Q6HA09 (ASTL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Astacin-like metalloendopeptidase
EC=3.4.-.-

Alternative name(s):
Oocyte astacin
Ovastacin
Sperm acrosomal SLLP1-binding protein

Gene names

Name:	Astl
Synonyms:	Sas1b

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	435 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	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 vesicle › secretory 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 process	Fertilization
Cellular component	Cell membrane Cytoplasm Cytoplasmic vesicle Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion 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_component	cortical granule Inferred from direct assay Ref.7. Source: UniProtKB plasma membrane Inferred from direct assay Ref.2. Source: UniProtKB transport vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	aspartic-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 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 435	412	Astacin-like metalloendopeptidase		PRO_0000041965
Sites
	Active site	183	1	By similarity UniProtKB P07584
	Metal binding	182	1	Zinc; catalytic By similarity UniProtKB P07584
	Metal binding	186	1	Zinc; catalytic By similarity UniProtKB P07584
	Metal binding	192	1	Zinc; catalytic By similarity UniProtKB P07584
Natural variations
	Alternative sequence	1 – 21	21	Missing in isoform 2, isoform 5 and isoform 6.		VSP_051832
	Alternative sequence	72 – 105	34	Missing in isoform 4 and isoform 6.		VSP_043997
	Alternative sequence	82 – 113	32	SPFRL…SRKYD → GVSHGVSFPN in isoform 3.		VSP_043998
	Alternative sequence	82 – 112	31	SPFRL…LSRKY → GVSHGVSFP in isoform 5.		VSP_043999
Experimental info
	Sequence conflict	45	1	E → G in CAD61264. Ref.1
	Sequence conflict	115	1	L → P in CAD61264. Ref.1
	Sequence conflict	283	1	R → Q in CAD61264. Ref.1
	Sequence conflict	300	1	S → R in CAD61264. Ref.1
	Sequence conflict	309	1	R → H in CAD61264. Ref.1
	Sequence conflict	368	1	D → A in CAD61264. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (V1) [UniParc]. Last modified September 27, 2005. Version 3. Checksum: 8530CC0E5B3B1350	FASTA	435	47,455
	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
	Isoform 2 (V2) [UniParc]. Checksum: 2B8809620D02A446	FASTA	414	45,153
	10 20 30 40 50 60 MGAPSASRCS GVCSTSVPEG FTPEGSPVFQ DKDIPAINQG LISEETPESS FLVEGDIIRP 70 80 90 100 110 120 SPFRLLSVTN NKWPKGVGGF VEIPFLLSRK YDELSRRVIM DAFAEFERFT CIRFVAYHGQ 130 140 150 160 170 180 RDFVSILPMA GCFSGVGRSG GMQVVSLAPT CLRKGRGIVL HELMHVLGFW HEHSRADRDR 190 200 210 220 230 240 YIQVNWNEIL PGFEINFIKS RSTNMLVPYD YSSVMHYGRF AFSWRGQPTI IPLWTSSVHI 250 260 270 280 290 300 GQRWNLSTSD ITRVCRLYNC SRSVPDSHGR GFEAQSDGSS LTPASISRLQ RLLEALSEES 310 320 330 340 350 360 GSSAPSGSRT GGQSIAGLGN SQQGWEHPPQ STFSVGALAR PPQMLADASK SGPGAGADSL 370 380 390 400 410 SLEQFQLAQA PTVPLALFPE ARDKPAPIQD AFERLAPLPG GCAPGSHIRE VPRD
	Isoform 3 (V6) [UniParc]. Checksum: C1C54E7EF96B07D0	FASTA	413	44,789
	10 20 30 40 50 60 MGIMGSLWPW ILTMLSLLGL SMGAPSASRC SGVCSTSVPE GFTPEGSPVF QDKDIPAINQ 70 80 90 100 110 120 GLISEETPES SFLVEGDIIR PGVSHGVSFP NELSRRVIMD AFAEFERFTC IRFVAYHGQR 130 140 150 160 170 180 DFVSILPMAG CFSGVGRSGG MQVVSLAPTC LRKGRGIVLH ELMHVLGFWH EHSRADRDRY 190 200 210 220 230 240 IQVNWNEILP GFEINFIKSR STNMLVPYDY SSVMHYGRFA FSWRGQPTII PLWTSSVHIG 250 260 270 280 290 300 QRWNLSTSDI TRVCRLYNCS RSVPDSHGRG FEAQSDGSSL TPASISRLQR LLEALSEESG 310 320 330 340 350 360 SSAPSGSRTG GQSIAGLGNS QQGWEHPPQS TFSVGALARP PQMLADASKS GPGAGADSLS 370 380 390 400 410 LEQFQLAQAP TVPLALFPEA RDKPAPIQDA FERLAPLPGG CAPGSHIREV PRD
	Isoform 4 (V4) [UniParc]. Checksum: C7A87D14F4431CF9	FASTA	401	43,690
	10 20 30 40 50 60 MGIMGSLWPW ILTMLSLLGL SMGAPSASRC SGVCSTSVPE GFTPEGSPVF QDKDIPAINQ 70 80 90 100 110 120 GLISEETPES SFLLSRKYDE LSRRVIMDAF AEFERFTCIR FVAYHGQRDF VSILPMAGCF 130 140 150 160 170 180 SGVGRSGGMQ VVSLAPTCLR KGRGIVLHEL MHVLGFWHEH SRADRDRYIQ VNWNEILPGF 190 200 210 220 230 240 EINFIKSRST NMLVPYDYSS VMHYGRFAFS WRGQPTIIPL WTSSVHIGQR WNLSTSDITR 250 260 270 280 290 300 VCRLYNCSRS VPDSHGRGFE AQSDGSSLTP ASISRLQRLL EALSEESGSS APSGSRTGGQ 310 320 330 340 350 360 SIAGLGNSQQ GWEHPPQSTF SVGALARPPQ MLADASKSGP GAGADSLSLE QFQLAQAPTV 370 380 390 400 PLALFPEARD KPAPIQDAFE RLAPLPGGCA PGSHIREVPR D
	Isoform 5 (V5) [UniParc]. Checksum: A52197139D38C30B	FASTA	392	42,488
	10 20 30 40 50 60 MGAPSASRCS GVCSTSVPEG FTPEGSPVFQ DKDIPAINQG LISEETPESS FLVEGDIIRP 70 80 90 100 110 120 GVSHGVSFPD ELSRRVIMDA FAEFERFTCI RFVAYHGQRD FVSILPMAGC FSGVGRSGGM 130 140 150 160 170 180 QVVSLAPTCL RKGRGIVLHE LMHVLGFWHE HSRADRDRYI QVNWNEILPG FEINFIKSRS 190 200 210 220 230 240 TNMLVPYDYS SVMHYGRFAF SWRGQPTIIP LWTSSVHIGQ RWNLSTSDIT RVCRLYNCSR 250 260 270 280 290 300 SVPDSHGRGF EAQSDGSSLT PASISRLQRL LEALSEESGS SAPSGSRTGG QSIAGLGNSQ 310 320 330 340 350 360 QGWEHPPQST FSVGALARPP QMLADASKSG PGAGADSLSL EQFQLAQAPT VPLALFPEAR 370 380 390 DKPAPIQDAF ERLAPLPGGC APGSHIREVP RD
	Isoform 6 (V3) [UniParc]. Checksum: B5C5B37A8C5DD84E	FASTA	380	41,388
	10 20 30 40 50 60 MGAPSASRCS GVCSTSVPEG FTPEGSPVFQ DKDIPAINQG LISEETPESS FLLSRKYDEL 70 80 90 100 110 120 SRRVIMDAFA EFERFTCIRF VAYHGQRDFV SILPMAGCFS GVGRSGGMQV VSLAPTCLRK 130 140 150 160 170 180 GRGIVLHELM HVLGFWHEHS RADRDRYIQV NWNEILPGFE INFIKSRSTN MLVPYDYSSV 190 200 210 220 230 240 MHYGRFAFSW RGQPTIIPLW TSSVHIGQRW NLSTSDITRV CRLYNCSRSV PDSHGRGFEA 250 260 270 280 290 300 QSDGSSLTPA SISRLQRLLE ALSEESGSSA PSGSRTGGQS IAGLGNSQQG WEHPPQSTFS 310 320 330 340 350 360 VGALARPPQM LADASKSGPG AGADSLSLEQ FQLAQAPTVP LALFPEARDK PAPIQDAFER 370 380 LAPLPGGCAP GSHIREVPRD

References

	« Hide 'large scale' referencesShow '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, 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. , 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. , 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 September2012

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.
IPI	IPI00283246. IPI00621570.
RefSeq	NP_766127.1. NM_172539.2.
UniGene	Mm.31313. Mm.58214.
3D structure databases
ProteinModelPortal	Q6HA09.
SMR	Q6HA09. Positions 40-322.
ModBase	Search...
Protein family/group databases
MEROPS	M12.245.
PTM databases
PhosphoSite	Q6HA09.
Proteomic databases
PRIDE	Q6HA09.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000059839; ENSMUSP00000054456; ENSMUSG00000050468. ENSMUST00000089673; ENSMUSP00000087102; ENSMUSG00000050468. ENSMUST00000179618; ENSMUSP00000135987; ENSMUSG00000050468.
GeneID	215095.
KEGG	mmu:215095.
UCSC	uc008mfg.1. mouse. uc029uen.1. mouse.
Organism-specific databases
CTD	431705.
MGI	MGI:3046414. Astl.
Phylogenomic databases
eggNOG	NOG330389.
GeneTree	ENSGT00550000074269.
HOGENOM	HOG000231483.
HOVERGEN	HBG080299.
InParanoid	Q6HA09.
KO	K08778.
OMA	IRFVAYQ.
OrthoDB	EOG4QZ7MW.
Gene expression databases
ArrayExpress	Q6HA09.
Bgee	Q6HA09.
CleanEx	MM_ASTL.
Genevestigator	Q6HA09.
GermOnline	ENSMUSG00000050468. Mus musculus.
Family and domain databases
Gene3D	3.40.390.10. 1 hit.
InterPro	IPR024079. MetalloPept_cat_dom. IPR001506. Peptidase_M12A. IPR006026. Peptidase_Metallo. [Graphical view]
Pfam	PF01400. Astacin. 1 hit. [Graphical view]
PRINTS	PR00480. ASTACIN.
SMART	SM00235. ZnMc. 1 hit. [Graphical view]
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	374608.
SOURCE	Search...

Entry information

Entry name

ASTL_MOUSE

Accession

Primary (citable) accession number: Q6HA09
Secondary accession number(s): A2AHU0 , A2AHU1, G7Z016, G7Z017, G7Z018, G7Z019, Q8BMA1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2005
Last sequence update:	September 27, 2005
Last modified:	May 29, 2013
This is version 79 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program