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Overview

Uniprot IDP02760
Protein NameProtein AMBP
Gene NameAMBP
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
100 ETSGAYEKTDTDGKF
106 EKTDTDGKFLYHKSK
111 DGKFLYHKSKWNITM
149 HGPTITAKLYGRAPQ
88 MTSTRWRKGVCEETS

Function

Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments (PubMed:11877257, PubMed:15683711, PubMed:22096585, PubMed:23157686, PubMed:23642167, PubMed:25698971, PubMed:32092412, PubMed:32823731). Intravascularly, plays a regulatory role in red cell homeostasis by preventing heme- and reactive oxygen species-induced cell damage. Binds and degrades free heme to protect fetal and adult red blood cells from hemolysis (PubMed:11877257, PubMed:32092412). Reduces extracellular methemoglobin, a Fe3+ (ferric) form of hemoglobin that cannot bind oxygen, back to the Fe2+ (ferrous) form deoxyhemoglobin, which has oxygen-carrying potential (PubMed:15683711). Upon acute inflammation, inhibits oxidation of low-density lipoprotein particles by MPO and limits vascular damage (PubMed:25698971). Extravascularly, protects from oxidation products formed on extracellular matrix structures and cell membranes. Catalyzes the reduction of carbonyl groups on oxidized collagen fibers and preserves cellular and extracellular matrix ultrastructures (PubMed:22096585, PubMed:23642167). Importantly, counteracts the oxidative damage at blood-placenta interface, preventing leakage of free fetal hemoglobin into the maternal circulation (PubMed:21356557). Intracellularly, has a role in maintaining mitochondrial redox homeostasis. Bound to complex I of the respiratory chain of mitochondria, may scavenge free radicals and preserve mitochondrial ATP synthesis. Protects renal tubule epithelial cells from heme-induced oxidative damage to mitochondria (PubMed:23157686, PubMed:32823731). Reduces cytochrome c from Fe3+ (ferric) to the Fe2+ (ferrous) state through formation of superoxide anion radicals in the presence of ascorbate or NADH/NADPH electron donor cofactors, ascorbate being the preferred cofactor (PubMed:15683711). Has a chaperone role in facilitating the correct folding of bikunin in the endoplasmic reticulum compartment (By similarity)

Protein Sequence

10 MRSLGALLLL 20 LSACLAVSAG 30 PVPTPPDNIQ 40 VQENFNISRI 50 YGKWYNLAIG 60 STCPWLKKIM 70 DRMTVSTLVL 80 GEGATEAEIS 90 MTSTRWRKGV 100 CEETSGAYEK 110 TDTDGKFLYH 120 KSKWNITMES 130 YVVHTNYDEY 140 AIFLTKKFSR 150 HHGPTITAKL 160 YGRAPQLRET 170 LLQDFRVVAQ 180 GVGIPEDSIF 190 TMADRGECVP 200 GEQEPEPILI 210 PRVRRAVLPQ 220 EEEGSGGGQL 230 VTEVTKKEDS 240 CQLGYSAGPC 250 MGMTSRYFYN 260 GTSMACETFQ 270 YGGCMGNGNN 280 FVTEKECLQT 290 CRTVAACNLP 300 IVRGPCRAFI 310 QLWAFDAVKG 320 KCVLFPYGGC 330 QGNGNKFYSE 340 KECREYCGVP 350 GDGDEELLRF SN

Gene Ontology

Classification GO ID Description
Cellular Component GO:0072562 blood microparticle
Molecular Function GO:0019855 calcium channel inhibitor activity
Molecular Function GO:0046904 calcium oxalate binding
Molecular Function GO:0030246 carbohydrate binding
Molecular Function GO:0020037 heme binding
Molecular Function GO:0019862 IgA binding
Molecular Function GO:0016491 oxidoreductase activity
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0004867 serine-type endopeptidase inhibitor activity
Biological Process GO:0007155 cell adhesion
Biological Process GO:0007565 female pregnancy
Biological Process GO:0042167 heme catabolic process
Biological Process GO:0050777 negative regulation of immune response
Biological Process GO:0046329 negative regulation of JNK cascade
Biological Process GO:0030163 protein catabolic process
Cellular Component GO:0009986 cell surface
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005783 endoplasmic reticulum
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0031012 extracellular matrix
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005615 extracellular space
Cellular Component GO:0005743 mitochondrial inner membrane
Cellular Component GO:0031965 nuclear membrane
Cellular Component GO:0005886 plasma membrane

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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.