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Conserved domains on  [gi|297374794|ref|NP_001172012.1|]
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insulin-2 preproprotein [Mus musculus]

Protein Classification

IlGF_insulin_like domain-containing protein (domain architecture ID 10137879)

IlGF_insulin_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IlGF_insulin_like cd04367
IlGF_like family, insulin_like subgroup, specific to vertebrates. Members include a number of ...
26-110 4.07e-40

IlGF_like family, insulin_like subgroup, specific to vertebrates. Members include a number of peptides including insulin and insulin-like growth factors I and II, which play a variety of roles in controlling processes such as metabolism, growth and differentiation, and reproduction. On a cellular level they affect cell cycle, apoptosis, cell migration, and differentiation. With the exception of the insulin-like growth factors, the active forms of these peptide hormones are composed of two chains (A and B) linked by two disulfide bonds; the arrangement of four cysteines is conserved in the "A" chain: Cys1 is linked by a disulfide bond to Cys3, Cys2 and Cys4 are linked by interchain disulfide bonds to cysteines in the "B" chain. This alignment contains both chains, plus the intervening linker region, arranged as found in the propeptide form. Propeptides are cleaved to yield two separate chains linked covalently by the two disulfide bonds.


:

Pssm-ID: 239833  Cd Length: 79  Bit Score: 131.02  E-value: 4.07e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297374794  26 VKQHLCGSHLVEALYLVCGERGFFYTPMSRREVEDPQVAQLElgggpgAGDLQTLALEVAQQKRGIVDQCCTSICSLYQL 105
Cdd:cd04367    1 VNQHLCGSHLVDALYLVCGDRGFFYTPKRRRDVEDPLVPQEQ------AAGLQPQAQEEIKRKRGIVEQCCHNICSLYQL 74

                 ....*
gi 297374794 106 ENYCN 110
Cdd:cd04367   75 ENYCN 79
 
Name Accession Description Interval E-value
IlGF_insulin_like cd04367
IlGF_like family, insulin_like subgroup, specific to vertebrates. Members include a number of ...
26-110 4.07e-40

IlGF_like family, insulin_like subgroup, specific to vertebrates. Members include a number of peptides including insulin and insulin-like growth factors I and II, which play a variety of roles in controlling processes such as metabolism, growth and differentiation, and reproduction. On a cellular level they affect cell cycle, apoptosis, cell migration, and differentiation. With the exception of the insulin-like growth factors, the active forms of these peptide hormones are composed of two chains (A and B) linked by two disulfide bonds; the arrangement of four cysteines is conserved in the "A" chain: Cys1 is linked by a disulfide bond to Cys3, Cys2 and Cys4 are linked by interchain disulfide bonds to cysteines in the "B" chain. This alignment contains both chains, plus the intervening linker region, arranged as found in the propeptide form. Propeptides are cleaved to yield two separate chains linked covalently by the two disulfide bonds.


Pssm-ID: 239833  Cd Length: 79  Bit Score: 131.02  E-value: 4.07e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297374794  26 VKQHLCGSHLVEALYLVCGERGFFYTPMSRREVEDPQVAQLElgggpgAGDLQTLALEVAQQKRGIVDQCCTSICSLYQL 105
Cdd:cd04367    1 VNQHLCGSHLVDALYLVCGDRGFFYTPKRRRDVEDPLVPQEQ------AAGLQPQAQEEIKRKRGIVEQCCHNICSLYQL 74

                 ....*
gi 297374794 106 ENYCN 110
Cdd:cd04367   75 ENYCN 79
Insulin pfam00049
Insulin/IGF/Relaxin family; Superfamily includes insulins; relaxins; insulin-like growth ...
28-109 4.74e-31

Insulin/IGF/Relaxin family; Superfamily includes insulins; relaxins; insulin-like growth factor; and bombyxin. All are secreted regulatory hormones. Disulfide rich, all-alpha fold. Alignment includes B chain, linker (which is processed out of the final product), and A chain.


Pssm-ID: 306545  Cd Length: 77  Bit Score: 107.57  E-value: 4.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297374794   28 QHLCGSHLVEALYLVCGERGFFYTPMSRrevEDPQVAQLELGggPGAGDLQTLALEVAQQKRGIVDQCCTSICSLYQLEN 107
Cdd:pfam00049   1 QHLCGRHLVRALYLVCGERGFFYTAPYW---PRPQVEQLPDG--EGAELKYLGADEHSRRKRGIVEECCHRPCTLDQLES 75

                  ..
gi 297374794  108 YC 109
Cdd:pfam00049  76 YC 77
IlGF smart00078
Insulin / insulin-like growth factor / relaxin family; Family of proteins including insulin, ...
28-109 1.92e-30

Insulin / insulin-like growth factor / relaxin family; Family of proteins including insulin, relaxin, and IGFs. Insulin decreases blood glucose concentration.


Pssm-ID: 214506  Cd Length: 66  Bit Score: 105.97  E-value: 1.92e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297374794    28 QHLCGSHLVEALYLVCGERGFFYTPMSRREVEDPQVAQlelgggpgagdlqtlaLEVAQQKRGIVDQCCTSICSLYQLEN 107
Cdd:smart00078   1 QHLCGRHLVRALYLVCGERGFFYSPKSRRYAPYGQVPP----------------LEERRGKRGIVEQCCHRGCSLYDLES 64

                   ..
gi 297374794   108 YC 109
Cdd:smart00078  65 YC 66
 
Name Accession Description Interval E-value
IlGF_insulin_like cd04367
IlGF_like family, insulin_like subgroup, specific to vertebrates. Members include a number of ...
26-110 4.07e-40

IlGF_like family, insulin_like subgroup, specific to vertebrates. Members include a number of peptides including insulin and insulin-like growth factors I and II, which play a variety of roles in controlling processes such as metabolism, growth and differentiation, and reproduction. On a cellular level they affect cell cycle, apoptosis, cell migration, and differentiation. With the exception of the insulin-like growth factors, the active forms of these peptide hormones are composed of two chains (A and B) linked by two disulfide bonds; the arrangement of four cysteines is conserved in the "A" chain: Cys1 is linked by a disulfide bond to Cys3, Cys2 and Cys4 are linked by interchain disulfide bonds to cysteines in the "B" chain. This alignment contains both chains, plus the intervening linker region, arranged as found in the propeptide form. Propeptides are cleaved to yield two separate chains linked covalently by the two disulfide bonds.


Pssm-ID: 239833  Cd Length: 79  Bit Score: 131.02  E-value: 4.07e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297374794  26 VKQHLCGSHLVEALYLVCGERGFFYTPMSRREVEDPQVAQLElgggpgAGDLQTLALEVAQQKRGIVDQCCTSICSLYQL 105
Cdd:cd04367    1 VNQHLCGSHLVDALYLVCGDRGFFYTPKRRRDVEDPLVPQEQ------AAGLQPQAQEEIKRKRGIVEQCCHNICSLYQL 74

                 ....*
gi 297374794 106 ENYCN 110
Cdd:cd04367   75 ENYCN 79
Insulin pfam00049
Insulin/IGF/Relaxin family; Superfamily includes insulins; relaxins; insulin-like growth ...
28-109 4.74e-31

Insulin/IGF/Relaxin family; Superfamily includes insulins; relaxins; insulin-like growth factor; and bombyxin. All are secreted regulatory hormones. Disulfide rich, all-alpha fold. Alignment includes B chain, linker (which is processed out of the final product), and A chain.


Pssm-ID: 306545  Cd Length: 77  Bit Score: 107.57  E-value: 4.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297374794   28 QHLCGSHLVEALYLVCGERGFFYTPMSRrevEDPQVAQLELGggPGAGDLQTLALEVAQQKRGIVDQCCTSICSLYQLEN 107
Cdd:pfam00049   1 QHLCGRHLVRALYLVCGERGFFYTAPYW---PRPQVEQLPDG--EGAELKYLGADEHSRRKRGIVEECCHRPCTLDQLES 75

                  ..
gi 297374794  108 YC 109
Cdd:pfam00049  76 YC 77
IlGF smart00078
Insulin / insulin-like growth factor / relaxin family; Family of proteins including insulin, ...
28-109 1.92e-30

Insulin / insulin-like growth factor / relaxin family; Family of proteins including insulin, relaxin, and IGFs. Insulin decreases blood glucose concentration.


Pssm-ID: 214506  Cd Length: 66  Bit Score: 105.97  E-value: 1.92e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297374794    28 QHLCGSHLVEALYLVCGERGFFYTPMSRREVEDPQVAQlelgggpgagdlqtlaLEVAQQKRGIVDQCCTSICSLYQLEN 107
Cdd:smart00078   1 QHLCGRHLVRALYLVCGERGFFYSPKSRRYAPYGQVPP----------------LEERRGKRGIVEQCCHRGCSLYDLES 64

                   ..
gi 297374794   108 YC 109
Cdd:smart00078  65 YC 66
IlGF cd04368
IlGF, insulin_like growth factors; specific to vertebrates. Members include a number of ...
30-109 5.27e-11

IlGF, insulin_like growth factors; specific to vertebrates. Members include a number of peptides including insulin-like growth factors I and II, which play a variety of roles in controlling processes such as growth, differentiation, and reproduction. On a cellular level they affect cell cycle, apoptosis, cell migration, proliferation, and differentiation. Typically, the active forms of these peptide hormones are single chains cross-linked by three disulfide bonds.


Pssm-ID: 239834  Cd Length: 67  Bit Score: 55.08  E-value: 5.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297374794  30 LCGSHLVEALYLVCGERGF-FYTPMSRREvedpqvaqlelgggpgagdlqtlalEVAQQKRGIVDQCCTSICSLYQLENY 108
Cdd:cd04368    5 LCGGELVDTLQFVCGDRGFyFSKPTGYGS-------------------------SRRRPNRGIVEECCFRSCDLRLLEMY 59

                 .
gi 297374794 109 C 109
Cdd:cd04368   60 C 60
IlGF_like cd00101
Insulin/insulin-like growth factor/relaxin family; insulin family of proteins. Members include ...
30-109 1.08e-10

Insulin/insulin-like growth factor/relaxin family; insulin family of proteins. Members include a number of active peptides which are evolutionary related including insulin, relaxin, prorelaxin, insulin-like growth factors I and II, mammalian Leydig cell-specific insulin-like peptide (gene INSL3), early placenta insulin-like peptide (ELIP; gene INSL4), insect prothoracicotropic hormone (bombyxin), locust insulin-related peptide (LIRP), molluscan insulin-related peptides 1 to 5 (MIP), and C. elegans insulin-like peptides. Typically, the active forms of these peptide hormones are composed of two chains (A and B) linked by two disulfide bonds; the arrangement of four cysteines is conserved in the "A" chain: Cys1 is linked by a disulfide bond to Cys3, Cys2 and Cys4 are linked by interchain disulfide bonds to cysteines in the "B" chain. This alignment contains both chains, plus the intervening linker region, arranged as found in the propeptide form. Propeptides are cleaved to yield two separate chains linked covalently by the two disulfide bonds.


Pssm-ID: 238049  Cd Length: 41  Bit Score: 53.79  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297374794  30 LCGSHLVEALYLVCGERGFFytpmsrrevedpqvaqlelgggpgagdlqtlalevaqqkRGIVDQCCTSICSLYQLENYC 109
Cdd:cd00101    1 LCGRELVRALIFVCGDRGFY---------------------------------------RGIVDECCFRGCTLRELASYC 41
IlGF_insulin_bombyxin_like cd04366
IlGF_like family, insulin_bombyxin_like subgroup. Members include a number of peptides ...
30-109 9.34e-07

IlGF_like family, insulin_bombyxin_like subgroup. Members include a number of peptides including insulin, insulin-like growth factors I and II, insect prothoracicotropic hormone (bombyxin), locust insulin-related peptide (LIRP), molluscan insulin-related peptides 1 to 5 (MIP), and C. elegans insulin-like peptides. With the exception of insulin-like growth factors, the active forms of these peptide hormones are composed of two chains (A and B) linked by two disulfide bonds; the arrangement of four cysteines is conserved in the "A" chain: Cys1 is linked by a disulfide bond to Cys3, Cys2 and Cys4 are linked by interchain disulfide bonds to cysteines in the "B" chain. This alignment contains both chains, plus the intervening linker region, arranged as found in the propeptide form. Propeptides are cleaved to yield two separate chains linked covalently by the two disulfide bonds.


Pssm-ID: 239832  Cd Length: 42  Bit Score: 42.61  E-value: 9.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297374794  30 LCGSHLVEALYLVCGERGFFytpmsrrevedpqvaqlelgggpgagdlqtlalevaqqKRGIVDQCCTSICSLYQLENYC 109
Cdd:cd04366    1 YCGRHLADTLALLCSEYNSP--------------------------------------RRGIVDECCRKSCTLDELLSYC 42
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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