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Protein

Acrosin

Gene

ACR

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.

Enzyme regulationi

Inhibited by SERPINA5.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei86 – 861Charge relay systemBy similarity
Active sitei140 – 1401Charge relay systemBy similarity
Active sitei238 – 2381Charge relay systemBy similarity

GO - Molecular functioni

  • amidase activity Source: UniProtKB
  • drug binding Source: UniProtKB
  • fucose binding Source: UniProtKB
  • mannose binding Source: UniProtKB
  • serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.21.10. 6170.

Protein family/group databases

MEROPSiS01.223.

Names & Taxonomyi

Protein namesi
Recommended name:
Acrosin (EC:3.4.21.10)
Alternative name(s):
53 kDa fucose-binding protein
Cleaved into the following 2 chains:
Gene namesi
Name:ACR
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • acrosomal matrix Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3243910.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 16163 PublicationsAdd
BLAST
Chaini17 – 415399AcrosinPRO_0000027526Add
BLAST
Chaini17 – 3923Acrosin light chainPRO_0000027527Add
BLAST
Chaini40 – 338299Acrosin heavy chainPRO_0000027528Add
BLAST
Propeptidei339 – 41577Pro-richPRO_0000027529Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi19 – 191N-linked (GlcNAc...)1 Publication
Disulfide bondi22 ↔ 152Interchain (between light and heavy chains)PROSITE-ProRule annotation1 Publication
Disulfide bondi26 ↔ 160Interchain (between light and heavy chains)PROSITE-ProRule annotation1 Publication
Disulfide bondi71 ↔ 87PROSITE-ProRule annotation1 Publication
Disulfide bondi175 ↔ 244PROSITE-ProRule annotation1 Publication
Disulfide bondi207 ↔ 223PROSITE-ProRule annotation1 Publication
Glycosylationi208 – 2081N-linked (GlcNAc...)1 Publication
Disulfide bondi234 ↔ 264PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP08001.

Interactioni

Subunit structurei

Heavy chain (catalytic) and a light chain linked by two disulfide bonds. Forms a heterodimer with SERPINA5 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000021991.

Chemistry

BindingDBiP08001.

Structurei

Secondary structure

1
415
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi24 – 274Combined sources
Beta strandi54 – 618Combined sources
Turni62 – 654Combined sources
Beta strandi66 – 7712Combined sources
Beta strandi80 – 834Combined sources
Helixi86 – 883Combined sources
Beta strandi96 – 1027Combined sources
Beta strandi108 – 1103Combined sources
Beta strandi119 – 12810Combined sources
Turni134 – 1374Combined sources
Beta strandi142 – 1487Combined sources
Beta strandi174 – 1818Combined sources
Beta strandi183 – 1864Combined sources
Beta strandi195 – 2028Combined sources
Helixi204 – 2085Combined sources
Turni210 – 2156Combined sources
Beta strandi221 – 2255Combined sources
Beta strandi241 – 2455Combined sources
Beta strandi253 – 2608Combined sources
Beta strandi262 – 2665Combined sources
Beta strandi271 – 2766Combined sources
Helixi277 – 2793Combined sources
Helixi280 – 2878Combined sources
Helixi289 – 2935Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FIZX-ray2.90A40-302[»]
L17-39[»]
ProteinModelPortaliP08001.
SMRiP08001. Positions 40-302.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08001.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 288249Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOVERGENiHBG013304.
InParanoidiP08001.
KOiK01317.

Family and domain databases

InterProiIPR012267. Pept_S1A_acrosin.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PANTHERiPTHR24252. PTHR24252. 1 hit.
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001141. Acrosin. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08001-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPTAVLLVL AVSVAARDNA TCDGPCGLRF RQKLESGMRV VGGMSAEPGA
60 70 80 90 100
WPWMVSLQIF MYHNNRRYHT CGGILLNSHW VLTAAHCFKN KKKVTDWRLI
110 120 130 140 150
FGANEVVWGS NKPVKPPLQE RFVEEIIIHE KYVSGLEIND IALIKITPPV
160 170 180 190 200
PCGPFIGPGC LPQFKAGPPR APQTCWVTGW GYLKEKGPRT SPTLQEARVA
210 220 230 240 250
LIDLELCNST RWYNGRIRST NVCAGYPRGK IDTCQGDSGG PLMCRDRAEN
260 270 280 290 300
TFVVVGITSW GVGCARAKRP GVYTSTWPYL NWIASKIGSN ALQMVQLGTP
310 320 330 340 350
PRPSTPAPPV RPPSVQTPVR PPWYFQRPPG PSQQPGSRPR PPAPPPAPPP
360 370 380 390 400
PPPPPPPPPP PPPPPPQQVS AKPPQALSFA KRLQQLIEAL KGTAFSSGRS
410
YYETETTDLQ ELPAS
Length:415
Mass (Da):45,362
Last modified:May 16, 2006 - v5
Checksum:iBAC41900AD43E768
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81Missing in CAA32948 (PubMed:2502391).Curated
Sequence conflicti211 – 2111R → Q in CAA32948 (PubMed:2502391).Curated
Sequence conflicti217 – 2182IR → VT in CAA32948 (PubMed:2502391).Curated
Sequence conflicti347 – 3471A → P in AAA31131 (PubMed:2745422).Curated
Sequence conflicti389 – 3891Missing in CAA32948 (PubMed:2502391).Curated
Sequence conflicti399 – 4024RSYY → KELL (PubMed:2502391).Curated
Sequence conflicti403 – 41513Missing (PubMed:2502391).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04950 mRNA. Translation: AAA31131.1.
X14844 mRNA. Translation: CAA32948.1.
X58549 Genomic DNA. Translation: CAA41440.1.
PIRiA34170.
RefSeqiNP_999198.1. NM_214033.1.
UniGeneiSsc.128.

Genome annotation databases

GeneIDi397098.
KEGGissc:397098.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04950 mRNA. Translation: AAA31131.1.
X14844 mRNA. Translation: CAA32948.1.
X58549 Genomic DNA. Translation: CAA41440.1.
PIRiA34170.
RefSeqiNP_999198.1. NM_214033.1.
UniGeneiSsc.128.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FIZX-ray2.90A40-302[»]
L17-39[»]
ProteinModelPortaliP08001.
SMRiP08001. Positions 40-302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000021991.

Chemistry

BindingDBiP08001.
ChEMBLiCHEMBL3243910.

Protein family/group databases

MEROPSiS01.223.

Proteomic databases

PaxDbiP08001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi397098.
KEGGissc:397098.

Organism-specific databases

CTDi49.

Phylogenomic databases

eggNOGiKOG3627. Eukaryota.
COG5640. LUCA.
HOVERGENiHBG013304.
InParanoidiP08001.
KOiK01317.

Enzyme and pathway databases

BRENDAi3.4.21.10. 6170.

Miscellaneous databases

EvolutionaryTraceiP08001.

Family and domain databases

InterProiIPR012267. Pept_S1A_acrosin.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PANTHERiPTHR24252. PTHR24252. 1 hit.
PfamiPF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001141. Acrosin. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS, GLYCOSYLATION AT ASN-19 AND ASN-208.
    Tissue: Sperm.

Entry informationi

Entry nameiACRO_PIG
AccessioniPrimary (citable) accession number: P08001
Secondary accession number(s): P08000, Q29015
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 16, 2006
Last modified: March 16, 2016
This is version 118 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.