the most abundant. This is cleaved to 30kD in the female genital tract by the end of mating. There may be a 33kD intermediate.

Generated from a 33kD species by an N-terminal cleavage step in the female genital tract.

Generated from the 37kD species by an N-terminal cleavage step in the female genital tract.

The 41kD, 37kD and 36kD forms of Acp26Aa protein differ in the extent of glycosylation. The 36kD species is far less abundant than the other two. By tracking with region-specific antibodies, it was shown that the 41kD species is processed to 38kD, 33kD and finally to 28kD while the 37kD species is processed to 33kD, 30kD and finally 25kD in parallel processing pathways. These processing steps were shown to consist of stepwise cleavage events in the N-terminal half of the protein. The processing sites were mapped by CNBr mapping and by analysis of conservated cle vage sites within several Drosophila species. Finally, it was found that accessory gland main cell secretions are necessary to process Acp26Aa protein in the female genital tract.

Thought to be generated from a putative 38kD product by an N-terminal cleavage step in the female genital tract.

Antibodies were prepared against the carboxy-terminal portion of the protein (amino acids 250-264), the amino terminus (amino acids 1-64) and the middle (amino acids 76-121).

Acp26Aa protein was found to contain carbohydrates.

Acp26Aa protein contains a signal sequence and 5 pairs of basic amino acids that may be sites of specific peptidase cleavage. It is thought to be a secreted protein which is glycosylated and cleaved into smaller peptides. Results show that it is transferred to the female genital tract upon mating. One stretch of the Acp26Aa amino acid sequence is similar to the Aplysia egg-laying hormone (11 or 17 amino acids identical).

(Chapman and Wolfner, 1988)

External Data

Linkouts

Crossreferences

InterPro domains - A database of protein families, domains, and functional sites

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Male Drosophila accessory gland secretory protein (IPR004315)

Sequences Consistent with the Gene Model

DDBJ /
EMBL /
GenBank

DNA sequence

Protein sequence

Name

P10333

UniProtKB/TrEMBL

Mapped Features

Mapped Features have been reorganized, please see this article for details.

Additional mapped features and mutations can be found on GBrowse or related reports.

Type

Symbol & Location

Additional Notes

References

External Data

Linkouts

Crossreferences

EPD - Eukarytoic Promoter Database, an annotated collection of POL II promoters

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Expression Data

Transcript Expression

northern blot

Stage

Tissue/Position (including subcellular localization)

Reference

pupal stage & adult stage

adult stage | male

male accessory gland

(Chapman and Wolfner, 1988)

Additional Descriptive Data

Acp26Aa transcripts were assayed in hand-sorted staged pupae. They are first detected at pupal stage 13. They are present at adult levels by one day after eclosion and persist at these levels for at least 10 days. Determination of expression occurs during the third larval instar which correlates with the time of determination of the accessory glands.

Acp26Aa transcripts are detected in RNA from adult males and specifically in accessory gland RNA.

Marker for

Subcellular Localization

CV Term

Polypeptide Expression

No Assay Recorded

Stage

Tissue/Position (including subcellular localization)

Reference

adult stage | female

vagina

immunolocalization

Stage

Tissue/Position (including subcellular localization)

Reference

adult stage | female

vagina

adult hemolymph

adult stage | male

male accessory gland

male accessory gland main cell

male accessory gland secondary cell

adult stage | mated female

uterus

(Lee et al., 2001)

western blot

Stage

Tissue/Position (including subcellular localization)

Reference

day 7 of adulthood & male -- day 7 of adulthood & male

male reproductive system

(Lee et al., 2001)

Additional Descriptive Data

The 30kD processed form of Acp26Aa protein is the major form in the female genital tract by the end of mating.

Acp26Aa protein is not detectable in stage P13 pupae but is detectable in accessory glands dissected from adult males 3-4 hours after eclosion. Levels reach a plateau about 3-5 days after eclosion. Levels remain high in accessory gland secretions, even in 30 day old virgin males. Staining is present in both the main cells and the secondary cells. In 5 day and older virgin males, protein is absent in the main cells but is present in the secondary cells where it is concentrated in large vesicles. Abundance of Acp26Ab protein is stimula ed by copulation. Acp26Aa protein is detected in the female genital tract 10 minutes after the start of copulation as well as in the hemolymph. Levels in the hemolymph decrease with time. It is still detected at 6 hours but not at 24 hours after copulation. In the female genital tract, it is present as a 30kD processed form by the end of copulation. By 30 minutes after the end of copulation, it is found predominantly as a 25kD form. Less abundant 33kD and 28kD bands may be further processing intermediates. By 2 hours, only the 25kD form is detected. It is still detected by 3 hours but not t 4 hours after copulation. Protein was not detected in any other tissue examined. The 25kD form was shown to contain the ELH-similar region of the protein.

The 25kD processed form of Acp26Aa protein is the major form in the female genital tract 30 minutes after mating, and by 2 hours, it is the only form detected.