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P3H3

Gene
P3H3
Protein
Prolyl 3-hydroxylase 3
Organism
Homo sapiens
Length
736 amino acids
Function
Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils. Required for normal hydroxylation of lysine residues in type I collagen chains in skin, bone, tendon, aorta and cornea. Required for normal skin stability via its role in hydroxylation of lysine residues in collagen alpha chains and in collagen fibril assembly. Apparently not required for normal prolyl 3-hydroxylation on collagen chains, possibly because it functions redundantly with other prolyl 3-hydroxylases.
Similarity
Belongs to the leprecan family.
Mass
81.837 kDa
Sequence
MLRLLRPLLLLLLLPPPGSPEPPGLTQLSPGAPPQAPDLLYADGLRAYAAGAWAPAVALLREALRSQAALGRVRLDCGASCAADPGAALPAVLLGAPEPDSGPGPTQGSWERQLLRAALRRADCLTQCAARRLGPGGAARLRVGSALRDAFRRREPYNYLQRAYYQLKKLDLAAAAAHTFFVANPMHLQMREDMAKYRRMSGVRPQSFRDLETPPHWAAYDTGLELLGRQEAGLALPRLEEALQGSLAQMESCRADCEGPEEQQGAEEEEDGAASQGGLYEAIAGHWIQVLQCRQRCVGETATRPGRSFPVPDFLPNQLRRLHEAHAQVGNLSQAIENVLSVLLFYPEDEAAKRALNQYQAQLGEPRPGLGPREDIQRFILRSLGEKRQLYYAMEHLGTSFKDPDPWTPAALIPEALREKLREDQEKRPWDHEPVKPKPLTYWKDVLLLEGVTLTQDSRQLNGSERAVLDGLLTPAECGVLLQLAKDAAGAGARSGYRGRRSPHTPHERFEGLTVLKAAQLARAGTVGSQGAKLLLEVSERVRTLTQAYFSPERPLHLSFTHLVCRSAIEGEQEQRMDLSHPVHADNCVLDPDTGECWREPPAYTYRDYSGLLYLNDDFQGGDLFFTEPNALTVTARVRPRCGRLVAFSSGVENPHGVWAVTRGRRCALALWHTWAPEHREQEWIEAKELLQESQEEEEEEEEEMPSKDPSPEPPSRRHQRVQDKTGRAPRVREEL

Gene
P3h3
Protein
Prolyl 3-hydroxylase 3
Organism
Mus musculus
Length
732 amino acids
Function
Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils (PubMed:27119146). Required for normal hydroxylation of lysine residues in type I collagen chains in skin, bone, tendon, aorta and cornea (PubMed:28115524). Required for normal skin stability via its role in hydroxylation of lysine residues in collagen alpha chains and in collagen fibril assembly (PubMed:27119146, PubMed:28115524). Apparently not required for normal prolyl 3-hydroxylation on collagen chains, possibly because it functions redundantly with other prolyl 3-hydroxylases (PubMed:28115524).
Similarity
Belongs to the leprecan family.
Mass
81.701 kDa
Sequence
MLRLLRLLLLLLLPPPGSPEPPEPPGLAQLSPGSPPQAPDLLYADGLRAYSAGAWAPAVALLREALRSRAALGRARQECGASCAAEPGAALPSQLLGAPHPVSGPGVWEPLLLRATLRRAECLTQCAVRRLGPGGAARLRVGSALRDAFRRREPYNYLQRAYYQLKKLDLAASAAHTFFVANPTHLQMREDMAKYRRMSAIRPQSFRDLVTPLYWAAYDTGLELLEQREAALALPQLEEALQGSLAHMESCRAACEGPEEHQGAEEEGEGSQGGLYEAIAGHWIRVLQCRQHCVADTATRPGRSFPVQDFLLSQLRRLHEAYAQVGNMSQAMENVLSVLLFYPEDEAAKKALNQYQTQLGEPRPDLGPREDIQRFILRSLGEKRQLYYAMEHLGTSFKDPDSWTPEALIPKALRERLREDQEKKPWDHQPPQQKPLAHWKDALLMEGVTLTQDAQQLNGSERAVLDGLLTSAECGVLLQLAKDAAQAGARSGYRGRRSPHSPHERFEGLTVLKAAQLARAGTVGRPGAKLLLEVSERVRTLTQAYFSPERPLHLSFTHLVCRSAIEGEQEQRMDLSHPVHADNCVLDPDTGECWREPPAYTYRDYSGLLYLNDDFKGGDLFFTQPNALTVTAQVRPRCGRLVAFSSGGENPHGVWAVTRGRRCALALWHTWAPEHSEQEWTEAKELLQEEEEEEEEEDILSRDPSPEPPSHKLQRVQEKAGKPRRVRVREEL