Q2UVH8 (ACRO_MELGA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acrosin
EC=3.4.21.10

Alternative name(s):
Proacrosin
Short name=Proacro1

Cleaved into the following 2 chains:

1. Acrosin light chain
2. Acrosin heavy chain

Gene names

Name:

ACR

Organism

Meleagris gallopavo (Common turkey) [Reference proteome]

Taxonomic identifier

9103 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Meleagridinae › Meleagris

Protein attributes

Sequence length	346 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	Serine protease of trypsin-like cleavage specificity. Synthesized in a zymogen form, proacrosin and stored in the acrosome By similarity. UniProtKB P10626
Catalytic activity	Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa. UniProtKB P10626
Enzyme regulation	Inhibited by aprotinin, ovomucoid, soybean trypsin inhibitor, benzamidine, p-aminobenzamidine, and zinc ions. Activity also inhibited by a Kazal-type proteinase inhibitor. Ref.1 Ref.3 Ref.4
Subunit structure	Heavy chain (catalytic) and a light chain linked by two disulfide bonds By similarity. UniProtKB P10323
Post-translational modification	Glycosylated. Ref.1 Ref.2
Miscellaneous	On the 2D-gel the determined pI of this protein is: 6.4. Ref.1
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.
Biophysicochemical properties	Kinetic parameters: KM=1.17 mM for N-alpha-benzoyl-DL-arginine-p-nitroanilide (at 25 degrees Celsius) Ref.3 Ref.4 Vmax=1.50 mmol/min/mg enzyme toward N-alpha-benzoyl-DL-arginine-p-nitroanilide Ref.3 pH dependence: Optimum pH is 8.0-8.5. Ref.3 Ref.4 Temperature dependence: Active between 20.0-37.0 degrees Celsius. Activity increases above 25 degrees Celsius. Ref.4
Mass spectrometry	Molecular mass is 30874 Da from positions 41 - 265. Determined by ESI. Ref.1

Ontologies

Keywords
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	Potential
	Chain	20 – 346	327	Acrosin		PRO_5000077652
	Chain	20 – 40	21	Acrosin light chain Ref.1		PRO_0000415801
	Chain	41 – 265	225	Acrosin heavy chain Ref.1 UniProtKB P10323		PRO_0000415802
	Propeptide	266 – 346	81	By similarity UniProtKB P10323		PRO_0000415803
Regions
	Domain	41 – 284	244	Peptidase S1
Sites
	Active site	85	1	Charge relay system By similarity UniProtKB Q9GL10
	Active site	134	1	Charge relay system By similarity UniProtKB Q9GL10
	Active site	234	1	Charge relay system By similarity UniProtKB Q9GL10
Amino acid modifications
	Glycosylation	128	1	N-linked (GlcNAc...) Potential
	Glycosylation	204	1	N-linked (GlcNAc...) Potential
	Disulfide bond	24 ↔ 146		Interchain (between light and heavy chains) By similarity UniProtKB Q9GL10
	Disulfide bond	27 ↔ 154		Interchain (between light and heavy chains) By similarity UniProtKB Q9GL10
	Disulfide bond	70 ↔ 86		By similarity UniProtKB Q9GL10
	Disulfide bond	168 ↔ 240		By similarity UniProtKB Q9GL10
	Disulfide bond	203 ↔ 219		By similarity UniProtKB Q9GL10
	Disulfide bond	230 ↔ 260		By similarity UniProtKB Q9GL10

Sequences

	Sequence		Length	Mass (Da)
	Q2UVH8 [UniParc]. Last modified January 24, 2006. Version 1. Checksum: FC0C38468C3310E1	FASTA	346	37,950
	10 20 30 40 50 60 MALLLPLAVL LAACRPGHGF SGGCDTCGLR PVAYHYGGMR VVGGTEALHG SWPWIVSIQN 70 80 90 100 110 120 PRFAGTGHMC GGSLITPQWV LSAAHCFGRP NYILQSRVVI GANDLTQLGQ EVEVRSIRRA 130 140 150 160 170 180 ILHEYFNNKT MINDIALLEL DRPVHCSYYI QLACVPDPSL RVSELTDCYV SGWGHMGMRS 190 200 210 220 230 240 AAPTQTAEVL QEAKVHLLDL NLCNSSHWYD GVLHSHNLCA GYPQGGIDTC QGDSGGPLMC 250 260 270 280 290 300 RDSSADYFWL VGVTSWGRGC GRAFRPGIYT STQHFYNWIL LQVRAAAHPT SRTWSHYMST 310 320 330 340 SSYHHGPNAV PTQPSVSDSC PFPAQKLREF FTGVQNLLQS LWGSKA

References

[1]	"Isolation, characterization and cDNA sequencing of acrosin from turkey spermatozoa." Slowinska M., Olczak M., Liszewska E., Watorek W., Ciereszko A. Comp. Biochem. Physiol. 157:127-136(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 41-66, ENZYME REGULATION, GLYCOSYLATION, MASS SPECTROMETRY. Tissue: Sperm and Testis.
[2]	"Turkey acrosin. I. Isolation, purification, and partial characterization." Richardson M.E., Bodine A.B., Froman D.P., Thurston R.J. Biol. Reprod. 38:645-651(1988) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION. Tissue: Sperm.
[3]	"Research note: kinetic and inhibition studies with turkey acrosin." Richardson M.E., Korn N., Bodine A.B., Thurston R.J. Poult. Sci. 71:1789-1793(1992) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Sperm.
[4]	"Acrosin activity in turkey spermatozoa: assay by clinical method and effect of zinc and benzamidine on the activity." Glogowski J., Jankowski J., Faruga A., Ottobre J.S., Ciereszko A. Theriogenology 56:889-901(2001) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Sperm.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM167974 mRNA. Translation: CAJ45027.1.
UniGene	Mga.4345.
3D structure databases
ProteinModelPortal	Q2UVH8.
ModBase	Search...
Protein family/group databases
MEROPS	S01.223.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR001254. Peptidase_S1. IPR018114. Peptidase_S1_AS. IPR001314. Peptidase_S1A. IPR009003. Trypsin-like_Pept_dom. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
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...

Entry information

Entry name

ACRO_MELGA

Accession

Primary (citable) accession number: Q2UVH8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 22, 2012
Last sequence update:	January 24, 2006
Last modified:	March 6, 2013
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program