Search Results

Overview

Uniprot IDP00450
Protein NameCeruloplasmin
Gene NameCP
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
104 IKAETGDKVYVHLKN
110 DKVYVHLKNLASRPY
468 IRVTFHNKGAYPLSI
69 RIGRLYKKALYLQYT
712 YTGGMKQKYTVNQCR

Function

Multifunctional blue, copper-binding (6-7 atoms per molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to Fe(3+) without releasing radical oxygen species. It is involved in iron transport across the cell membrane (PubMed:16150804). Copper ions provide a large number of enzymatic activites. Oxidizes highly toxic ferrous ions to the ferric state for further incorporation onto apo-transferrins, catalyzes Cu(+) oxidation and promotes the oxidation of biogenic amines such as norepinephrin and serotonin (PubMed:14623105, PubMed:4643313, PubMed:5912351). Provides Cu(2+) ions for the ascorbate-mediated deaminase degradation of the heparan sulfate chains of GPC1 (By similarity). Has glutathione peroxidase-like activity, can remove both hydrogen peroxide and lipid hydroperoxide in the presence of thiols (PubMed:10481051). Acts as an inhibitor of the peroxidase activity of MPO (By similarity). Also shows NO-oxidase and NO2 synthase activities that determine endocrine NO homeostasis (PubMed:16906150)

Protein Sequence

10 MKILILGIFL 20 FLCSTPAWAK 30 EKHYYIGIIE 40 TTWDYASDHG 50 EKKLISVDTE 60 HSNIYLQNGP 70 DRIGRLYKKA 80 LYLQYTDETF 90 RTTIEKPVWL 100 GFLGPIIKAE 110 TGDKVYVHLK 120 NLASRPYTFH 130 SHGITYYKEH 140 EGAIYPDNTT 150 DFQRADDKVY 160 PGEQYTYMLL 170 ATEEQSPGEG 180 DGNCVTRIYH 190 SHIDAPKDIA 200 SGLIGPLIIC 210 KKDSLDKEKE 220 KHIDREFVVM 230 FSVVDENFSW 240 YLEDNIKTYC 250 SEPEKVDKDN 260 EDFQESNRMY 270 SVNGYTFGSL 280 PGLSMCAEDR 290 VKWYLFGMGN 300 EVDVHAAFFH 310 GQALTNKNYR 320 IDTINLFPAT 330 LFDAYMVAQN 340 PGEWMLSCQN 350 LNHLKAGLQA 360 FFQVQECNKS 370 SSKDNIRGKH 380 VRHYYIAAEE 390 IIWNYAPSGI 400 DIFTKENLTA 410 PGSDSAVFFE 420 QGTTRIGGSY 430 KKLVYREYTD 440 ASFTNRKERG 450 PEEEHLGILG 460 PVIWAEVGDT 470 IRVTFHNKGA 480 YPLSIEPIGV 490 RFNKNNEGTY 500 YSPNYNPQSR 510 SVPPSASHVA 520 PTETFTYEWT 530 VPKEVGPTNA 540 DPVCLAKMYY 550 SAVEPTKDIF 560 TGLIGPMKIC 570 KKGSLHANGR 580 QKDVDKEFYL 590 FPTVFDENES 600 LLLEDNIRMF 610 TTAPDQVDKE 620 DEDFQESNKM 630 HSMNGFMYGN 640 QPGLTMCKGD 650 SVVWYLFSAG 660 NEADVHGIYF 670 SGNTYLWRGE 680 RRDTANLFPQ 690 TSLTLHMWPD 700 TEGTFNVECL 710 TTDHYTGGMK 720 QKYTVNQCRR 730 QSEDSTFYLG 740 ERTYYIAAVE 750 VEWDYSPQRE 760 WEKELHHLQE 770 QNVSNAFLDK 780 GEFYIGSKYK 790 KVVYRQYTDS 800 TFRVPVERKA 810 EEEHLGILGP 820 QLHADVGDKV 830 KIIFKNMATR 840 PYSIHAHGVQ 850 TESSTVTPTL 860 PGETLTYVWK 870 IPERSGAGTE 880 DSACIPWAYY 890 STVDQVKDLY 900 SGLIGPLIVC 910 RRPYLKVFNP 920 RRKLEFALLF 930 LVFDENESWY 940 LDDNIKTYSD 950 HPEKVNKDDE 960 EFIESNKMHA 970 INGRMFGNLQ 980 GLTMHVGDEV 990 NWYLMGMGNE 1000 IDLHTVHFHG 1010 HSFQYKHRGV 1020 YSSDVFDIFP 1030 GTYQTLEMFP 1040 RTPGIWLLHC 1050 HVTDHIHAGM 1060 ETTYTVLQNE DTKSG

Gene Ontology

Classification GO ID Description
Cellular Component GO:0072562 blood microparticle
Cellular Component GO:0005788 endoplasmic reticulum lumen
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0005765 lysosomal membrane
Cellular Component GO:0005886 plasma membrane
Molecular Function GO:0005507 copper ion binding
Molecular Function GO:0004322 ferroxidase activity
Molecular Function GO:0004602 glutathione peroxidase activity
Molecular Function GO:0016491 oxidoreductase activity
Molecular Function GO:0016724 oxidoreductase activity, acting on metal ions, oxygen as acceptor
Molecular Function GO:0036479 peroxidase inhibitor activity
Molecular Function GO:0047066 phospholipid-hydroperoxide glutathione peroxidase activity
Molecular Function GO:0051087 protein-folding chaperone binding
Biological Process GO:0006878 intracellular copper ion homeostasis
Biological Process GO:0006879 intracellular iron ion homeostasis

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.