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P10323 (ACRO_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acrosin

EC=3.4.21.10

Cleaved into the following 2 chains:

  1. Acrosin light chain
  2. Acrosin heavy chain
Gene names
Name:ACR
Synonyms:ACRS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length421 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 a heterodimer with SERPINA5.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacrosome matrix dispersal

Non-traceable author statement PubMed 10418103. Source: UniProtKB

acrosome reaction

Inferred from mutant phenotype PubMed 2550339. Source: UniProtKB

activation of adenylate cyclase activity

Inferred from direct assay PubMed 3880736. Source: UniProtKB

binding of sperm to zona pellucida

Inferred from electronic annotation. Source: Ensembl

multicellular organism reproduction

Traceable author statement. Source: Reactome

response to steroid hormone

Inferred from electronic annotation. Source: Ensembl

single fertilization

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi-associated vesicle

Inferred from electronic annotation. Source: Ensembl

acrosomal matrix

Traceable author statement PubMed 12398221. Source: HGNC

extracellular region

Traceable author statement. Source: Reactome

protein complex

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionDNA binding

Non-traceable author statement PubMed 1937464. Source: UniProtKB

amidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

copper ion binding

Non-traceable author statement PubMed 6815104. 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 PubMed 15950652. Source: UniProtKB

serine-type endopeptidase activity

Inferred from direct assay PubMed 6802470. Source: UniProtKB

zinc ion binding

Non-traceable author statement PubMed 6815104. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Chain20 – 421402Acrosin
PRO_0000027518
Chain20 – 4223Acrosin light chain
PRO_0000027519
Chain43 – 343301Acrosin heavy chain
PRO_0000027520
Propeptide344 – 42178Pro-rich Probable
PRO_0000027521

Regions

Domain43 – 290248Peptidase S1

Sites

Active site881Charge relay system By similarity
Active site1421Charge relay system By similarity
Active site2401Charge relay system By similarity

Amino acid modifications

Glycosylation221N-linked (GlcNAc...) By similarity
Glycosylation2101N-linked (GlcNAc...) By similarity
Disulfide bond25 ↔ 154Interchain (between light and heavy chains) By similarity
Disulfide bond29 ↔ 162Interchain (between light and heavy chains) By similarity
Disulfide bond73 ↔ 89 By similarity
Disulfide bond177 ↔ 246 By similarity
Disulfide bond209 ↔ 225 By similarity
Disulfide bond236 ↔ 266 By similarity

Natural variations

Natural variant1201L → V.
Corresponds to variant rs1064734 [ dbSNP | Ensembl ].
VAR_011650
Natural variant1661F → L.
Corresponds to variant rs1064735 [ dbSNP | Ensembl ].
VAR_011651

Experimental info

Sequence conflict641T → R Ref.2
Sequence conflict641T → R Ref.4
Sequence conflict2261A → V Ref.3
Sequence conflict2681R → L Ref.2
Sequence conflict2681R → L Ref.4
Sequence conflict2961M → V in CAG30252. Ref.6
Sequence conflict3451R → P Ref.2
Sequence conflict3451R → P Ref.3
Sequence conflict3451R → P Ref.4

Sequences

Sequence LengthMass (Da)Tools
P10323 [UniParc].

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

FASTA42145,847
        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' 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]Erratum
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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PROPEPTIDE, ACTIVATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00970 mRNA. Translation: CAA68784.1.
X54017 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , X54018, X54019, X54020 Genomic DNA. Translation: CAA46956.1.
CR456366 mRNA. Translation: CAG30252.1.
PIRS11674.
RefSeqNP_001088.2. NM_001097.2.
UniGeneHs.370870.

3D structure databases

ProteinModelPortalP10323.
SMRP10323. Positions 43-301.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106565. 3 interactions.
STRING9606.ENSP00000216139.

Chemistry

BindingDBP10323.
ChEMBLCHEMBL2738.

Protein family/group databases

MEROPSS01.223.

Polymorphism databases

DMDM115502349.

Proteomic databases

PaxDbP10323.
PRIDEP10323.

Protocols and materials databases

DNASU49.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216139; ENSP00000216139; ENSG00000100312.
GeneID49.
KEGGhsa:49.
UCSCuc003bnh.4. human.

Organism-specific databases

CTD49.
GeneCardsGC22P051176.
H-InvDBHIX0041187.
HGNCHGNC:126. ACR.
HPAHPA048687.
MIM102480. gene.
neXtProtNX_P10323.
PharmGKBPA24451.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000033792.
HOVERGENHBG013304.
InParanoidP10323.
KOK01317.
OMAGIYTATW.
OrthoDBEOG75B84T.
PhylomeDBP10323.
TreeFamTF335943.

Enzyme and pathway databases

BRENDA3.4.21.10. 2681.
ReactomeREACT_163848. Reproduction.

Gene expression databases

ArrayExpressP10323.
BgeeP10323.
CleanExHS_ACR.
GenevestigatorP10323.

Family and domain databases

InterProIPR012267. Pept_S1A_acrosin.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001141. Acrosin. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
PROSITEPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAcrosin.
GenomeRNAi49.
NextBio191.
PROP10323.
SOURCESearch...

Entry information

Entry nameACRO_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 150 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

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