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Conserved domains on  [gi|38258558|sp|Q8CHK2|]
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RecName: Full=Relaxin-3; AltName: Full=Insulin-like peptide INSL7; Short=Insulin-like peptide 7; AltName: Full=Prorelaxin M3; Contains: RecName: Full=Relaxin-3 B chain; Contains: RecName: Full=Relaxin-3 A chain; Flags: Precursor

Protein Classification

relaxin family protein( domain architecture ID 10137868)

relaxin family protein or peptide such as human H1 relaxin, H2 relaxin, H3 relaxin, insulin-like peptide (INSL)3, INSL4, INSL5, and INSL6; the actions of relaxin peptides are mediated by relaxin family peptide receptors (RXFPs)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IlGF_relaxin_like cd04365
IlGF_like family, relaxin_like subgroup, specific to vertebrates. Members include a number of ...
 30-141 7.42e-15

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: 64.26  E-value: 7.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38258558  30 GVKLCGREFIRAVIFTCGGSRWRRadilaheslgdffadgeantdhlaseldeavgssewlaltkspqafyggraswQGS 109
Cdd:cd04365   1 VVKLCGRELVRAVIEICGGSRWRR-----------------------------------------------------LGL 27

                        90       100       110
                ....*....|....*....|....*....|..
gi 38258558 110 PGVVRGSRDVLAGLSSSCCEWGCSKSQISSLC 141
Cdd:cd04365  28 DTHSRKKRQFSRGLSEKCCKVGCTKEELAKLC 59
 
Name Accession Description Interval E-value
IlGF_relaxin_like cd04365
IlGF_like family, relaxin_like subgroup, specific to vertebrates. Members include a number of ...
 30-141 7.42e-15

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: 64.26  E-value: 7.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38258558  30 GVKLCGREFIRAVIFTCGGSRWRRadilaheslgdffadgeantdhlaseldeavgssewlaltkspqafyggraswQGS 109
Cdd:cd04365   1 VVKLCGRELVRAVIEICGGSRWRR-----------------------------------------------------LGL 27

                        90       100       110
                ....*....|....*....|....*....|..
gi 38258558 110 PGVVRGSRDVLAGLSSSCCEWGCSKSQISSLC 141
Cdd:cd04365  28 DTHSRKKRQFSRGLSEKCCKVGCTKEELAKLC 59
IlGF smart00078
Insulin / insulin-like growth factor / relaxin family; Family of proteins including insulin, ...
 32-141 3.00e-06

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: 42.41  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38258558     32 KLCGREFIRAVIFTCGGSRWRRadilaheslgdffadgeantdhlaseldeavgssewlaltkSPQAFYGGRASWQGSPG 111
Cdd:smart00078   2 HLCGRHLVRALYLVCGERGFFY-----------------------------------------SPKSRRYAPYGQVPPLE 40

                           90       100       110
                   ....*....|....*....|....*....|
gi 38258558    112 VVRGSRdvlaGLSSSCCEWGCSKSQISSLC 141
Cdd:smart00078  41 ERRGKR----GIVEQCCHRGCSLYDLESYC 66
 
Name Accession Description Interval E-value
IlGF_relaxin_like cd04365
IlGF_like family, relaxin_like subgroup, specific to vertebrates. Members include a number of ...
 30-141 7.42e-15

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: 64.26  E-value: 7.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38258558  30 GVKLCGREFIRAVIFTCGGSRWRRadilaheslgdffadgeantdhlaseldeavgssewlaltkspqafyggraswQGS 109
Cdd:cd04365   1 VVKLCGRELVRAVIEICGGSRWRR-----------------------------------------------------LGL 27

                        90       100       110
                ....*....|....*....|....*....|..
gi 38258558 110 PGVVRGSRDVLAGLSSSCCEWGCSKSQISSLC 141
Cdd:cd04365  28 DTHSRKKRQFSRGLSEKCCKVGCTKEELAKLC 59
IlGF smart00078
Insulin / insulin-like growth factor / relaxin family; Family of proteins including insulin, ...
 32-141 3.00e-06

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: 42.41  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38258558     32 KLCGREFIRAVIFTCGGSRWRRadilaheslgdffadgeantdhlaseldeavgssewlaltkSPQAFYGGRASWQGSPG 111
Cdd:smart00078   2 HLCGRHLVRALYLVCGERGFFY-----------------------------------------SPKSRRYAPYGQVPPLE 40

                           90       100       110
                   ....*....|....*....|....*....|
gi 38258558    112 VVRGSRdvlaGLSSSCCEWGCSKSQISSLC 141
Cdd:smart00078  41 ERRGKR----GIVEQCCHRGCSLYDLESYC 66
IlGF_like cd00101
Insulin/insulin-like growth factor/relaxin family; insulin family of proteins. Members include ...
 33-53 9.70e-05

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: 37.61  E-value: 9.70e-05
                        10        20
                ....*....|....*....|.
gi 38258558  33 LCGREFIRAVIFTCGGSRWRR 53
Cdd:cd00101   1 LCGRELVRALIFVCGDRGFYR 21
 
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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