Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 (EC 1.14.11.4) (Lysyl hydroxylase 2) (LH2)
1_MGGCT 6_ VKPQL 11_ LLLAL 16_ VLHPW 21_ NPCLG 26_ ADSEK 31_ PSSIP 36_ TDKLL 41_ VITVA 46_ TKESD 51_ GFHRF 56_ MQSAK 61_ YFNYT 66_ VKVLG 71_ QGEEW 76_ RGGDG 81_ INSIG 86_ GGQKV 91_ RLMKE 96_ VMEHY 101_ ADQDD 106_ LVVMF 111_ TECFD 116_ VIFAG 121_ GPEEV 126_ LKKFQ 131_ KANHK 136_ VVFAA 141_ DGILW 146_ PDKRL 151_ ADKYP 156_ VVHIG 161_ KRYLN 166_ SGGFI 171_ GYAPY 176_ VNRIV 181_ QQWNL 186_ QDNDD 191_ DQLFY 196_ TKVYI 201_ DPLKR 206_ EAINI 211_ TLDHK 216_ CKIFQ 221_ TLNGA 226_ VDEVV 231_ LKFEN 236_ GKARA 241_ KNTFY 246_ ETLPV 251_ AINGN 256_ GPTKI 261_ LLNYF 266_ GNYVP 271_ NSWTQ 276_ DNGCT 281_ LCEFD 286_ TVDLS 291_ AVDVH 296_ PNVSI 301_ GVFIE 306_ QPTPF 311_ LPRFL 316_ DILLT 321_ LDYPK 326_ EALKL 331_ FIHNK 336_ EVYHE 341_ KDIKV 346_ FFDKA 351_ KHEIK 356_ TIKIV 361_ GPEEN 366_ LSQAE 371_ ARNMG 376_ MDFCR 381_ QDEKC 386_ DYYFS 391_ VDADV 396_ VLTNP 401_ RTLKI 406_ LIEQN 411_ RKIIA 416_ PLVTR 421_ HGKLW 426_ SNFWG 431_ ALSPD 436_ GYYAR 441_ SEDYV 446_ DIVQG 451_ NRVGV 456_ WNVPY 461_ MANVY 466_ LIKGK 471_ TLRSE 476_ MNERN 481_ YFVRD 486_ KLDPD 491_ MALCR 496_ NAREM 501_ GVFMY 506_ ISNRH 511_ EFGRL 516_ LSTAN 521_ YNTSH 526_ YNNDL 531_ WQIFE 536_ NPVDW 541_ KEKYI 546_ NRDYS 551_ KIFTE 556_ NIVEQ 561_ PCPDV 566_ FWFPI 571_ FSEKA 576_ CDELV 581_ EEMEH 586_ YGKWS 591_ GGKHH 596_ DSRIS 601_ GGYEN 606_ VPTDD 611_ IHMKQ 616_ VDLEN 621_ VWLHF 626_ IREFI 631_ APVTL 636_ KVFAG 641_ YYTKG 646_ FALLN 651_ FVVKY 656_ SPERQ 661_ RSLRP 666_ HHDAS 671_ TFTIN 676_ IALNN 681_ VGEDF 686_ QGGGC 691_ KFLRY 696_ NCSIE 701_ SPRKG 706_ WSFMH 711_ PGRLT 716_ HLHEG 721_ LPVKN 726_ GTRYI 731_AVSFI
1: Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links