Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a recently-identified subfamily composed of SH3BGR and similar proteins possessing significant sequence similarity to GRX, but without a redox active CXXC motif. The SH3BGR gene was cloned in an effort to identify genes mapping to chromosome 21, which could be involved in the pathogenesis of congenital heart disease affecting Down syndrome newborns. Several human SH3BGR-like (SH3BGRL) genes have been identified since, mapping to different locations in the chromosome. Of these, SH3BGRL3 was identified as a tumor necrosis factor (TNF) alpha inhibitory protein and was also named TIP-B1. Upregulation of expression of SH3BGRL3 is associated with differentiation. It has been suggested that it functions as a regulator of differentiation-related signal transduction pathways.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393683  53 IKKKQQDVLGFLEANKIGFEEKDIAANEENRKWMRENVPENSrpatGYPLPPQIFNESQYRGDYDAFFEARENNAVYAFL 132
Cdd:cd03030    15 IKKRQQEVLGFLEAKKIEFEEVDISMNEENRQWMRENVPNEN----GKPLPPQIFNGDEYCGDYEAFFEAKENNTLEEFL 90

                  ..
gi 2217393683 133 GL 134
Cdd:cd03030    91 KL 92

Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a recently-identified subfamily composed of SH3BGR and similar proteins possessing significant sequence similarity to GRX, but without a redox active CXXC motif. The SH3BGR gene was cloned in an effort to identify genes mapping to chromosome 21, which could be involved in the pathogenesis of congenital heart disease affecting Down syndrome newborns. Several human SH3BGR-like (SH3BGRL) genes have been identified since, mapping to different locations in the chromosome. Of these, SH3BGRL3 was identified as a tumor necrosis factor (TNF) alpha inhibitory protein and was also named TIP-B1. Upregulation of expression of SH3BGRL3 is associated with differentiation. It has been suggested that it functions as a regulator of differentiation-related signal transduction pathways.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393683  53 IKKKQQDVLGFLEANKIGFEEKDIAANEENRKWMRENVPENSrpatGYPLPPQIFNESQYRGDYDAFFEARENNAVYAFL 132
Cdd:cd03030    15 IKKRQQEVLGFLEAKKIEFEEVDISMNEENRQWMRENVPNEN----GKPLPPQIFNGDEYCGDYEAFFEAKENNTLEEFL 90

                  ..
gi 2217393683 133 GL 134
Cdd:cd03030    91 KL 92

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217393683  63 FLEANKIGFEEKDIAANEENRKWMREnvpensrpATGYPLPPQIFNESQYRGDYD 117
Cdd:COG0695    19 LLDEKGIPYEEIDVDEDPEAREELRE--------RSGRRTVPVIFIGGEHLGGFD 65

Glutaredoxin (GRX) family, SH3BGR (SH3 domain binding glutamic acid-rich protein) subfamily; a recently-identified subfamily composed of SH3BGR and similar proteins possessing significant sequence similarity to GRX, but without a redox active CXXC motif. The SH3BGR gene was cloned in an effort to identify genes mapping to chromosome 21, which could be involved in the pathogenesis of congenital heart disease affecting Down syndrome newborns. Several human SH3BGR-like (SH3BGRL) genes have been identified since, mapping to different locations in the chromosome. Of these, SH3BGRL3 was identified as a tumor necrosis factor (TNF) alpha inhibitory protein and was also named TIP-B1. Upregulation of expression of SH3BGRL3 is associated with differentiation. It has been suggested that it functions as a regulator of differentiation-related signal transduction pathways.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217393683  53 IKKKQQDVLGFLEANKIGFEEKDIAANEENRKWMRENVPENSrpatGYPLPPQIFNESQYRGDYDAFFEARENNAVYAFL 132
Cdd:cd03030    15 IKKRQQEVLGFLEAKKIEFEEVDISMNEENRQWMRENVPNEN----GKPLPPQIFNGDEYCGDYEAFFEAKENNTLEEFL 90

                  ..
gi 2217393683 133 GL 134
Cdd:cd03030    91 KL 92

Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217393683  54 KKKQQDVLGFLEANKIGFEEKDIAANEENRKWMRENvpensrpaTGYPLPPQIFNESQYRGDYDAFFEARE 124
Cdd:cd02066    10 CPYCKRAKRLLESLGIEFEEIDILEDGELREELKEL--------SGWPTVPQIFINGEFIGGYDDLKALHE 72