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Conserved domains on  [gi|7387805|sp|Q9WUG6|]
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RecName: Full=Insulin-like peptide INSL5; Short=Insulin-like peptide 5; AltName: Full=Relaxin/insulin-like factor 2; AltName: Full=Relaxin/insulin-like protein; Contains: RecName: Full=Insulin-like peptide INSL5 B chain; Contains: RecName: Full=Insulin-like peptide INSL5 A chain; Flags: Precursor

Protein Classification

IlGF_relaxin_like domain-containing protein (domain architecture ID 10137868)

IlGF_relaxin_like domain-containing protein

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 ...
25-135 8.47e-11

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: 53.48  E-value: 8.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387805   25 TVKLCGLDYVRTVIYICASSRWRRhleghfhsqqaetrnylqlldrhepskktlehslpktdlsgqelvrdpqapkeglW 104
Cdd:cd04365   1 VVKLCGRELVRAVIEICGGSRWRR-------------------------------------------------------L 25
                        90       100       110
                ....*....|....*....|....*....|....
gi 7387805  105 ELKKHSVVSR---RDLQALCCREGCSMKELSTLC 135
Cdd:cd04365  26 GLDTHSRKKRqfsRGLSEKCCKVGCTKEELAKLC 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 ...
25-135 8.47e-11

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: 53.48  E-value: 8.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387805   25 TVKLCGLDYVRTVIYICASSRWRRhleghfhsqqaetrnylqlldrhepskktlehslpktdlsgqelvrdpqapkeglW 104
Cdd:cd04365   1 VVKLCGRELVRAVIEICGGSRWRR-------------------------------------------------------L 25
                        90       100       110
                ....*....|....*....|....*....|....
gi 7387805  105 ELKKHSVVSR---RDLQALCCREGCSMKELSTLC 135
Cdd:cd04365  26 GLDTHSRKKRqfsRGLSEKCCKVGCTKEELAKLC 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 ...
25-135 8.47e-11

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: 53.48  E-value: 8.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7387805   25 TVKLCGLDYVRTVIYICASSRWRRhleghfhsqqaetrnylqlldrhepskktlehslpktdlsgqelvrdpqapkeglW 104
Cdd:cd04365   1 VVKLCGRELVRAVIEICGGSRWRR-------------------------------------------------------L 25
                        90       100       110
                ....*....|....*....|....*....|....
gi 7387805  105 ELKKHSVVSR---RDLQALCCREGCSMKELSTLC 135
Cdd:cd04365  26 GLDTHSRKKRqfsRGLSEKCCKVGCTKEELAKLC 59
IlGF_like cd00101
Insulin/insulin-like growth factor/relaxin family; insulin family of proteins. Members include ...
28-48 8.82e-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: 32.22  E-value: 8.82e-03
                        10        20
                ....*....|....*....|.
gi 7387805   28 LCGLDYVRTVIYICASSRWRR 48
Cdd:cd00101   1 LCGRELVRALIFVCGDRGFYR 21
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
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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