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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574331  61 IALIVDKHNEYRNKFAGGMDQN-PKAARMTTIEWDPELAKVADGLVRRCEPIRDQCAITPNYGhaEVSYSleKYFCMTTK 139
Cdd:cd05380   1 RQEILDAHNELRSKVAKGKLKGlPPAANMPKLKWDCELAKLAQNWAKTCVFAHSPCRNTGGVG--QNLAS--VSSSGKDL 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574331 140 KEALRKQLDHWFDPNSKDEVQKLFfswTKNQQELSKNYFQVLRDRANRVGCAIVEYVRPALVHQLLKCVYN 210
Cdd:cd05380  77 KELIEDAVNAWFDELKDYGFGSNP---NNNFNSGIGHFTQMVWAKTTKVGCAVARCPKGGGNKTYVVCNYS 144

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574331  61 IALIVDKHNEYRNKFAGGMDQN-PKAARMTTIEWDPELAKVADGLVRRCEPIRDQCAITPNYGhaEVSYSleKYFCMTTK 139
Cdd:cd05380   1 RQEILDAHNELRSKVAKGKLKGlPPAANMPKLKWDCELAKLAQNWAKTCVFAHSPCRNTGGVG--QNLAS--VSSSGKDL 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574331 140 KEALRKQLDHWFDPNSKDEVQKLFfswTKNQQELSKNYFQVLRDRANRVGCAIVEYVRPALVHQLLKCVYN 210
Cdd:cd05380  77 KELIEDAVNAWFDELKDYGFGSNP---NNNFNSGIGHFTQMVWAKTTKVGCAVARCPKGGGNKTYVVCNYS 144

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574331    65 VDKHNEYRnkfaggmdqnpKAARMTTIEWDPELAKVADGLVRRCePIRDQCAITPNYGHAEVSYSlekyfcmttkkealr 144
Cdd:pfam00188   1 LDLHNEYR-----------AAAGLPPLSWDNELAAAAQDHAKYC-ADNGSHNHRSPYGGNIYARV--------------- 53

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 28574331   145 KQLDHWFDPNSKDEVQKLFFSWTKNQQELS-KNYFQVLRDRANRVGCAIVEYvrPALVHQLLKCVY 209
Cdd:pfam00188  54 VAAGYALGDAGPDSAEDAVDGWYDSPGTYNcGHRTNLLWPKSTKVGCAVAKC--GDGGTYYFVCNY 117

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574331  61 IALIVDKHNEYRNKFAGGMDQN-PKAARMTTIEWDPELAKVADGLVRRCEPIRDQCAITPNYGhaEVSYSleKYFCMTTK 139
Cdd:cd05380   1 RQEILDAHNELRSKVAKGKLKGlPPAANMPKLKWDCELAKLAQNWAKTCVFAHSPCRNTGGVG--QNLAS--VSSSGKDL 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28574331 140 KEALRKQLDHWFDPNSKDEVQKLFfswTKNQQELSKNYFQVLRDRANRVGCAIVEYVRPALVHQLLKCVYN 210
Cdd:cd05380  77 KELIEDAVNAWFDELKDYGFGSNP---NNNFNSGIGHFTQMVWAKTTKVGCAVARCPKGGGNKTYVVCNYS 144

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574331  65 VDKHNEYRNKFaggmdqNPKAARMTTIEWDPELAKVADGLVRRCEPIRDQCAITPNYGHAEVSYSLEKYFCMTTKKEALR 144
Cdd:cd05385   7 VRIHNELRSKV------SPPAANMRYMSWDKALAKTARAWARKCKFSHNICLKEPGKCHPNFTTLGENIWLGSIFSFSVE 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 28574331 145 KQLDHWFdpnskDEVQklFFSWTKNQ-QELSKNYFQVLRDRANRVGCAI 192
Cdd:cd05385  81 SAITSWY-----NEVK--DYNFKTNScSRVCGHYTQVVWADSYKVGCAV 122

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28574331  63 LIVDKHNEYRNKfaggmdQNPKAARMTTIEWDPELAKVADGLVRRCEpirdqcaitpnYGH-AEVSYSLEKYFCMTTKKE 141
Cdd:cd05559   3 LLVDLHNQYRSQ------VSPSAANMLKMTWDTELEALAKAYARKCI-----------WEHnPDRGRVGENLFASTGKPL 65

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 28574331 142 ALRKQLDHWFDpnskdevQKLFFSWTKNQQELSK---NYFQVLRDRANRVGCA 191
Cdd:cd05559  66 DVELAVEDWHN-------EKEYYNFETKTCAPGKmcgHYTQVVWANTEKIGCG 111

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.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 28574331  64 IVDKHNEYRNKfaggmdQNPKAARMTTIEWDPELAKVADGLVRRC 108
Cdd:cd00168   4 ILDLHNSYRSS------VSPPASNMPLMAWDQELADVAIGYAKDC 42