NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|325296757|ref|NP_001191615|]
View 

insulin precursor [Aplysia californica]

Protein Classification

insulin family protein( domain architecture ID 10137877)

insulin family protein may play a variety of roles in controlling processes such as growth, differentiation, and reproduction

PubMed:  11445250|1322139

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
IlGF_insulin_bombyxin_like cd04366
IlGF_like family, insulin_bombyxin_like subgroup. Members include a number of peptides ...
 48-128 3.46e-05

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: 39.15  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325296757  48 LCGEDLHVIISNLCSSLGGNRRflakymvkrdtenvndklrgillnkkeafsyltkreasgSITCECCFNQCRIFELAQY 127
Cdd:cd04366    1 YCGRHLADTLALLCSEYNSPRR---------------------------------------GIVDECCRKSCTLDELLSY 41


                 .
gi 325296757 128 C 128
Cdd:cd04366   42 C 42
 
Name Accession Description Interval E-value
IlGF_insulin_bombyxin_like cd04366
IlGF_like family, insulin_bombyxin_like subgroup. Members include a number of peptides ...
 48-128 3.46e-05

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: 39.15  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325296757  48 LCGEDLHVIISNLCSSLGGNRRflakymvkrdtenvndklrgillnkkeafsyltkreasgSITCECCFNQCRIFELAQY 127
Cdd:cd04366    1 YCGRHLADTLALLCSEYNSPRR---------------------------------------GIVDECCRKSCTLDELLSY 41


                 .
gi 325296757 128 C 128
Cdd:cd04366   42 C 42
 
Name Accession Description Interval E-value
IlGF_insulin_bombyxin_like cd04366
IlGF_like family, insulin_bombyxin_like subgroup. Members include a number of peptides ...
 48-128 3.46e-05

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: 39.15  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325296757  48 LCGEDLHVIISNLCSSLGGNRRflakymvkrdtenvndklrgillnkkeafsyltkreasgSITCECCFNQCRIFELAQY 127
Cdd:cd04366    1 YCGRHLADTLALLCSEYNSPRR---------------------------------------GIVDECCRKSCTLDELLSY 41


                 .
gi 325296757 128 C 128
Cdd:cd04366   42 C 42
IlGF_like cd00101
Insulin/insulin-like growth factor/relaxin family; insulin family of proteins. Members include ...
 107-128 2.90e-03

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: 33.76  E-value: 2.90e-03
                         10        20
                 ....*....|....*....|..
gi 325296757 107 SGSITCECCFNQCRIFELAQYC 128
Cdd:cd00101   20 YRGIVDECCFRGCTLRELASYC 41
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH