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Q6HA09 (ASTL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Astacin-like metalloendopeptidase

EC=3.4.-.-
Alternative name(s):
Oocyte astacin
Ovastacin
Sperm acrosomal SLLP1-binding protein
Gene names
Name:Astl
Synonyms:Sas1b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length435 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Oocyte-specific oolemmal receptor involved in sperm and egg adhesion and fertilization. Plays a role in the polyspermy inhibition. Probably acts as a protease for the post-fertilization cleavage of ZP2. Cleaves the sperm-binding ZP2 at the surface of the zona pellucida after fertilization and cortical granule exocytosis, rendering the zona pellucida unable to support further sperm binding. Ref.2 Ref.7

Enzyme regulation

Inhibited by wide spectrum metalloproteinase inhibitor batimastat (BB-94). Also inhibited by EDTA By similarity. UniProtKB Q6HA08

Subunit structure

Interacts (via N-terminus domain) with SPACA3; the interaction occurs during fertilization. Ref.2

Subcellular location

Cytoplasm. Cell membrane. Cytoplasmic granule. Cytoplasmic vesiclesecretory vesicle. Note: Secretory granules. Localizes to the peripheral cortical granules of ovulated eggs. Probably exocytosed from cortical granules during post-fertilization. Detected throughout the ooplasm of germinal vesicle stage oocytes in early bilaminar secondary follicles at postnatal (PN) day 3. Detected in the microvillar domain of the oolemma in arrested ovulated secondary oocytes and in the first polar body prior to fertilization. Upon fertilization, detected in the perivitelline space (PVS) and occasionally on the oolemma in 2-cell through morulae stages. Colocalizes with SPACA3 at the microvillar domain of the oolemma and in the perivitelline space (PVS). Ref.2 Ref.7

Tissue specificity

Ovary-specific. Expressed in secondary, antral and Graafian follicle oocytes. Expressed in the egg cells. Not detected in two-cell embryos. Not detected in naked oocytes, oocytes in primordial or unilaminar primary follicles, or in any other ovarian cells at pre-pubertal, pubertal or adult stages (at protein level). Ovary-specific. Ref.2 Ref.7

Developmental stage

Expressed in embryonic stem cells. Highly expressed in unfertilized oocytes. Upon fertilization, expression drops to undetectable levels, although at 1.5 dpc a significant amount of ovastacin RNA could still be detected. Not detected from 1.5 dpc to implantation of the embryo. Ref.1 Ref.6

Induction

Up-regulated by superovulation. Ref.1

Disruption phenotype

Absence of cortical granules exocytosis during post-fertilization. Multiple capacitated sperm binding to eggs and two-cell embryos are not prevented. Post-fertilization cleavage of ZP2 does not occur. Ref.2 Ref.7

Sequence similarities

Belongs to the peptidase M12A family.

Ontologies

Keywords
   Biological processFertilization
   Cellular componentCell membrane
Cytoplasm
Cytoplasmic vesicle
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMZymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion

Inferred from mutant phenotype Ref.2. Source: UniProtKB

fertilization

Inferred from mutant phenotype Ref.2. Source: UniProtKB

negative regulation of binding of sperm to zona pellucida

Inferred from direct assay Ref.7. Source: UniProtKB

positive regulation of protein processing

Inferred from direct assay Ref.7. Source: UniProtKB

prevention of polyspermy

Inferred from direct assay Ref.7. Source: UniProtKB

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcortical granule

Inferred from direct assay Ref.7. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.2. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.2. Source: UniProtKB

transport vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaspartic-type peptidase activity

Inferred from direct assay Ref.7. Source: UniProtKB

glutamic-type peptidase activity

Inferred from direct assay Ref.7. Source: UniProtKB

metalloendopeptidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

peptidase activity

Inferred from direct assay Ref.2. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q6HA09-1)

Also known as: V1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q6HA09-2)

Also known as: V2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q6HA09-3)

Also known as: V6;

The sequence of this isoform differs from the canonical sequence as follows:
     82-113: SPFRLLSVTNNKWPKGVGGFVEIPFLLSRKYD → GVSHGVSFPN
Isoform 4 (identifier: Q6HA09-4)

Also known as: V4;

The sequence of this isoform differs from the canonical sequence as follows:
     72-105: Missing.
Isoform 5 (identifier: Q6HA09-5)

Also known as: V5;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
     82-112: SPFRLLSVTNNKWPKGVGGFVEIPFLLSRKY → GVSHGVSFP
Isoform 6 (identifier: Q6HA09-6)

Also known as: V3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
     72-105: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 435412Astacin-like metalloendopeptidase
PRO_0000041965

Sites

Active site1831 By similarity UniProtKB P07584
Metal binding1821Zinc; catalytic By similarity UniProtKB P07584
Metal binding1861Zinc; catalytic By similarity UniProtKB P07584
Metal binding1921Zinc; catalytic By similarity UniProtKB P07584

Natural variations

Alternative sequence1 – 2121Missing in isoform 2, isoform 5 and isoform 6.
VSP_051832
Alternative sequence72 – 10534Missing in isoform 4 and isoform 6.
VSP_043997
Alternative sequence82 – 11332SPFRL…SRKYD → GVSHGVSFPN in isoform 3.
VSP_043998
Alternative sequence82 – 11231SPFRL…LSRKY → GVSHGVSFP in isoform 5.
VSP_043999

Experimental info

Sequence conflict451E → G in CAD61264. Ref.1
Sequence conflict1151L → P in CAD61264. Ref.1
Sequence conflict2831R → Q in CAD61264. Ref.1
Sequence conflict3001S → R in CAD61264. Ref.1
Sequence conflict3091R → H in CAD61264. Ref.1
Sequence conflict3681D → A in CAD61264. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (V1) [UniParc].

Last modified September 27, 2005. Version 3.
Checksum: 8530CC0E5B3B1350

FASTA43547,455
        10         20         30         40         50         60 
MGIMGSLWPW ILTMLSLLGL SMGAPSASRC SGVCSTSVPE GFTPEGSPVF QDKDIPAINQ 

        70         80         90        100        110        120 
GLISEETPES SFLVEGDIIR PSPFRLLSVT NNKWPKGVGG FVEIPFLLSR KYDELSRRVI 

       130        140        150        160        170        180 
MDAFAEFERF TCIRFVAYHG QRDFVSILPM AGCFSGVGRS GGMQVVSLAP TCLRKGRGIV 

       190        200        210        220        230        240 
LHELMHVLGF WHEHSRADRD RYIQVNWNEI LPGFEINFIK SRSTNMLVPY DYSSVMHYGR 

       250        260        270        280        290        300 
FAFSWRGQPT IIPLWTSSVH IGQRWNLSTS DITRVCRLYN CSRSVPDSHG RGFEAQSDGS 

       310        320        330        340        350        360 
SLTPASISRL QRLLEALSEE SGSSAPSGSR TGGQSIAGLG NSQQGWEHPP QSTFSVGALA 

       370        380        390        400        410        420 
RPPQMLADAS KSGPGAGADS LSLEQFQLAQ APTVPLALFP EARDKPAPIQ DAFERLAPLP 

       430 
GGCAPGSHIR EVPRD 

« Hide

Isoform 2 (V2) [UniParc].

Checksum: 2B8809620D02A446
Show »

FASTA41445,153
Isoform 3 (V6) [UniParc].

Checksum: C1C54E7EF96B07D0
Show »

FASTA41344,789
Isoform 4 (V4) [UniParc].

Checksum: C7A87D14F4431CF9
Show »

FASTA40143,690
Isoform 5 (V5) [UniParc].

Checksum: A52197139D38C30B
Show »

FASTA39242,488
Isoform 6 (V3) [UniParc].

Checksum: B5C5B37A8C5DD84E
Show »

FASTA38041,388

References

« Hide 'large scale' references
[1]"Identification and characterization of human and mouse ovastacin, a novel metalloproteinase similar to hatching enzymes from arthropods, birds, amphibians, and fish."
Quesada V., Sanchez J., Alvarez J., Lopez-Otin C.
J. Biol. Chem. 279:26627-26634(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, DEVELOPMENTAL STAGE.
Strain: C57BL/6J.
Tissue: Ovary.
[2]"Oocyte specific oolemmal SAS1B involved in sperm binding through intra-acrosomal SLLP1 during fertilization."
Sachdev M., Mandal A., Mulders S., Digilio L.C., Panneerdoss S., Suryavathi V., Pires E., Klotz K.L., Hermens L., Herrero M.B., Flickinger C.J., van Duin M., Herr J.C.
Dev. Biol. 363:40-51(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), FUNCTION IN FERTILIZATION, TOPOLOGY, ENZYME ACTIVITY, INTERACTION WITH SPACA3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Swiss Webster.
Tissue: Ovary.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Egg.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Egg.
[6]"Astacin-like metallo-endopeptidase is dynamically expressed in embryonic stem cells and embryonic epithelium during morphogenesis."
Acloque H., Lavial F., Pain B.
Dev. Dyn. 241:574-582(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[7]"Ovastacin, a cortical granule protease, cleaves ZP2 in the zona pellucida to prevent polyspermy."
Burkart A.D., Xiong B., Baibakov B., Jimenez-Movilla M., Dean J.
J. Cell Biol. 197:37-44(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN POLYSPERMY INHIBITION, CLEAVAGE OF ZP2, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.

Web resources

Protein Spotlight

Life's boundaries - Issue 141 of September 2012

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ537599 mRNA. Translation: CAD61264.2.
FJ187790 mRNA. Translation: ACN71160.1.
FJ187791 mRNA. Translation: ACN71161.1.
FJ187792 mRNA. Translation: ACN71162.1.
FJ187793 mRNA. Translation: ACN71163.1.
FJ187794 mRNA. Translation: ACN71164.1.
FJ187795 mRNA. Translation: ACN71165.1.
AK033037 mRNA. Translation: BAC28134.1.
AL731836, AL845368 Genomic DNA. Translation: CAM13879.1.
AL731836, AL845368 Genomic DNA. Translation: CAM13880.1.
AL845368, AL731836 Genomic DNA. Translation: CAM17447.1.
AL845368, AL731836 Genomic DNA. Translation: CAM17448.1.
BC064729 mRNA. Translation: AAH64729.2.
RefSeqNP_766127.1. NM_172539.2.
XP_006499185.1. XM_006499122.1.
UniGeneMm.31313.
Mm.58214.

3D structure databases

ProteinModelPortalQ6HA09.
SMRQ6HA09. Positions 40-322.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM12.245.

PTM databases

PhosphoSiteQ6HA09.

Proteomic databases

PRIDEQ6HA09.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000059839; ENSMUSP00000054456; ENSMUSG00000050468. [Q6HA09-2]
ENSMUST00000089673; ENSMUSP00000087102; ENSMUSG00000050468. [Q6HA09-1]
ENSMUST00000179618; ENSMUSP00000135987; ENSMUSG00000050468. [Q6HA09-2]
GeneID215095.
KEGGmmu:215095.
UCSCuc008mfg.1. mouse. [Q6HA09-1]

Organism-specific databases

CTD431705.
MGIMGI:3046414. Astl.

Phylogenomic databases

eggNOGNOG330389.
GeneTreeENSGT00740000115263.
HOGENOMHOG000231483.
HOVERGENHBG080299.
InParanoidQ6HA09.
KOK08778.
OMARWNLSAS.
OrthoDBEOG73V6MT.
PhylomeDBQ6HA09.
TreeFamTF315280.

Gene expression databases

BgeeQ6HA09.
CleanExMM_ASTL.
GenevestigatorQ6HA09.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR024079. MetalloPept_cat_dom.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
[Graphical view]
PfamPF01400. Astacin. 1 hit.
[Graphical view]
PRINTSPR00480. ASTACIN.
SMARTSM00235. ZnMc. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio374608.
PROQ6HA09.
SOURCESearch...

Entry information

Entry nameASTL_MOUSE
AccessionPrimary (citable) accession number: Q6HA09
Secondary accession number(s): A2AHU0 expand/collapse secondary AC list , A2AHU1, G7Z016, G7Z017, G7Z018, G7Z019, Q8BMA1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: September 27, 2005
Last modified: April 16, 2014
This is version 86 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot