Reviewed, UniProtKB/Swiss-Prot P10323 (ACRO_HUMAN)

Names and origin

Protein names

Recommended name:
    Acrosin
    EC=3.4.21.10
Cleaved into the following 2 chains:
    1- Recommended name:
            Acrosin light chain
    2- Recommended name:
            Acrosin heavy chain

Gene names

Name:	ACR
Synonyms:	ACRS

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	421 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Acrosin is the major protease of mammalian spermatozoa. It is a serine protease of trypsin-like cleavage specificity, it is synthesized in a zymogen form, proacrosin and stored in the acrosome.
Catalytic activity	Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
Subunit structure	Heavy chain (catalytic) and a light chain linked by two disulfide bonds.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	acrosome matrix dispersal Non-traceable author statement. Source: UniProtKB activation of adenylate cyclase activity Inferred from direct assay. Source: UniProtKB
Cellular component	acrosomal matrix Traceable author statement. Source: HGNC protein complex Inferred from direct assay. Source: UniProtKB
Molecular function	DNA binding Non-traceable author statement. Source: UniProtKB amidase activity Inferred from sequence or structural similarity. Source: UniProtKB copper ion binding Non-traceable author statement. Source: UniProtKB drug binding Inferred from sequence or structural similarity. Source: UniProtKB fucose binding Inferred from sequence or structural similarity. Source: UniProtKB mannose binding Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB serine-type endopeptidase activity Inferred from direct assay. Source: UniProtKB zinc ion binding Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19
	Chain	20 – 421	402	Acrosin		PRO_0000027518
	Chain	20 – 42	23	Acrosin light chain		PRO_0000027519
	Chain	43 – 343	301	Acrosin heavy chain		PRO_0000027520
	Propeptide	344 – 421	78	Pro-rich Probable		PRO_0000027521
Regions
	Domain	43 – 290	248	Peptidase S1
Sites
	Active site	88	1	Charge relay system By similarity
	Active site	142	1	Charge relay system By similarity
	Active site	240	1	Charge relay system By similarity
Amino acid modifications
	Glycosylation	22	1	N-linked (GlcNAc...) By similarity
	Glycosylation	210	1	N-linked (GlcNAc...) By similarity
	Disulfide bond	25 ↔ 154		Interchain (between light and heavy chains) By similarity
	Disulfide bond	29 ↔ 162		Interchain (between light and heavy chains) By similarity
	Disulfide bond	73 ↔ 89		By similarity
	Disulfide bond	177 ↔ 246		By similarity
	Disulfide bond	209 ↔ 225		By similarity
	Disulfide bond	236 ↔ 266		By similarity
Natural variations
	Natural variant	120	1	L → V: dbSNP rs1064734.		VAR_011650
	Natural variant	166	1	F → L: dbSNP rs1064735.		VAR_011651
Experimental info
	Sequence conflict	64	1	T → R Ref.2
	Sequence conflict	64	1	T → R Ref.4
	Sequence conflict	226	1	A → V Ref.3
	Sequence conflict	268	1	R → L Ref.2
	Sequence conflict	268	1	R → L Ref.4
	Sequence conflict	296	1	M → V in CAG30252. Ref.6
	Sequence conflict	345	1	R → P Ref.2
	Sequence conflict	345	1	R → P Ref.3
	Sequence conflict	345	1	R → P Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P10323-1 [UniParc]. Last modified October 3, 2006. Version 4. Checksum: 7A2F7ECEC98008FA	FASTA	421	45,847
	10 20 30 40 50 60 MVEMLPTAIL LVLAVSVVAK DNATCDGPCG LRFRQNPQGG VRIVGGKAAQ HGAWPWMVSL 70 80 90 100 110 120 QIFTYNSHRY HTCGGSLLNS RWVLTAAHCF VGKNNVHDWR LVFGAKEITY GNNKPVKAPL 130 140 150 160 170 180 QERYVEKIII HEKYNSATEG NDIALVEITP PISCGRFIGP GCLPHFKAGL PRGSQSCWVA 190 200 210 220 230 240 GWGYIEEKAP RPSSILMEAR VDLIDLDLCN STQWYNGRVQ PTNVCAGYPV GKIDTCQGDS 250 260 270 280 290 300 GGPLMCKDSK ESAYVVVGIT SWGVGCARAK RPGIYTATWP YLNWIASKIG SNALRMIQSA 310 320 330 340 350 360 TPPPPTTRPP PIRPPFSHPI SAHLPWYFQP PPRPLPPRPP AAQPRPPPSP PPPPPPPASP 370 380 390 400 410 420 LPPPPPPPPP TPSSTTKLPQ GLSFAKRLQQ LIEVLKGKTY SDGKNHYDME TTELPELTST S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of human proacrosin deduced from its cDNA sequence." Baba T., Watanabe K., Kashiwabara S., Arai Y. FEBS Lett. 244:296-300(1989) [PubMed: 2493394] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[2]	"Nucleotide sequence and exon-intron organization of the human proacrosin gene." Keime S., Adham I.M., Engel W. Eur. J. Biochem. 190:195-200(1990) [PubMed: 2114285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Leukocyte.
[3]	"Molecular cloning of human preproacrosin cDNA." Adham I.M., Klemm U., Maier W.-M., Engel W. Hum. Genet. 84:125-128(1990) [PubMed: 2298447] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Molecular cloning, sequencing and restriction mapping of the genomic sequence encoding human proacrosin." Vazquez-Levin M.H., Reventos J., Gordon J.W. Eur. J. Biochem. 207:23-26(1992) [PubMed: 1628652] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	Adham I.M., Spitzer U., Schloesser M., Kremling H., Keime S., Engel W. Eur. J. Biochem. 207:27-28(1992) Cited for: DISCUSSION OF PUBMED:1628652.
[6]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Evaluation of the proacrosin/acrosin system and its mechanism of activation in human sperm extracts." Zahn A., Furlong L.I., Biancotti J.C., Ghiringhelli P.D., Marijn-Briggiler C.I., Vazquez-Levin M.H. J. Reprod. Immunol. 54:43-63(2002) [PubMed: 11839395] [Abstract] Cited for: PROPEPTIDE, ACTIVATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y00970 mRNA. Translation: CAA68784.1. X54017 , X54018, X54019, X54020 Genomic DNA. Translation: CAA37964.1. M77378 Genomic DNA. Translation: AAA51572.1. M77379 Genomic DNA. Translation: AAA51573.1. M77380 Genomic DNA. Translation: AAA51574.1. M77381 Genomic DNA. Translation: AAA51575.1. X66188 , X54018, X54019, X54020 Genomic DNA. Translation: CAA46956.1. CR456366 mRNA. Translation: CAG30252.1.
IPI	IPI00289614.
PIR	S11674.
RefSeq	NP_001088.2.
UniGene	Hs.370870
3D structure databases
HSSP	HSSP built from PDB template 1FIZ based on UniProtKB P08001.
SMR	P10323. Positions 43-301.
ModBase	Search...
Protein-protein interaction databases
STRING	P10323.
Protein family/group databases
MEROPS	S01.223.
Proteomic databases
PRIDE	P10323.
Genome annotation databases
Ensembl	ENST00000216139; ENSP00000216139; ENSG00000100312; Homo sapiens. [Genome view]
GeneID	49.
KEGG	hsa:49.
NMPDR	fig|9606.3.peg.22000.
UCSC	uc003bnh.2. human.
Organism-specific databases
CTD	49.
GeneCards	GC22P049466.
HGNC	HGNC:126. ACR.
MIM	102480. gene.
PharmGKB	PA24451.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P10323.
HOVERGEN	P10323.
OMA	GLRFRQN.
Enzyme and pathway databases
BRENDA	3.4.21.10. 247.
Gene expression databases
Bgee	P10323.
CleanEx	HS_ACR.
Genevestigator	P10323.
GermOnline	ENSG00000100312. Homo sapiens.
Family and domain databases
InterPro	IPR012267. Pept_S1A_acrosin. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
PANTHER	PTHR19355:SF158. Pept_S1A_acrosin. 1 hit.
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PIRSF	PIRSF001141. Acrosin. 1 hit.
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	191.
SOURCE	Search...

Entry information

Entry name

ACRO_HUMAN

Accession

Primary (citable) accession number: P10323
Secondary accession number(s): Q6ICK2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 3, 2006
Last modified:	November 3, 2009
This is version 110 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.