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Conserved domains on  [gi|259089433|ref|NP_001158729|]
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secretogranin-3 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SGIII super family cl21284
Secretogranin-3; Secretogranin_3 is a family of vertebrate proteins that is one of the granin ...
 1-236 6.41e-127

Secretogranin-3; Secretogranin_3 is a family of vertebrate proteins that is one of the granin family. Granins are rich in acidic amino acids, exhibit aggregation at low pH, and possess a high capacity for calcium binding. Because granins are restricted in their localization to secretory granules of neuroendocrine cells, two interesting characteriztics of their sorting mechanisms have been observed. These are, first, that they aggregate on low pH/high calcium concentrations and second that two of them carry an N-terminal disulfide loop, mutations in which lead to mis-sorting. Thus, granins are thought to be essential for the sorting of secretory proteins at the trans-Golgi network. Chromogranin A (CgA) binds to SGIII in secretory granules of endocrine cells. SGIII directly binds to cholesterol components of the secretory granule membrane and targets CgA to secretory granules in pituitary and pancreatic endocrine cells. Mutations in the SGIII gene may influence the risk of obesity through possible regulation of hypothalamic neuropeptide secretion.


The actual alignment was detected with superfamily member pfam15467:

Pssm-ID: 464732  Cd Length: 449  Bit Score: 366.41  E-value: 6.41e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259089433    1 MAAIQDGLAKGEN-DETVSNTLTLTNGLERRTKTYSEDNFEELQYFPNFYALLKSIDSEKEAKEKETLITIMKTLIDFVK 79
Cdd:pfam15467 218 PKPRQDEEDEEENeDDTVDNTWDLPNGLERRNELSPEDGLQDLQYFPNFYRLLKSLNSEQDAKEKETLITIMKTLIDFVK 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259089433   80 MMVKYGTISPEEGVSYLENLDEMIALQTKNKLEKNATDNISKlfpAPSEKSHEETDSTKEEAAKMEKEYGSLKDSTKDDN 159
Cdd:pfam15467 298 MMVKYGTITPEEGVSYLENLDAMIALQTKNKLGKSLGTPDIK---APTGKNLEEDDNTKAEAAKMEKEYENLKDSTKEEQ 374

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259089433  160 SNPgGKTDEPkGKTEAYLEAIRKNIEWLKKHDKKGNKEDYDLSKMRDFINKQADAYVEKGILDKEEAEAIKRIYSSL 236
Cdd:pfam15467 375 QNT-EETDQP-GKSETYLEAIRKNIEWLKKHNKEGNKEDYDLSKLRDFMDQQVDSYIEKGILAKEEGDVIKRIYSSL 449
 
Name Accession Description Interval E-value
SGIII pfam15467
Secretogranin-3; Secretogranin_3 is a family of vertebrate proteins that is one of the granin ...
 1-236 6.41e-127

Secretogranin-3; Secretogranin_3 is a family of vertebrate proteins that is one of the granin family. Granins are rich in acidic amino acids, exhibit aggregation at low pH, and possess a high capacity for calcium binding. Because granins are restricted in their localization to secretory granules of neuroendocrine cells, two interesting characteriztics of their sorting mechanisms have been observed. These are, first, that they aggregate on low pH/high calcium concentrations and second that two of them carry an N-terminal disulfide loop, mutations in which lead to mis-sorting. Thus, granins are thought to be essential for the sorting of secretory proteins at the trans-Golgi network. Chromogranin A (CgA) binds to SGIII in secretory granules of endocrine cells. SGIII directly binds to cholesterol components of the secretory granule membrane and targets CgA to secretory granules in pituitary and pancreatic endocrine cells. Mutations in the SGIII gene may influence the risk of obesity through possible regulation of hypothalamic neuropeptide secretion.


Pssm-ID: 464732  Cd Length: 449  Bit Score: 366.41  E-value: 6.41e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259089433    1 MAAIQDGLAKGEN-DETVSNTLTLTNGLERRTKTYSEDNFEELQYFPNFYALLKSIDSEKEAKEKETLITIMKTLIDFVK 79
Cdd:pfam15467 218 PKPRQDEEDEEENeDDTVDNTWDLPNGLERRNELSPEDGLQDLQYFPNFYRLLKSLNSEQDAKEKETLITIMKTLIDFVK 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259089433   80 MMVKYGTISPEEGVSYLENLDEMIALQTKNKLEKNATDNISKlfpAPSEKSHEETDSTKEEAAKMEKEYGSLKDSTKDDN 159
Cdd:pfam15467 298 MMVKYGTITPEEGVSYLENLDAMIALQTKNKLGKSLGTPDIK---APTGKNLEEDDNTKAEAAKMEKEYENLKDSTKEEQ 374

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259089433  160 SNPgGKTDEPkGKTEAYLEAIRKNIEWLKKHDKKGNKEDYDLSKMRDFINKQADAYVEKGILDKEEAEAIKRIYSSL 236
Cdd:pfam15467 375 QNT-EETDQP-GKSETYLEAIRKNIEWLKKHNKEGNKEDYDLSKLRDFMDQQVDSYIEKGILAKEEGDVIKRIYSSL 449
 
Name Accession Description Interval E-value
SGIII pfam15467
Secretogranin-3; Secretogranin_3 is a family of vertebrate proteins that is one of the granin ...
 1-236 6.41e-127

Secretogranin-3; Secretogranin_3 is a family of vertebrate proteins that is one of the granin family. Granins are rich in acidic amino acids, exhibit aggregation at low pH, and possess a high capacity for calcium binding. Because granins are restricted in their localization to secretory granules of neuroendocrine cells, two interesting characteriztics of their sorting mechanisms have been observed. These are, first, that they aggregate on low pH/high calcium concentrations and second that two of them carry an N-terminal disulfide loop, mutations in which lead to mis-sorting. Thus, granins are thought to be essential for the sorting of secretory proteins at the trans-Golgi network. Chromogranin A (CgA) binds to SGIII in secretory granules of endocrine cells. SGIII directly binds to cholesterol components of the secretory granule membrane and targets CgA to secretory granules in pituitary and pancreatic endocrine cells. Mutations in the SGIII gene may influence the risk of obesity through possible regulation of hypothalamic neuropeptide secretion.


Pssm-ID: 464732  Cd Length: 449  Bit Score: 366.41  E-value: 6.41e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259089433    1 MAAIQDGLAKGEN-DETVSNTLTLTNGLERRTKTYSEDNFEELQYFPNFYALLKSIDSEKEAKEKETLITIMKTLIDFVK 79
Cdd:pfam15467 218 PKPRQDEEDEEENeDDTVDNTWDLPNGLERRNELSPEDGLQDLQYFPNFYRLLKSLNSEQDAKEKETLITIMKTLIDFVK 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259089433   80 MMVKYGTISPEEGVSYLENLDEMIALQTKNKLEKNATDNISKlfpAPSEKSHEETDSTKEEAAKMEKEYGSLKDSTKDDN 159
Cdd:pfam15467 298 MMVKYGTITPEEGVSYLENLDAMIALQTKNKLGKSLGTPDIK---APTGKNLEEDDNTKAEAAKMEKEYENLKDSTKEEQ 374

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 259089433  160 SNPgGKTDEPkGKTEAYLEAIRKNIEWLKKHDKKGNKEDYDLSKMRDFINKQADAYVEKGILDKEEAEAIKRIYSSL 236
Cdd:pfam15467 375 QNT-EETDQP-GKSETYLEAIRKNIEWLKKHNKEGNKEDYDLSKLRDFMDQQVDSYIEKGILAKEEGDVIKRIYSSL 449
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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