cysteine-rich secretory protein 3 isoform 3 [Homo sapiens]
CRISP family CAP domain-containing protein( domain architecture ID 10143563)
CRISP (cysteine-rich secretory protein) family CAP (CSP/antigen 5/PR1) domain-containing protein similar to Varanus acanthurus cysteine-rich venom proteins that block ryanodine receptors, and potassium channels
List of domain hits
Name | Accession | Description | Interval | E-value | |||
CAP_CRISP | cd05383 | CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ... |
68-205 | 1.09e-82 | |||
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory proteins; Cysteine-rich secretory proteins (CRISPs) are two-domain proteins with an evolutionary diverse and structurally conserved N-terminal CAP domain and a C-terminal cysteine-rich domain, which is comprised of a hinge and an ICR (ion channel regulator) region. CRISPs are involved in response to pathogens, fertilization, and sperm maturation. One member, Tex31 from the venom duct of Conus textile, has been shown to possess proteolytic activity sensitive to serine protease inhibitors. CRISP-1 has been shown to mediate gamete fusion by binding to the egg surface. Other members of the CRISP family secreted in the testis (CRISP2), epididymis (CRISP3-4), or during ejaculation (CRISP3), are also involved in sperm-egg interaction, supporting the existence of a functional redundancy and cooperation between homolog proteins ensuring the success of fertilization. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1) and allergen 5 from vespid venom, among others. : Pssm-ID: 349402 Cd Length: 139 Bit Score: 244.57 E-value: 1.09e-82
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Crisp | pfam08562 | Crisp; This domain is found on Crisp proteins which contain pfam00188 and has been termed the ... |
222-276 | 2.04e-25 | |||
Crisp; This domain is found on Crisp proteins which contain pfam00188 and has been termed the Crisp domain. It is found in the mammalian reproductive tract and the venom of reptiles, and has been shown to regulate ryanodine receptor Ca2+ signalling. It contains 10 conserved cysteines which are all involved in disulphide bonds and is structurally related to the ion channel inhibitor toxins BgK and ShK. : Pssm-ID: 462519 Cd Length: 55 Bit Score: 95.40 E-value: 2.04e-25
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Name | Accession | Description | Interval | E-value | |||
CAP_CRISP | cd05383 | CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ... |
68-205 | 1.09e-82 | |||
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory proteins; Cysteine-rich secretory proteins (CRISPs) are two-domain proteins with an evolutionary diverse and structurally conserved N-terminal CAP domain and a C-terminal cysteine-rich domain, which is comprised of a hinge and an ICR (ion channel regulator) region. CRISPs are involved in response to pathogens, fertilization, and sperm maturation. One member, Tex31 from the venom duct of Conus textile, has been shown to possess proteolytic activity sensitive to serine protease inhibitors. CRISP-1 has been shown to mediate gamete fusion by binding to the egg surface. Other members of the CRISP family secreted in the testis (CRISP2), epididymis (CRISP3-4), or during ejaculation (CRISP3), are also involved in sperm-egg interaction, supporting the existence of a functional redundancy and cooperation between homolog proteins ensuring the success of fertilization. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1) and allergen 5 from vespid venom, among others. Pssm-ID: 349402 Cd Length: 139 Bit Score: 244.57 E-value: 1.09e-82
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SCP | smart00198 | SCP / Tpx-1 / Ag5 / PR-1 / Sc7 family of extracellular domains; Human glioma ... |
68-204 | 1.47e-46 | |||
SCP / Tpx-1 / Ag5 / PR-1 / Sc7 family of extracellular domains; Human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein represent functional links between plant defense systems and human immune system. This family has no known function. Pssm-ID: 214553 [Multi-domain] Cd Length: 144 Bit Score: 152.54 E-value: 1.47e-46
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Crisp | pfam08562 | Crisp; This domain is found on Crisp proteins which contain pfam00188 and has been termed the ... |
222-276 | 2.04e-25 | |||
Crisp; This domain is found on Crisp proteins which contain pfam00188 and has been termed the Crisp domain. It is found in the mammalian reproductive tract and the venom of reptiles, and has been shown to regulate ryanodine receptor Ca2+ signalling. It contains 10 conserved cysteines which are all involved in disulphide bonds and is structurally related to the ion channel inhibitor toxins BgK and ShK. Pssm-ID: 462519 Cd Length: 55 Bit Score: 95.40 E-value: 2.04e-25
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CAP | pfam00188 | Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory ... |
74-202 | 7.18e-14 | |||
Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins (CAP) that are found in a wide range of organizms, including prokaryotes and non-vertebrate eukaryotes, The nine subfamilies of the mammalian CAP 'super'family include: the human glioma pathogenesis-related 1 (GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), cysteine-rich secretory proteins (CRISPs), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), mannose receptor like and the R3H domain containing like proteins. Members are most often secreted and have an extracellular endocrine or paracrine function and are involved in processes including the regulation of extracellular matrix and branching morphogenesis, potentially as either proteases or protease inhibitors; in ion channel regulation in fertility; as tumour suppressor or pro-oncogenic genes in tissues including the prostate; and in cell-cell adhesion during fertilization. The overall protein structural conservation within the CAP 'super'family results in fundamentally similar functions for the CAP domain in all members, yet the diversity outside of this core region dramatically alters the target specificity and, thus, the biological consequences. The Ca++-chelating function would fit with the various signalling processes (e.g. the CRISP proteins) that members of this family are involved in, and also the sequence and structural evidence of a conserved pocket containing two histidines and a glutamate. It also may explain how Swiss:Q91055 blocks the Ca++ transporting ryanodine receptors. Pssm-ID: 395136 Cd Length: 117 Bit Score: 66.46 E-value: 7.18e-14
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Name | Accession | Description | Interval | E-value | |||
CAP_CRISP | cd05383 | CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ... |
68-205 | 1.09e-82 | |||
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory proteins; Cysteine-rich secretory proteins (CRISPs) are two-domain proteins with an evolutionary diverse and structurally conserved N-terminal CAP domain and a C-terminal cysteine-rich domain, which is comprised of a hinge and an ICR (ion channel regulator) region. CRISPs are involved in response to pathogens, fertilization, and sperm maturation. One member, Tex31 from the venom duct of Conus textile, has been shown to possess proteolytic activity sensitive to serine protease inhibitors. CRISP-1 has been shown to mediate gamete fusion by binding to the egg surface. Other members of the CRISP family secreted in the testis (CRISP2), epididymis (CRISP3-4), or during ejaculation (CRISP3), are also involved in sperm-egg interaction, supporting the existence of a functional redundancy and cooperation between homolog proteins ensuring the success of fertilization. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1) and allergen 5 from vespid venom, among others. Pssm-ID: 349402 Cd Length: 139 Bit Score: 244.57 E-value: 1.09e-82
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SCP | smart00198 | SCP / Tpx-1 / Ag5 / PR-1 / Sc7 family of extracellular domains; Human glioma ... |
68-204 | 1.47e-46 | |||
SCP / Tpx-1 / Ag5 / PR-1 / Sc7 family of extracellular domains; Human glioma pathogenesis-related protein GliPR and the plant pathogenesis-related protein represent functional links between plant defense systems and human immune system. This family has no known function. Pssm-ID: 214553 [Multi-domain] Cd Length: 144 Bit Score: 152.54 E-value: 1.47e-46
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CAP | cd00168 | CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ... |
72-203 | 4.93e-44 | |||
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain family; The CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain, also called SCP (sperm-coating glycoprotein), is found in eukaryotes and prokaryotes. This family includes plant pathogenesis-related protein 1 (PR-1), which accumulates after infections with pathogens, and may act as an anti-fungal agent or be involved in cell wall loosening. This family also includes CRISPs (cysteine-rich secretory proteins), which combine the CAP/SCP domain with a C-terminal cysteine rich domain, and allergen 5 from vespid venom. Roles for CRISP, in response to pathogens, fertilization, and sperm maturation have been proposed. One member, Tex31 from the venom duct of Conus textile, has been shown to possess proteolytic activity sensitive to serine protease inhibitors. The human GAPR-1 protein has been reported to dimerize, and such a dimer may form an active site containing a catalytic triad. CAP/SCP has also been proposed to be a Ca++ chelating serine protease. The Ca++-chelating function would fit with various signaling processes that members of this family, such as the CRISPs, are involved in, and is supported by sequence and structural evidence of a conserved pocket containing two histidines and a glutamate. It also may explain how helothermine, a toxic peptide secreted by the beaded lizard, blocks Ca++ transporting ryanodine receptors. Little is known about the biological roles of the bacterial and archaeal CAP/SCP domains. Pssm-ID: 349397 Cd Length: 128 Bit Score: 145.84 E-value: 4.93e-44
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CAP_euk | cd05380 | Eukaryotic CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 ... |
70-202 | 5.62e-39 | |||
Eukaryotic CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain proteins; The CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain is found mainly in eukaryotes. This family includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), glioma pathogenesis-related 1 (GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), and allergen 5 from vespid venom. Pssm-ID: 349399 Cd Length: 144 Bit Score: 133.35 E-value: 5.62e-39
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CAP_PI16_HrTT-1 | cd05559 | CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ... |
70-202 | 1.19e-30 | |||
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor 16 and HrTT-1 protein; Human peptidase inhibitor 16 (PI16) is also called cysteine-rich secretory protein 9 (CRISP-9) or PSP94-binding protein. Mouse PI16 is also called cysteine-rich protease inhibitor. PI16 is predominantly expressed by cardiac fibroblasts and is exposed to the interstitium via a glycophosphatidylinositol (-GPI) membrane anchor. It suppresses the activation of the chemokine chemerin in the myocardium, which may be a part of the cardiac stress response. At high endothelial shear stress, PI16 is an inflammation-regulated inhibitor of matrix metalloproteinase 2 (MMP2). Also included in this subfamily is the HrTT-1 protein, a tail-tip epidermis marker in ascidians. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Pssm-ID: 349405 Cd Length: 134 Bit Score: 111.36 E-value: 1.19e-30
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CAP_GLIPR1-like | cd05385 | CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ... |
71-206 | 6.30e-29 | |||
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of glioma pathogenesis-related protein 1 and similar proteins; Glioma pathogenesis-related protein 1 (GLIPR1) is also called related to testes-specific, vespid, and pathogenesis protein 1 (RTVP-1). The GLIPR1 gene has been identified as a p53 target gene and was shown to be methylated and down-regulated in prostate cancer. It is a novel broad-spectrum tumor suppressor whose proapoptotic properties are exerted in part through ROS-JNK signaling. GLIPR1 is composed of a signal peptide that directs its secretion, a CAP domain, and a transmembrane domain. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Pssm-ID: 349404 Cd Length: 148 Bit Score: 107.49 E-value: 6.30e-29
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Crisp | pfam08562 | Crisp; This domain is found on Crisp proteins which contain pfam00188 and has been termed the ... |
222-276 | 2.04e-25 | |||
Crisp; This domain is found on Crisp proteins which contain pfam00188 and has been termed the Crisp domain. It is found in the mammalian reproductive tract and the venom of reptiles, and has been shown to regulate ryanodine receptor Ca2+ signalling. It contains 10 conserved cysteines which are all involved in disulphide bonds and is structurally related to the ion channel inhibitor toxins BgK and ShK. Pssm-ID: 462519 Cd Length: 55 Bit Score: 95.40 E-value: 2.04e-25
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CAP_GAPR1-like | cd05382 | CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ... |
70-208 | 1.73e-24 | |||
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of Golgi-associated plant pathogenesis-related protein 1 and similar proteins; Golgi-associated plant pathogenesis related protein 1 (GAPR1), also called Golgi-associated PR-1 protein or glioma pathogenesis-related protein 2 (GLIPR-2), forms amyloid-like fibrils in the presence of liposomes containing acidic phospholipids. It has been identified in mice as an up-regulated protein in kidney fibrosis, and is involved in epithelial to mesenchymal transition and in generating a pool of myofibroblasts contributing to fibrosis. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Pssm-ID: 349401 Cd Length: 132 Bit Score: 95.36 E-value: 1.73e-24
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CAP_PR-1 | cd05381 | CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ... |
70-211 | 7.50e-22 | |||
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of pathogenesis-related protein 1 (PR-1) family proteins; Members of pathogenesis-related protein 1 (PR-1) family are among the most abundantly produced proteins in plants on pathogen attack. They are considered hallmarks of hypersensitive response/defense pathways and may act as anti-fungal agents or be involved in cell wall loosening. Pssm-ID: 349400 Cd Length: 136 Bit Score: 88.46 E-value: 7.50e-22
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CAP_PRY1-like | cd05384 | CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ... |
68-210 | 2.07e-21 | |||
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of pathogen-related yeast 1 (PRY1) protein and similar fungal proteins; PRY1, also called pathogenesis-related protein 1, is a yeast protein that is up-regulated in core ESCRT mutants. It is a secreted protein required for efficient export of lipids such as acetylated sterols, and acts in detoxification of hydrophobic compounds. This PRY1-like group also contains fruiting body proteins SC7/14 from Schizophyllum commune. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Pssm-ID: 349403 Cd Length: 129 Bit Score: 87.00 E-value: 2.07e-21
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CAP_CRISPLD2 | cd18816 | CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ... |
70-202 | 2.04e-18 | |||
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory protein LCCL domain-containing 2; Cysteine-rich secretory protein LCCL domain-containing 2 (CRISPLD2) is also called cysteine-rich secretory protein 11 (CRSIP-11), LCCL domain-containing cysteine-rich secretory protein 2 (LCRISP2), or CAP and LCCL domain containing protein 2 (CAPLD2). It plays a role in the etiology of NSCLP (non-syndromic cleft lip with or without cleft palate). It is required for neural crest cell migration and cell viability during craniofacial development. The CRISPLD2 gene has been identified a glucocorticoid responsive gene that modulates cytokine function in airway smooth muscle cells. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Pssm-ID: 349410 Cd Length: 146 Bit Score: 79.64 E-value: 2.04e-18
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CAP_PI15-like | cd18812 | CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ... |
72-202 | 1.15e-17 | |||
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor 15 and similar proteins; This family is composed of peptidase inhibitor 15 (PI15), peptidase inhibitor R3HDML, cysteine-rich secretory protein LCCL domain-containing 1 (CRISPLD1), and cysteine-rich secretory protein LCCL domain-containing 2 (CRISPLD2). PI15 is a serine protease inhibitor which displays weak inhibitory activity against trypsin and may play a role in facial patterning during embryonic development. The PI15 gene is a candidate gene for abdominal aortic internal elastic lamina ruptures in the rat. R3HDML is a putative serine protease inhibitor, whose gene may be associated with clinical dimensions of schizophrenia. CRISPLD1 may play a role in NSCLP (nonsyndromic cleft lip with or without cleft palate) through the interaction with CRISPLD2 and folate pathway genes. plays a role in the etiology of NSCLP and is required for neural crest cell migration and cell viability during craniofacial development. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Pssm-ID: 349406 Cd Length: 146 Bit Score: 77.64 E-value: 1.15e-17
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CAP_CRISPLD1 | cd18813 | CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ... |
73-202 | 3.93e-17 | |||
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of cysteine-rich secretory protein LCCL domain-containing 1; Cysteine-rich secretory protein LCCL domain-containing 1 (CRISPLD1) is also called cysteine-rich secretory protein 10 (CRISP-10), CocoaCrisp, LCCL domain-containing cysteine-rich secretory protein 1 (LCRISP1), or CAP and LCCL domain containing protein 1 (CAPLD1). CRISPLD1 is clearly distinct from CRISPs because they do not contain the 10 absolutely conserved cysteines or the ICR (ion channel regulator) domain of the CRISPs. It may play a role in NSCLP (nonsyndromic cleft lip with or without cleft palate) through the interaction with CRISPLD2 and folate pathway genes. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Pssm-ID: 349407 Cd Length: 146 Bit Score: 76.20 E-value: 3.93e-17
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CAP_PI15 | cd18814 | CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ... |
73-202 | 4.82e-16 | |||
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor 15; Peptidase inhibitor 15 (PI15) is also called 25 kDa trypsin inhibitor (p25TI), cysteine-rich secretory protein 8 (CRISP-8), or SugarCrisp. It is a serine protease inhibitor which displays weak inhibitory activity against trypsin and may play a role in facial patterning during embryonic development. The PI15 gene is a candidate gene for abdominal aortic internal elastic lamina ruptures in the rat. PI15 may also participate in the regulation of drug resistance in ovarian cancer and serve as a potential target in targeted therapies. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Pssm-ID: 349408 Cd Length: 146 Bit Score: 73.11 E-value: 4.82e-16
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CAP_R3HDML | cd18815 | CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain ... |
73-202 | 6.30e-16 | |||
CAP (cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins) domain of peptidase inhibitor R3HDML; Peptidase inhibitor R3HDML, also called cysteine-rich secretory protein R3HDML, is a putative serine protease inhibitor. The R3HDML gene may be associated with clinical dimensions of schizophrenia. The wider family of CAP domain containing proteins includes plant pathogenesis-related protein 1 (PR-1), cysteine-rich secretory proteins (CRISPs), and allergen 5 from vespid venom, among others. Pssm-ID: 349409 Cd Length: 146 Bit Score: 73.01 E-value: 6.30e-16
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CAP | pfam00188 | Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory ... |
74-202 | 7.18e-14 | |||
Cysteine-rich secretory protein family; This is a large family of cysteine-rich secretory proteins, antigen 5, and pathogenesis-related 1 proteins (CAP) that are found in a wide range of organizms, including prokaryotes and non-vertebrate eukaryotes, The nine subfamilies of the mammalian CAP 'super'family include: the human glioma pathogenesis-related 1 (GLIPR1), Golgi associated pathogenesis related-1 (GAPR1) proteins, peptidase inhibitor 15 (PI15), peptidase inhibitor 16 (PI16), cysteine-rich secretory proteins (CRISPs), CRISP LCCL domain containing 1 (CRISPLD1), CRISP LCCL domain containing 2 (CRISPLD2), mannose receptor like and the R3H domain containing like proteins. Members are most often secreted and have an extracellular endocrine or paracrine function and are involved in processes including the regulation of extracellular matrix and branching morphogenesis, potentially as either proteases or protease inhibitors; in ion channel regulation in fertility; as tumour suppressor or pro-oncogenic genes in tissues including the prostate; and in cell-cell adhesion during fertilization. The overall protein structural conservation within the CAP 'super'family results in fundamentally similar functions for the CAP domain in all members, yet the diversity outside of this core region dramatically alters the target specificity and, thus, the biological consequences. The Ca++-chelating function would fit with the various signalling processes (e.g. the CRISP proteins) that members of this family are involved in, and also the sequence and structural evidence of a conserved pocket containing two histidines and a glutamate. It also may explain how Swiss:Q91055 blocks the Ca++ transporting ryanodine receptors. Pssm-ID: 395136 Cd Length: 117 Bit Score: 66.46 E-value: 7.18e-14
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Blast search parameters | ||||
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