Tag Content
UniProt Accession
Theoretical PI
Molecular Weight
27605 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Gene Synonyms/Alias
Tpx-1, Tpx1 
Protein Name
Cysteine-rich secretory protein 2 
Protein Synonyms/Alias
CRISP-2 Testis-specific protein TPX-1;Flags: Precursor 
Mus musculus (Mouse) 
NCBI Taxonomy ID
Chromosome Location
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Probability (GAS) of Function in Spermatogenesis
The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
Temporarily unavailable 
Abstract of related literatures
1. A testis-specific gene Tpx-1, located between Pgk-2 and Mep-1 on mouse chromosome 17, was isolated from a cosmid clone, and its cDNA sequences were determined. The predicted coding sequence of Tpx-1 isolated from BALB/c mice showed 64.2% nucleotide and 55.1% amino acid sequence similarity with that of a rat sperm-coating glycoprotein gene, the protein product of which is secreted by the epididymis. To examine the evolutionary relationship between Tpx-1 and a sperm-coating glycoprotein gene, the cDNA sequence of TPX1, the human counterpart of Tpx-1, was determined. The comparison of the predicted coding sequences of Tpx-1 and TPX1 showed 77.8% nucleotide and 70% amino acid sequence similarity. Since Tpx-1 (from mouse) is more similar to TPX1 (from man) than it is to a rat sperm-coating glycoprotein gene, we conclude that Tpx-1 (TPX1) and a sperm-coating glycoprotein gene are closely related, but distinct, genes belonging to the same gene family. The predicted Tpx-1 protein of a t mutant mouse CRO437 differs from that of BALB/c mice by one amino acid insertion in the putative signal peptide. TPX1 was mapped to 6p21-qter by Southern blot analysis of interspecies somatic hybrid cell lines. PMID: [2613236] 

2. The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a random strategy to select clones from a large number of cDNA libraries from diverse tissues. Candidate clones were chosen based on 5'-EST sequences, and then fully sequenced to high accuracy and analyzed by algorithms developed for this project. Currently, more than 11,000 human and 10,000 mouse genes are represented in MGC by at least one clone with a full ORF. The random selection approach is now reaching a saturation point, and a transition to protocols targeted at the missing transcripts is now required to complete the mouse and human collections. Comparison of the sequence of the MGC clones to reference genome sequences reveals that most cDNA clones are of very high sequence quality, although it is likely that some cDNAs may carry missense variants as a consequence of experimental artifact, such as PCR, cloning, or reverse transcriptase errors. Recently, a rat cDNA component was added to the project, and ongoing frog (Xenopus) and zebrafish (Danio) cDNA projects were expanded to take advantage of the high-throughput MGC pipeline. PMID: [15489334] 



CRISP2 (cysteine-rich secretory protein 2) is a sperm acrosome and tail protein with the ability to regulate Ca2+ flow through ryanodine receptors. Based on these properties, CRISP2 has a potential role in fertilization through the regulation of ion signalling in the acrosome reaction and sperm motility. The purpose of the present study was to determine the expression, subcellular localization and the role in spermatogenesis of a novel CRISP2-binding partner, which we have designated SHTAP (sperm head and tail associated protein). PMID: [19686095] 

4. The cysteine-rich secretory proteins (Crisp) are predominantly found in the mammalian male reproductive tract as well as in the venom of reptiles. Crisps are two domain proteins with a structurally similar yet evolutionary diverse N-terminal domain and a characteristic cysteine-rich C-terminal domain, which we refer to as the Crisp domain. We presented the NMR solution structure of the Crisp domain of mouse Tpx-1, and we showed that it contains two subdomains, one of which has a similar fold to the ion channel regulators BgK and ShK. Furthermore, we have demonstrated for the first time that the ion channel regulatory activity of Crisp proteins is attributed to the Crisp domain. Specifically, the Tpx-1 Crisp domain inhibited cardiac ryanodine receptor (RyR) 2 with an IC(50) between 0.5 and 1.0 microM and activated the skeletal RyR1 with an AC(50) between 1 and 10 microM when added to the cytoplasmic domain of the receptor. This activity was nonvoltage-dependent and weakly voltage-dependent, respectively. Furthermore, the Tpx-1 Crisp domain activated both RyR forms at negative bilayer potentials and showed no effect at positive bilayer potentials when added to the luminal domain of the receptor. These data show that the Tpx-1 Crisp domain on its own can regulate ion channel activity and provide compelling evidence for a role for Tpx-1 in the regulation of Ca(2+) fluxes observed during sperm capacitation. PMID: [16339766] 

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May regulate some ion channels' activity and therebyeregulate calcium fluxes during sperm capacitation. 
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Subcellular Location
Secreted (Probable). 
Tissue Specificity
Gene Ontology
GO IDGO termEvidence
GO:0005576 C:extracellular region IEA:UniProtKB-SubCell.
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IPR001283;    Allrgn_V5/Tpx1.
IPR018244;    Allrgn_V5/Tpx1_CS.
IPR014044;    CAP_domain.
IPR013871;    Cysteine_rich_secretory.
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PF00188;    CAP;    1.
PF08562;    Crisp;    1.
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SM00198;    SCP;    1.
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PS01009;    CRISP_1;    1.
PS01010;    CRISP_2;    1.
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PR00837;    V5TPXLIKE.;   
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Created Date
Record Type
GAS predicted 
Sequence Annotation
SIGNAL        1     22       Potential.
CHAIN        23    243       Cysteine-rich secretory protein 2.
MOD_RES     181    181       Phosphothreonine (By similarity).
MOD_RES     183    183       Phosphotyrosine (By similarity).
MOD_RES     187    187       Phosphothreonine (By similarity).
DISULFID    189    196
DISULFID    192    201
DISULFID    205    238
DISULFID    214    232
DISULFID    223    236
STRAND      197    200
HELIX       214    220
HELIX       228    231
HELIX       233    236
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Nucleotide Sequence
Length: 1418 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 243 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
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