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Conserved domains on  [gi|937346086|ref|NP_001302418|]
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insulin-like growth factor II isoform 2 preproprotein [Mus musculus]

Protein Classification

insulin-like growth factor 2( domain architecture ID 10137888)

insulin-like growth factor 2 (IlGF2) plays 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; includes C-terminal IlGF2 E-peptide

Gene Symbol:  IGF2
Gene Ontology:  GO:0008083|GO:0005102
PubMed:  24593700

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IlGF cd04368
IlGF, insulin_like growth factors; specific to vertebrates. Members include a number of ...
 28-91 1.31e-37

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: 124.03  E-value: 1.31e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937346086  28 PGETLCGGELVDTLQFVCSDRGFYFSRPSSRAN---RRSRGIVEECCFRSCDLALLETYCATPAKSE 91
Cdd:cd04368    1 GPETLCGGELVDTLQFVCGDRGFYFSKPTGYGSsrrRPNRGIVEECCFRSCDLRLLEMYCAKPKKSE 67
IGF2_C pfam08365
Insulin-like growth factor II E-peptide; This domain is found at the C-terminal domain of the ...
 112-166 4.63e-25

Insulin-like growth factor II E-peptide; This domain is found at the C-terminal domain of the insulin-like growth factor II (IGF-2, also see pfam00049) in vertebrates and seems to represent the E-peptide.


:

Pssm-ID: 462445  Cd Length: 56  Bit Score: 91.86  E-value: 4.63e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 937346086  112 KFFQYDTWRQ-SAGRLRRGLPALLRARRGRMLAKELKEFREAKRHRPLIVLPPKDP 166
Cdd:pfam08365   1 KYSKYDVWQQkSAQRLRRGLPAILRARRGRRQAEELEAFEEAKRHRPLISLPSQDP 56
 
Name Accession Description Interval E-value
IlGF cd04368
IlGF, insulin_like growth factors; specific to vertebrates. Members include a number of ...
 28-91 1.31e-37

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: 124.03  E-value: 1.31e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937346086  28 PGETLCGGELVDTLQFVCSDRGFYFSRPSSRAN---RRSRGIVEECCFRSCDLALLETYCATPAKSE 91
Cdd:cd04368    1 GPETLCGGELVDTLQFVCGDRGFYFSKPTGYGSsrrRPNRGIVEECCFRSCDLRLLEMYCAKPKKSE 67
IGF2_C pfam08365
Insulin-like growth factor II E-peptide; This domain is found at the C-terminal domain of the ...
 112-166 4.63e-25

Insulin-like growth factor II E-peptide; This domain is found at the C-terminal domain of the insulin-like growth factor II (IGF-2, also see pfam00049) in vertebrates and seems to represent the E-peptide.


Pssm-ID: 462445  Cd Length: 56  Bit Score: 91.86  E-value: 4.63e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 937346086  112 KFFQYDTWRQ-SAGRLRRGLPALLRARRGRMLAKELKEFREAKRHRPLIVLPPKDP 166
Cdd:pfam08365   1 KYSKYDVWQQkSAQRLRRGLPAILRARRGRRQAEELEAFEEAKRHRPLISLPSQDP 56
IlGF smart00078
Insulin / insulin-like growth factor / relaxin family; Family of proteins including insulin, ...
 30-84 1.44e-19

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: 77.85  E-value: 1.44e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937346086    30 ETLCGGELVDTLQFVCSDRGFYFSRPSSRAN-----------RRSRGIVEECCFRSCDLALLETYC 84
Cdd:smart00078   1 QHLCGRHLVRALYLVCGERGFFYSPKSRRYApygqvppleerRGKRGIVEQCCHRGCSLYDLESYC 66
Insulin pfam00049
Insulin/IGF/Relaxin family; Superfamily includes insulins; relaxins; insulin-like growth ...
 30-84 8.41e-17

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: 459651  Cd Length: 77  Bit Score: 70.97  E-value: 8.41e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937346086   30 ETLCGGELVDTLQFVCSDRGFYFSrPSSRAN-----------------------RRSRGIVEECCFRSCDLALLETYC 84
Cdd:pfam00049   1 QHLCGRHLVRALYLVCGDRGFFYA-PKPREDpqveqlpdgegaelkylgadehsRRKRGIVEECCHRPCTLDQLESYC 77
 
Name Accession Description Interval E-value
IlGF cd04368
IlGF, insulin_like growth factors; specific to vertebrates. Members include a number of ...
 28-91 1.31e-37

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: 124.03  E-value: 1.31e-37
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 937346086  28 PGETLCGGELVDTLQFVCSDRGFYFSRPSSRAN---RRSRGIVEECCFRSCDLALLETYCATPAKSE 91
Cdd:cd04368    1 GPETLCGGELVDTLQFVCGDRGFYFSKPTGYGSsrrRPNRGIVEECCFRSCDLRLLEMYCAKPKKSE 67
IGF2_C pfam08365
Insulin-like growth factor II E-peptide; This domain is found at the C-terminal domain of the ...
 112-166 4.63e-25

Insulin-like growth factor II E-peptide; This domain is found at the C-terminal domain of the insulin-like growth factor II (IGF-2, also see pfam00049) in vertebrates and seems to represent the E-peptide.


Pssm-ID: 462445  Cd Length: 56  Bit Score: 91.86  E-value: 4.63e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 937346086  112 KFFQYDTWRQ-SAGRLRRGLPALLRARRGRMLAKELKEFREAKRHRPLIVLPPKDP 166
Cdd:pfam08365   1 KYSKYDVWQQkSAQRLRRGLPAILRARRGRRQAEELEAFEEAKRHRPLISLPSQDP 56
IlGF smart00078
Insulin / insulin-like growth factor / relaxin family; Family of proteins including insulin, ...
 30-84 1.44e-19

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: 77.85  E-value: 1.44e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937346086    30 ETLCGGELVDTLQFVCSDRGFYFSRPSSRAN-----------RRSRGIVEECCFRSCDLALLETYC 84
Cdd:smart00078   1 QHLCGRHLVRALYLVCGERGFFYSPKSRRYApygqvppleerRGKRGIVEQCCHRGCSLYDLESYC 66
Insulin pfam00049
Insulin/IGF/Relaxin family; Superfamily includes insulins; relaxins; insulin-like growth ...
 30-84 8.41e-17

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: 459651  Cd Length: 77  Bit Score: 70.97  E-value: 8.41e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937346086   30 ETLCGGELVDTLQFVCSDRGFYFSrPSSRAN-----------------------RRSRGIVEECCFRSCDLALLETYC 84
Cdd:pfam00049   1 QHLCGRHLVRALYLVCGDRGFFYA-PKPREDpqveqlpdgegaelkylgadehsRRKRGIVEECCHRPCTLDQLESYC 77
IlGF_insulin_like cd04367
IlGF_like family, insulin_like subgroup, specific to vertebrates. Members include a number of ...
 28-84 1.47e-16

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: 70.55  E-value: 1.47e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 937346086  28 PGETLCGGELVDTLQFVCSDRGFYFSRPSSRAN---------------------RRSRGIVEECCFRSCDLALLETYC 84
Cdd:cd04367    1 VNQHLCGSHLVDALYLVCGDRGFFYTPKRRRDVedplvpqeqaaglqpqaqeeiKRKRGIVEQCCHNICSLYQLENYC 78
IlGF_like cd00101
Insulin/insulin-like growth factor/relaxin family; insulin family of proteins. Members include ...
 32-84 1.24e-15

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: 66.88  E-value: 1.24e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 937346086  32 LCGGELVDTLQFVCSDRGFYfsrpssranrrsRGIVEECCFRSCDLALLETYC 84
Cdd:cd00101    1 LCGRELVRALIFVCGDRGFY------------RGIVDECCFRGCTLRELASYC 41
IlGF_insulin_bombyxin_like cd04366
IlGF_like family, insulin_bombyxin_like subgroup. Members include a number of peptides ...
 32-84 2.22e-11

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: 56.10  E-value: 2.22e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 937346086  32 LCGGELVDTLQFVCSDRGFyfsrpssranrRSRGIVEECCFRSCDLALLETYC 84
Cdd:cd04366    1 YCGRHLADTLALLCSEYNS-----------PRRGIVDECCRKSCTLDELLSYC 42
IlGF_relaxin_like cd04365
IlGF_like family, relaxin_like subgroup, specific to vertebrates. Members include a number of ...
 32-84 2.92e-04

IlGF_like family, relaxin_like subgroup, specific to vertebrates. Members include a number of active peptides including (pro)relaxin, mammalian Leydig cell-specific insulin-like peptide (gene INSL3), early placenta insulin-like peptide (ELIP; gene INSL4), and insulin-like peptides 5 (INSL5) and 6 (INSL6). Members of this subgroup are widely expressed in testes (INSL3, INSL6), decidua, placenta, prostate, corpus luteum, brain (various relaxins), GI tract, and kidney (INSL5) where they serve a variety of functions in parturition and development. 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: 239831  Cd Length: 59  Bit Score: 37.30  E-value: 2.92e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 937346086  32 LCGGELVDTLQFVC--SDRGFYFSRPSSRANRR-SRGIVEECCFRSCDLALLETYC 84
Cdd:cd04365    4 LCGRELVRAVIEICggSRWRRLGLDTHSRKKRQfSRGLSEKCCKVGCTKEELAKLC 59
 
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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