HUMAN:ACRO

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	ACR (synonyms: ACRS)
Protein Name(s)	Acrosin Acrosin light chain Acrosin heavy chain
External Links
UniProt	P10323
EMBL	Y00970 X54017 X54018 X54019 X54020 M77378 M77379 M77380 M77381 X66188 X54018 X54019 X54020 CR456366
CCDS	CCDS14101.1
PIR	S11674
RefSeq	NP_001088.2
UniGene	Hs.370870
ProteinModelPortal	P10323
SMR	P10323
BioGrid	106565
STRING	9606.ENSP00000216139
BindingDB	P10323
ChEMBL	CHEMBL2738
MEROPS	S01.223
DMDM	115502349
PaxDb	P10323
PRIDE	P10323
DNASU	49
Ensembl	ENST00000216139
GeneID	49
KEGG	hsa:49
UCSC	uc003bnh.4
CTD	49
GeneCards	GC22P051176
H-InvDB	HIX0041187
HGNC	HGNC:126
HPA	HPA048687
MIM	102480
neXtProt	NX_P10323
PharmGKB	PA24451
eggNOG	COG5640
GeneTree	ENSGT00770000120515
HOGENOM	HOG000033792
HOVERGEN	HBG013304
InParanoid	P10323
KO	K01317
OMA	KKVYDWR
OrthoDB	EOG75B84T
PhylomeDB	P10323
TreeFam	TF335943
BRENDA	3.4.21.10
Reactome	REACT_163938
GeneWiki	Acrosin
GenomeRNAi	49
NextBio	191
PRO	PR:P10323
Proteomes	UP000005640
Bgee	P10323
CleanEx	HS_ACR
ExpressionAtlas	P10323
Genevestigator	P10323
GO	GO:0043159 GO:0005576 GO:0005798 GO:0005634 GO:0043234 GO:0004040 GO:0005507 GO:0003677 GO:0008144 GO:0042806 GO:0005537 GO:0004252 GO:0008270 GO:0002077 GO:0007340 GO:0007190 GO:0007339 GO:0032504 GO:0048545 GO:0007338
InterPro	IPR012267 IPR001254 IPR018114 IPR001314 IPR009003
Pfam	PF00089
PIRSF	PIRSF001141
PRINTS	PR00722
SMART	SM00020
SUPFAM	SSF50494
PROSITE	PS50240 PS00134 PS00135

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
part_of	GO:0005634	nucleus	PMID:21630459^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000019)	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:7521127^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042806	fucose binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P08001	F		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:6815104^[3]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008144	drug binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P08001	F		Seeded From UniProt	complete
involved_in	GO:0007340	acrosome reaction	PMID:2550339^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007338	single fertilization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P23578	P		Seeded From UniProt	complete
involved_in	GO:0007190	activation of adenylate cyclase activity	PMID:3880736^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005537	mannose binding	PMID:15950652^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005507	copper ion binding	PMID:6815104^[3]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	PMID:6802470^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004040	amidase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P08001	F		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	PMID:1937464^[8]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0002077	acrosome matrix dispersal	PMID:10418103^[9]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007340	acrosome reaction	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000665983 UniProtKB:P10323	P		Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	PMID:21873635^[10]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000665983 UniProtKB:P10323	F		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23578 ensembl:ENSMUSP00000023295	F		Seeded From UniProt	complete
involved_in	GO:0007341	penetration of zona pellucida	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23578 ensembl:ENSMUSP00000023295	P		Seeded From UniProt	complete
involved_in	GO:0007339	binding of sperm to zona pellucida	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23578 ensembl:ENSMUSP00000023295	P		Seeded From UniProt	complete
involved_in	GO:0007338	single fertilization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23578 ensembl:ENSMUSP00000023295	P		Seeded From UniProt	complete
part_of	GO:0001669	acrosomal vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P23578 ensembl:ENSMUSP00000023295	C		Seeded From UniProt	complete
involved_in	GO:0048545	response to steroid hormone	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P29293 ensembl:ENSRNOP00000046900	P		Seeded From UniProt	complete
involved_in	GO:0030163	protein catabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P29293 ensembl:ENSRNOP00000046900	P		Seeded From UniProt	complete
involved_in	GO:0007341	penetration of zona pellucida	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P29293 ensembl:ENSRNOP00000046900	P		Seeded From UniProt	complete
part_of	GO:0005798	Golgi-associated vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P29293 ensembl:ENSRNOP00000046900	C		Seeded From UniProt	complete
involved_in	GO:0002077	acrosome matrix dispersal	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P29293 ensembl:ENSRNOP00000046900	P		Seeded From UniProt	complete
part_of	GO:0001669	acrosomal vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P29293 ensembl:ENSRNOP00000046900	C		Seeded From UniProt	complete
part_of	GO:0001669	acrosomal vesicle	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012267	C		Seeded From UniProt	complete
enables	GO:0004252	serine-type endopeptidase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001254 InterPro:IPR001314 InterPro:IPR012267 InterPro:IPR018114	F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001254 InterPro:IPR001314 InterPro:IPR018114	P		Seeded From UniProt	complete
part_of	GO:0043159	acrosomal matrix	PMID:12398221^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0007340	acrosome reaction	Reactome:R-HSA-1300645	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-1297354 Reactome:R-HSA-1297333	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0002020	protease binding	Reactome:R-HSA-1297354	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008233	peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0645	P		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
enables	GO:0008236	serine-type peptidase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0720	F		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ de Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page
↑ Zheng, X et al. (1994) Inhibition of acrosin by protein C inhibitor and localization of protein C inhibitor to spermatozoa. Am. J. Physiol. 267 C466-72 PubMed GONUTS page
↑ ^3.0 ^3.1 Steven, FS et al. (1982) Inhibition of human and bovine sperm acrosin by divalent metal ions. Possible role of zinc as a regulator of acrosin activity. Int. J. Androl. 5 401-12 PubMed GONUTS page
↑ De Jonge, CJ et al. (1989) Inhibition of the human sperm acrosome reaction by proteinase inhibitors. Gamete Res 23 387-97 PubMed GONUTS page
↑ Johnson, RA et al. (1985) Extraction of the adenylate cyclase-activating factor of bovine sperm and its identification as a trypsin-like protease. J. Biol. Chem. 260 114-21 PubMed GONUTS page
↑ Furlong, LI et al. (2005) Binding of recombinant human proacrosin/acrosin to zona pellucida glycoproteins. II. Participation of mannose residues in the interaction. Fertil. Steril. 83 1791-6 PubMed GONUTS page
↑ Elce, JS & McIntyre, EJ (1982) Purification of bovine and human acrosin. Can. J. Biochem. 60 8-14 PubMed GONUTS page
↑ Klemm, U et al. (1991) Acrosin, the peculiar sperm-specific serine protease. Hum. Genet. 87 635-41 PubMed GONUTS page
↑ Moreno, RD et al. (1999) Functional interactions between sulphated polysaccharides and proacrosin: implications in sperm binding and digestion of zona pellucida. Zygote 7 105-11 PubMed GONUTS page
↑ ^10.0 ^10.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Honda, A et al. () Role of acrosomal matrix proteases in sperm-zona pellucida interactions. Hum. Reprod. Update 8 405-12 PubMed GONUTS page

[PMID:21630459-1] Mateo, S et al. (2011) Proteomic characterization of the human sperm nucleus. Proteomics 11 2714-26 PubMed GONUTS page

[PMID:7521127-2] Zheng, X et al. (1994) Inhibition of acrosin by protein C inhibitor and localization of protein C inhibitor to spermatozoa. Am. J. Physiol. 267 C466-72 PubMed GONUTS page

[PMID:6815104-3] 3.0 ^3.1 Steven, FS et al. (1982) Inhibition of human and bovine sperm acrosin by divalent metal ions. Possible role of zinc as a regulator of acrosin activity. Int. J. Androl. 5 401-12 PubMed GONUTS page

[PMID:2550339-4] De Jonge, CJ et al. (1989) Inhibition of the human sperm acrosome reaction by proteinase inhibitors. Gamete Res 23 387-97 PubMed GONUTS page

[PMID:3880736-5] Johnson, RA et al. (1985) Extraction of the adenylate cyclase-activating factor of bovine sperm and its identification as a trypsin-like protease. J. Biol. Chem. 260 114-21 PubMed GONUTS page

[PMID:15950652-6] Furlong, LI et al. (2005) Binding of recombinant human proacrosin/acrosin to zona pellucida glycoproteins. II. Participation of mannose residues in the interaction. Fertil. Steril. 83 1791-6 PubMed GONUTS page

[PMID:6802470-7] Elce, JS & McIntyre, EJ (1982) Purification of bovine and human acrosin. Can. J. Biochem. 60 8-14 PubMed GONUTS page

[PMID:1937464-8] Klemm, U et al. (1991) Acrosin, the peculiar sperm-specific serine protease. Hum. Genet. 87 635-41 PubMed GONUTS page

[PMID:10418103-9] Moreno, RD et al. (1999) Functional interactions between sulphated polysaccharides and proacrosin: implications in sperm binding and digestion of zona pellucida. Zygote 7 105-11 PubMed GONUTS page

[PMID:21873635-10] 10.0 ^10.1 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:12398221-11] Honda, A et al. () Role of acrosomal matrix proteases in sperm-zona pellucida interactions. Hum. Reprod. Update 8 405-12 PubMed GONUTS page

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HUMAN:ACRO

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