P08001 (ACRO_PIG) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acrosin
EC=3.4.21.10

Alternative name(s):
53 kDa fucose-binding protein

Cleaved into the following 2 chains:

1. Acrosin light chain
2. Acrosin heavy chain

Gene names

Name:

ACR

Organism

Sus scrofa (Pig) [Complete proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	415 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	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 By similarity.
Subunit structure	Heavy chain (catalytic) and a light chain linked by two disulfide bonds. Forms heterodimer with SERPINA5 By similarity.
Sequence similarities	Belongs to the peptidase S1 family. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Domain	Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	acrosome reaction Inferred from sequence or structural similarity. Source: UniProtKB activation of adenylate cyclase activity Inferred from sequence or structural similarity. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	acrosomal matrix Non-traceable author statement. Source: UniProtKB protein complex Inferred from direct assay. Source: UniProtKB
Molecular function	amidase activity Inferred from mutant phenotype. Source: UniProtKB drug binding Inferred from direct assay. Source: UniProtKB fucose binding Inferred from direct assay. Source: UniProtKB mannose binding Inferred from sequence or structural similarity. Source: UniProtKB protein binding Inferred from physical interaction. Source: UniProtKB serine-type endopeptidase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Ref.4 Ref.6 Ref.7

Chain

17 – 415

399

Acrosin

PRO_0000027526

Chain

17 – 39

23

Acrosin light chain

PRO_0000027527

Chain

40 – 338

299

Acrosin heavy chain

PRO_0000027528

Propeptide

339 – 415

77

Pro-rich

PRO_0000027529

Regions

Domain

40 – 288

249

Peptidase S1

Sites

Active site

86

1

Charge relay system By similarity

Active site

140

1

Charge relay system By similarity

Active site

238

1

Charge relay system By similarity

Amino acid modifications

Glycosylation

19

1

N-linked (GlcNAc...) Ref.8

Glycosylation

208

1

N-linked (GlcNAc...) Ref.8

Disulfide bond

22 ↔ 152

Interchain (between light and heavy chains) Ref.8

Disulfide bond

26 ↔ 160

Interchain (between light and heavy chains) Ref.8

Disulfide bond

71 ↔ 87

Ref.8

Disulfide bond

175 ↔ 244

Ref.8

Disulfide bond

207 ↔ 223

Ref.8

Disulfide bond

234 ↔ 264

Ref.8

Experimental info

Sequence conflict

8

1

Missing in CAA32948. Ref.2

Sequence conflict

211

1

R → Q in CAA32948. Ref.2

Sequence conflict

217 – 218

2

IR → VT in CAA32948. Ref.2

Sequence conflict

347

1

A → P in AAA31131. Ref.1

Sequence conflict

389

1

Missing in CAA32948. Ref.2

Sequence conflict

399 – 402

4

RSYY → KELL Ref.2

Sequence conflict

403 – 415

13

Missing Ref.2

Secondary structure

1

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415

Helix Strand Turn

Details...

Beta strand

24 – 27

4

Beta strand

54 – 61

8

Turn

62 – 65

4

Beta strand

66 – 77

12

Beta strand

80 – 83

4

Helix

86 – 88

3

Beta strand

96 – 102

7

Beta strand

108 – 110

3

Beta strand

119 – 128

10

Turn

134 – 137

4

Beta strand

142 – 148

7

Beta strand

174 – 181

8

Beta strand

183 – 186

4

Beta strand

195 – 202

8

Helix

204 – 208

5

Turn

210 – 215

6

Beta strand

221 – 225

5

Beta strand

241 – 245

5

Beta strand

253 – 260

8

Beta strand

262 – 266

5

Beta strand

271 – 276

6

Helix

277 – 279

3

Helix

280 – 287

8

Helix

289 – 293

5

Sequences

	Sequence		Length	Mass (Da)
	P08001 [UniParc]. Last modified May 16, 2006. Version 5. Checksum: BAC41900AD43E768	FASTA	415	45,362
	10 20 30 40 50 60 MLPTAVLLVL AVSVAARDNA TCDGPCGLRF RQKLESGMRV VGGMSAEPGA WPWMVSLQIF 70 80 90 100 110 120 MYHNNRRYHT CGGILLNSHW VLTAAHCFKN KKKVTDWRLI FGANEVVWGS NKPVKPPLQE 130 140 150 160 170 180 RFVEEIIIHE KYVSGLEIND IALIKITPPV PCGPFIGPGC LPQFKAGPPR APQTCWVTGW 190 200 210 220 230 240 GYLKEKGPRT SPTLQEARVA LIDLELCNST RWYNGRIRST NVCAGYPRGK IDTCQGDSGG 250 260 270 280 290 300 PLMCRDRAEN TFVVVGITSW GVGCARAKRP GVYTSTWPYL NWIASKIGSN ALQMVQLGTP 310 320 330 340 350 360 PRPSTPAPPV RPPSVQTPVR PPWYFQRPPG PSQQPGSRPR PPAPPPAPPP PPPPPPPPPP 370 380 390 400 410 PPPPPPQQVS AKPPQALSFA KRLQQLIEAL KGTAFSSGRS YYETETTDLQ ELPAS

References

[1]	"Activation and maturation mechanisms of boar acrosin zymogen based on the deduced primary structure." Baba T., Kashiwabara S., Watanabe K., Itoh H., Michikawa Y., Kimura K., Takada M., Fukamizu A., Arai Y. J. Biol. Chem. 264:11920-11927(1989) [PubMed: 2745422] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning of preproacrosin and analysis of its expression pattern in spermatogenesis." Adham I.M., Maier W.-M., Hoyer-Fender S., Tsaousidou S., Engel W., Klemm U. Eur. J. Biochem. 182:563-568(1989) [PubMed: 2502391] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Testis.
[3]	"The structures of the bovine and porcine proacrosin genes and their conservation during mammals." Adham I.M., Kremling H., Nieter S., Zimmermann S., Hummel M., Schroeter U., Engel W. Biol. Chem. Hoppe-Seyler 377:261-265(1996) [PubMed: 8737992] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Liver.
[4]	"Boar acrosin is a two-chain molecule. Isolation and primary structure of the light chain; homology with the pro-part of other serine proteinases." Fock-Nuezel R., Lottspeich F., Henschen A., Mueller-Esterl W. Eur. J. Biochem. 141:441-446(1984) [PubMed: 6378631] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-39. Tissue: Sperm.
[5]	"N-terminal amino acid sequence of boar sperm acrosin. Homology with other serine proteinases." Fock-Nuezel R., Lottspeich F., Henschen A., Mueller-Esterl W., Fritz H. Hoppe-Seyler's Z. Physiol. Chem. 361:1823-1828(1980) [PubMed: 7007202] [Abstract] Cited for: PROTEIN SEQUENCE OF 25-91. Tissue: Sperm.
[6]	"Acrosin shows zona and fucose binding, novel properties for a serine proteinase." Toepfer-Petersen E., Henschen A. FEBS Lett. 226:38-42(1987) [PubMed: 3480243] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-32 AND 40-53. Tissue: Sperm.
[7]	"Is sperminogen a modified proacrosin? Isolation, purification, and partial characterization of low-molecular-mass boar proacrosin." Cechova D., Toepfer-Petersen E., Zucker A., Jonakova V. Biol. Chem. Hoppe-Seyler 371:317-323(1990) [PubMed: 2111146] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-40.
[8]	"Complete localization of the disulfide bridges and glycosylation sites in boar sperm acrosin." Toepfer-Petersen E., Calvete J.J., Schaefer W., Henschen A. FEBS Lett. 275:139-142(1990) [PubMed: 2261983] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-19 AND ASN-208. Tissue: Sperm.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J04950 mRNA. Translation: AAA31131.1.
X14844 mRNA. Translation: CAA32948.1.
X58549 Genomic DNA. Translation: CAA41440.1.

PIR

A34170.

RefSeq

NP_999198.1. NM_214033.1.

UniGene

Ssc.128.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FIZ	X-ray	2.90	A	40-302	[»]
			L	17-39	[»]

ProteinModelPortal

P08001.

SMR

P08001. Positions 40-302.

ModBase

Search...

Protein family/group databases

MEROPS

S01.223.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

397098.

KEGG

ssc:397098.

Organism-specific databases

CTD

49.

Phylogenomic databases

HOVERGEN

HBG013304.

Enzyme and pathway databases

BRENDA

3.4.21.10. 6170.

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...

Entry information

Entry name

ACRO_PIG

Accession

Primary (citable) accession number: P08001
Secondary accession number(s): P08000, Q29015

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	May 16, 2006
Last modified:	December 14, 2011
This is version 95 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program