Prolyl 3-hydroxylase 3 (EC 1.14.11.7) (Leprecan-like protein 2) (Protein B)
1_MLRLL 6_ RPLLL 11_ LLLLP 16_ PPGSP 21_ EPPGL 26_ TQLSP 31_ GAPPQ 36_ APDLL 41_ YADGL 46_ RAYAA 51_ GAWAP 56_ AVALL 61_ REALR 66_ SQAAL 71_ GRVRL 76_ DCGAS 81_ CAADP 86_ GAALP 91_ AVLLG 96_ APEPD 101_ SGPGP 106_ TQGSW 111_ ERQLL 116_ RAALR 121_ RADCL 126_ TQCAA 131_ RRLGP 136_ GGAAR 141_ LRVGS 146_ ALRDA 151_ FRRRE 156_ PYNYL 161_ QRAYY 166_ QLKKL 171_ DLAAA 176_ AAHTF 181_ FVANP 186_ MHLQM 191_ REDMA 196_ KYRRM 201_ SGVRP 206_ QSFRD 211_ LETPP 216_ HWAAY 221_ DTGLE 226_ LLGRQ 231_ EAGLA 236_ LPRLE 241_ EALQG 246_ SLAQM 251_ ESCRA 256_ DCEGP 261_ EEQQG 266_ AEEEE 271_ DGAAS 276_ QGGLY 281_ EAIAG 286_ HWIQV 291_ LQCRQ 296_ RCVGE 301_ TATRP 306_ GRSFP 311_ VPDFL 316_ PNQLR 321_ RLHEA 326_ HAQVG 331_ NLSQA 336_ IENVL 341_ SVLLF 346_ YPEDE 351_ AAKRA 356_ LNQYQ 361_ AQLGE 366_ PRPGL 371_ GPRED 376_ IQRFI 381_ LRSLG 386_ EKRQL 391_ YYAME 396_ HLGTS 401_ FKDPD 406_ PWTPA 411_ ALIPE 416_ ALREK 421_ LREDQ 426_ EKRPW 431_ DHEPV 436_ KPKPL 441_ TYWKD 446_ VLLLE 451_ GVTLT 456_ QDSRQ 461_ LNGSE 466_ RAVLD 471_ GLLTP 476_ AECGV 481_ LLQLA 486_ KDAAG 491_ AGARS 496_ GYRGR 501_ RSPHT 506_ PHERF 511_ EGLTV 516_ LKAAQ 521_ LARAG 526_ TVGSQ 531_ GAKLL 536_ LEVSE 541_ RVRTL 546_ TQAYF 551_ SPERP 556_ LHLSF 561_ THLVC 566_ RSAIE 571_ GEQEQ 576_ RMDLS 581_ HPVHA 586_ DNCVL 591_ DPDTG 596_ ECWRE 601_ PPAYT 606_ YRDYS 611_ GLLYL 616_ NDDFQ 621_ GGDLF 626_ FTEPN 631_ ALTVT 636_ ARVRP 641_ RCGRL 646_ VAFSS 651_ GVENP 656_ HGVWA 661_ VTRGR 666_ RCALA 671_ LWHTW 676_ APEHR 681_ EQEWI 686_ EAKEL 691_ LQESQ 696_ EEEEE 701_ EEEEM 706_ PSKDP 711_ SPEPP 716_ SRRHQ 721_ RVQDK 726_ TGRAP 731_RVREE
1: 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