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UniProtKB/Swiss-Prot entry P10323


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACRO_HUMAN
Primary accession number P10323
Secondary accession number Q6ICK2
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on October 3, 2006 (Sequence version 4)
Annotations were last modified on    June 16, 2009 (Entry version 105)
Name and origin of the protein
Protein name Acrosin [Precursor]
Synonym EC 3.4.21.10
Contains Acrosin light chain
Acrosin heavy chain
Gene name
Name: ACR
Synonyms: ACRS
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
DOI=10.1016/0014-5793(89)80549-6; PubMed=2493394 [NCBI, ExPASy, EBI, Israel, Japan]
Baba T., Watanabe K., Kashiwabara S., Arai Y.;
"Primary structure of human proacrosin deduced from its cDNA sequence.";
FEBS Lett. 244:296-300(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Leukocyte;
DOI=10.1111/j.1432-1033.1990.tb15564.x; PubMed=2114285 [NCBI, ExPASy, EBI, Israel, Japan]
Keime S., Adham I.M., Engel W.;
"Nucleotide sequence and exon-intron organization of the human proacrosin gene.";
Eur. J. Biochem. 190:195-200(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1007/BF00208925; PubMed=2298447 [NCBI, ExPASy, EBI, Israel, Japan]
Adham I.M., Klemm U., Maier W.-M., Engel W.;
"Molecular cloning of human preproacrosin cDNA.";
Hum. Genet. 84:125-128(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1111/j.1432-1033.1992.tb17014.x; PubMed=1628652 [NCBI, ExPASy, EBI, Israel, Japan]
Vazquez-Levin M.H., Reventos J., Gordon J.W.;
"Molecular cloning, sequencing and restriction mapping of the genomic sequence encoding human proacrosin.";
Eur. J. Biochem. 207:23-26(1992).
[5]
DISCUSSION OF PUBMED:1628652.
Adham I.M., Spitzer U., Schloesser M., Kremling H., Keime S., Engel W.;
Eur. J. Biochem. 207:27-28(1992).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y00970; CAA68784.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X54017; CAA37964.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X54018; CAA37964.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X54019; CAA37964.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X54020; CAA37964.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77378; AAA51572.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77379; AAA51573.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77380; AAA51574.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77381; AAA51575.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X66188; CAA46956.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X54018; CAA46956.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X54019; CAA46956.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X54020; CAA46956.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456366; CAG30252.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00289614; -.
PIR S11674; S11674.
RefSeq NP_001088.2; -.
UniGene Hs.370870
3D structure databases
HSSP P08001; 1FIZ. [HSSP ENTRY / PDB]
SMR P10323; 43-301.
ModBase P10323.
Protein family/group databases
MEROPS S01.223; -.
Enzyme and pathway databases
BRENDA 3.4.21.10; 247.
Organism-specific databases
GeneCards GC22P049466; -.
HGNC HGNC:126; ACR.
GenAtlas ACR.
MIM 102480; gene. [NCBI / EBI]
PharmGKB PA24451; -.
Gene expression databases
Bgee P10323; -.
CleanEx HS_ACR; -.
GermOnline ENSG00000100312; Homo sapiens.
Ontologies
GO
GO:0043159; Cellular component: acrosomal matrix (traceable author statement from HGNC).
GO:0043234; Cellular component: protein complex (inferred from direct assay from UniProtKB).
GO:0004040; Molecular function: amidase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0005507; Molecular function: copper ion binding (non-traceable author statement from UniProtKB).
GO:0003677; Molecular function: DNA binding (non-traceable author statement from UniProtKB).
GO:0008144; Molecular function: drug binding (inferred from sequence or structural similarity from UniProtKB).
GO:0042806; Molecular function: fucose binding (inferred from sequence or structural similarity from UniProtKB).
GO:0005537; Molecular function: mannose binding (inferred from direct assay from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004252; Molecular function: serine-type endopeptidase activity (inferred from direct assay from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (non-traceable author statement from UniProtKB).
GO:0002077; Biological process: acrosome matrix dispersal (non-traceable author statement from UniProtKB).
GO:0007190; Biological process: activation of adenylate cyclase activity (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR012267; Pept_S1A_acrosin.
IPR018114; Peptidase_S1/S6_AS.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.
PANTHER PTHR19355:SF158; Pept_S1A_acrosin; 1.
Pfam PF00089; Trypsin; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001141; Acrosin; 1.
PRINTS PR00722; CHYMOTRYPSIN.
SMART SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.
PROSITE PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P10323; -.
Genome annotation databases
Ensembl ENSG00000100312; Homo sapiens. [Contig view]
GeneID 49; -.
KEGG hsa:49; -.
NMPDR fig|9606.3.peg.22000; -.
Phylogenomic databases
HOGENOM P10323; -.
HOVERGEN P10323; -.
OMA P10323; GLRFRQN.
Other
NextBio 191; -.
SOURCE ACR; Homo sapiens.
ProtoNet P10323.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Disulfide bond; Glycoprotein; Hydrolase; Polymorphism; Protease; Serine protease; Signal; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     19  19      
CHAIN   20    421  402     Acrosin. PRO_0000027518
CHAIN   20     42  23     Acrosin light chain. PRO_0000027519
CHAIN   43   ?343        Acrosin heavy chain. PRO_0000027520
PROPEP   ?344    421        Pro-rich. PRO_0000027521
DOMAIN   43    290  248     Peptidase S1. 
ACT_SITE   88     88        Charge relay system (By similarity). 
ACT_SITE   142    142        Charge relay system (By similarity). 
ACT_SITE   240    240        Charge relay system (By similarity). 
CARBOHYD   22     22        N-linked (GlcNAc...) (By similarity). 
CARBOHYD   210    210        N-linked (GlcNAc...) (By similarity). 
DISULFID   25    154        Interchain (between light and heavy chains) (By similarity). 
DISULFID   29    162        Interchain (between light and heavy chains) (By similarity). 
DISULFID   73     89        By similarity. 
DISULFID   177    246        By similarity. 
DISULFID   209    225        By similarity. 
DISULFID   236    266        By similarity. 
VARIANT   120    120  1     L -> V (in dbSNP:rs1064734 [NCBI]). VAR_011650 [3D]
VARIANT   166    166  1     F -> L (in dbSNP:rs1064735 [NCBI]). VAR_011651 [3D]
CONFLICT   64     64        T -> R (in Ref. 2 and 4). 
CONFLICT   226    226        A -> V (in Ref. 3). 
CONFLICT   268    268        R -> L (in Ref. 2 and 4). 
CONFLICT   296    296        M -> V (in Ref. 6; CAG30252). 
CONFLICT   345    345        R -> P (in Ref. 2, 3 and 4). 
Sequence information
Length: 421 AA [This is the length of the unprocessed precursor] Molecular weight: 45847 Da [This is the MW of the unprocessed precursor] CRC64: 7A2F7ECEC98008FA [This is a checksum on the sequence]
        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 

P10323 in FASTA format

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