PKAT, KLD domain; This is the Kringle-like domain (KLD) found in Melanocyte protein PMEL, Transmembrane glycoprotein NMB (GPNMB) and TMEM130, which is downstream the PKD domain. It contains six highly conserved cysteine residues that form the disulphide bonds of mature PMEL dimers. (Chrystal et. al., Molecules 2021, 26(12), 3529; https://doi.org/10.3390/molecules26123529). This domain is perfectly conserved in PMEL and GPNMB which suggests that GPNMB also forms dimers. PMEL and GPNMB, together with TMEM130 (its most ancient paralogue), have a conserved domain architecture and have been recently described as the PKAT (PKD- and KLD-Associated Transmembrane) protein family (Chrystal et. al., Molecules 2021, 26(12), 3529; https://doi.org/10.3390/molecules26123529). PMEL and GPNMB share overlapping phenotypes and disease associations, such as melanin-based pigmentation, cancer, neurodegenerative disease and glaucoma.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 281371438  269 GSPPLHVCWGLK-PQCLALEDRECHPVLVTRTSF-NLTHVFQDPGDYC 314
Cdd:pfam20433   4 GSLPTEVCTVVSdPTCQTPQNTVCNPVSPSPECQlVLRRAFNGSGTYC 51

PKAT, KLD domain; This is the Kringle-like domain (KLD) found in Melanocyte protein PMEL, Transmembrane glycoprotein NMB (GPNMB) and TMEM130, which is downstream the PKD domain. It contains six highly conserved cysteine residues that form the disulphide bonds of mature PMEL dimers. (Chrystal et. al., Molecules 2021, 26(12), 3529; https://doi.org/10.3390/molecules26123529). This domain is perfectly conserved in PMEL and GPNMB which suggests that GPNMB also forms dimers. PMEL and GPNMB, together with TMEM130 (its most ancient paralogue), have a conserved domain architecture and have been recently described as the PKAT (PKD- and KLD-Associated Transmembrane) protein family (Chrystal et. al., Molecules 2021, 26(12), 3529; https://doi.org/10.3390/molecules26123529). PMEL and GPNMB share overlapping phenotypes and disease associations, such as melanin-based pigmentation, cancer, neurodegenerative disease and glaucoma.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 281371438  269 GSPPLHVCWGLK-PQCLALEDRECHPVLVTRTSF-NLTHVFQDPGDYC 314
Cdd:pfam20433   4 GSLPTEVCTVVSdPTCQTPQNTVCNPVSPSPECQlVLRRAFNGSGTYC 51

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 281371438 161 LSFLLHDPSDffkSASFFYRWDFGDGTMLITDNSVVYYNYSSPGTFTVKVRV 212
Cdd:cd00146   17 VTFSASDSSG---GSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTV 65

Uncharacterized conserved protein, PKD repeat domain [Function unknown];

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 281371438 179 YRWDFGDGTmlITDNSVVYYNYSSPGTFTVKVRVVAEWEQTklDTTKGII 228
Cdd:COG3291   27 YEWDFGDGT--TSTEANPSHTYTTPGTYTVTLTVTDAAGCS--DTTTKTI 72

PKAT, KLD domain; This is the Kringle-like domain (KLD) found in Melanocyte protein PMEL, Transmembrane glycoprotein NMB (GPNMB) and TMEM130, which is downstream the PKD domain. It contains six highly conserved cysteine residues that form the disulphide bonds of mature PMEL dimers. (Chrystal et. al., Molecules 2021, 26(12), 3529; https://doi.org/10.3390/molecules26123529). This domain is perfectly conserved in PMEL and GPNMB which suggests that GPNMB also forms dimers. PMEL and GPNMB, together with TMEM130 (its most ancient paralogue), have a conserved domain architecture and have been recently described as the PKAT (PKD- and KLD-Associated Transmembrane) protein family (Chrystal et. al., Molecules 2021, 26(12), 3529; https://doi.org/10.3390/molecules26123529). PMEL and GPNMB share overlapping phenotypes and disease associations, such as melanin-based pigmentation, cancer, neurodegenerative disease and glaucoma.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 281371438  269 GSPPLHVCWGLK-PQCLALEDRECHPVLVTRTSF-NLTHVFQDPGDYC 314
Cdd:pfam20433   4 GSLPTEVCTVVSdPTCQTPQNTVCNPVSPSPECQlVLRRAFNGSGTYC 51

polycystic kidney disease I (PKD) domain; similar to other cell-surface modules, with an IG-like fold; domain probably functions as a ligand binding site in protein-protein or protein-carbohydrate interactions; a single instance of the repeat is presented here. The domain is also found in microbial collagenases and chitinases.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 281371438 161 LSFLLHDPSDffkSASFFYRWDFGDGTMLITDNSVVYYNYSSPGTFTVKVRV 212
Cdd:cd00146   17 VTFSASDSSG---GSIVSYKWDFGDGEVSSSGEPTVTHTYTKPGTYTVTLTV 65

Repeats in polycystic kidney disease 1 (PKD1) and other proteins; Polycystic kidney disease 1 protein contains 14 repeats, present elsewhere such as in microbial collagenases.

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 281371438   178 FYRWDFGDGTmlITDNSVVYYNYSSPGTFTVKVRV 212
Cdd:smart00089  31 SYTWDFGDGT--SSTGPTVTHTYTKPGTYTVTLTV 63