Acrosin precursor - Homo sapiens (Human)

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P10323 (ACRO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 128. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Acrosin
EC=3.4.21.10

Gene names

Name:	ACR
Synonyms:	ACRS

Organism

Homo sapiens (Human)

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.
Enzyme regulation	Inhibited by SERPINA5. Ref.7
Subunit structure	Heavy chain (catalytic) and a light chain linked by two disulfide bonds. Forms heterodimer with SERPINA5.
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 Reference 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 Ref.7. 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 Ref.7. 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

Chain

20 – 421

402

Acrosin

PRO_0000027518

Chain

20 – 42

Acrosin light chain

PRO_0000027519

Chain

43 – 343

301

Acrosin heavy chain

PRO_0000027520

Propeptide

344 – 421

Pro-rich Probable

PRO_0000027521

Regions

Domain

43 – 290

248

Peptidase S1

Sites

Active site

Charge relay system By similarity

Active site

142

Charge relay system By similarity

Active site

240

Charge relay system By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) By similarity

Glycosylation

210

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

L → V.
Corresponds to variant rs1064734 [ dbSNP | Ensembl ].

VAR_011650

Natural variant

166

F → L.
Corresponds to variant rs1064735 [ dbSNP | Ensembl ].

VAR_011651

Experimental info

Sequence conflict

T → R Ref.2

Sequence conflict

T → R Ref.4

Sequence conflict

226

A → V Ref.3

Sequence conflict

268

R → L Ref.2

Sequence conflict

268

R → L Ref.4

Sequence conflict

296

M → V in CAG30252. Ref.6

Sequence conflict

345

R → P Ref.2

Sequence conflict

345

R → P Ref.3

Sequence conflict

345

R → P Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P10323 [UniParc].

Last modified October 3, 2006. Version 4.
Checksum: 7A2F7ECEC98008FA
Show »

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

« Hide

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:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Inhibition of acrosin by protein C inhibitor and localization of protein C inhibitor to spermatozoa." Zheng X., Geiger M., Ecke S., Bielek E., Donner P., Eberspacher U., Schleuning W.D., Binder B.R. Am. J. Physiol. 267:C466-C472(1994) [PubMed: 7521127] [Abstract] Cited for: ENZYME REGULATION, HETERODIMER WITH SERPINA5.
[8]	"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
EMBL GenBank DDBJ	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. NM_001097.2.
UniGene	Hs.370870.
3D structure databases
ProteinModelPortal	P10323.
SMR	P10323. Positions 43-301.
ModBase	Search...
Protein-protein interaction databases
STRING	P10323.
Protein family/group databases
MEROPS	S01.223.
Polymorphism databases
DMDM	115502349.
Proteomic databases
PRIDE	P10323.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000216139; ENSP00000216139; ENSG00000100312.
GeneID	49.
KEGG	hsa:49.
NMPDR	fig\|9606.3.peg.22000.
UCSC	uc003bnh.2. human.
Organism-specific databases
CTD	49.
GeneCards	GC22P051176.
H-InvDB	HIX0041187.
HGNC	HGNC:126. ACR.
MIM	102480. gene.
neXtProt	NX_P10323.
PharmGKB	PA24451.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG09746.
GeneTree	ENSGT00600000084256.
HOGENOM	HBG755338.
HOVERGEN	HBG013304.
InParanoid	P10323.
OMA	KKVYDWR.
OrthoDB	EOG4NP73V.
PhylomeDB	P10323.
Enzyme and pathway databases
BRENDA	3.4.21.10. 2681.
Gene expression databases
Bgee	P10323.
CleanEx	HS_ACR.
Genevestigator	P10323.
GermOnline	ENSG00000100312. Homo sapiens.
Family and domain databases
InterPro	IPR009003. Pept_cys/ser_Trypsin-like. IPR012267. Pept_S1A_acrosin. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
KO	K01317.
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PIRSF	PIRSF001141. Acrosin. 1 hit.
PRINTS	PR00722. CHYMOTRYPSIN.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
SUPFAM	SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
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:	January 25, 2012
This is version 128 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents