P02760 Trypstatin AMBP 9606 None SL-0178 SL-0182 [Alpha-1-microglobulin]: Secreted {ECO:0000269|PubMed:11877257, ECO:0000269|PubMed:32092412}. Endoplasmic reticulum {ECO:0000269|PubMed:22096585}. Cytoplasm, cytosol {ECO:0000269|PubMed:32092412}. Cell membrane {ECO:0000269|PubMed:22096585, ECO:0000269|PubMed:32092412}; Peripheral membrane protein {ECO:0000305|PubMed:22096585, ECO:0000305|PubMed:32092412}. Nucleus membrane {ECO:0000269|PubMed:22096585}; Peripheral membrane protein {ECO:0000305|PubMed:22096585}. Mitochondrion inner membrane {ECO:0000305|PubMed:23157686}; Peripheral membrane protein {ECO:0000305|PubMed:23157686}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:22096585}. Note=The cellular uptake occurs via a non-endocytotic pathway and allows for localization to various membrane structures. A specific binding to plasma membrane suggests the presence of a cell receptor, yet to be identified. Directly binds collagen fibers type I. {ECO:0000269|PubMed:22096585}. UNIPROT P02760 UNIPROT P00977 UNIPROT P02759 UNIPROT P78491 UNIPROT Q2TU33 UNIPROT Q5TBD7 UNIPROT Q9UC58 UNIPROT Q9UDI8 PDB 1BIK PDB 3QKG PDB 4ES7 PDB 4U30 PDB 6EJ7 PDB 6EJ8 PDB 6EJ9 PDB 6EJA PDB 6EJB PDB 6EJC PDB 6EJD Pfam PF00014 Pfam PF00061 PROSITE PS00280 PROSITE PS50279 PROSITE PS00213 OMIM 176870 DisGeNET 259 [Alpha-1-microglobulin]: 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:32823731, PubMed:32092412). 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:23642167, PubMed:22096585). 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). {ECO:0000250|UniProtKB:Q07456, ECO:0000269|PubMed:11877257, ECO:0000269|PubMed:15683711, ECO:0000269|PubMed:21356557, ECO:0000269|PubMed:22096585, ECO:0000269|PubMed:23157686, ECO:0000269|PubMed:23642167, ECO:0000269|PubMed:25698971, ECO:0000269|PubMed:32092412, ECO:0000269|PubMed:32823731}. [Inter-alpha-trypsin inhibitor light chain]: Kunitz-type serine protease inhibitor and structural component of extracellular matrix with a role in extracellular space remodeling and cell adhesion (PubMed:25301953, PubMed:20463016). Among others, has antiprotease activity toward kallikrein, a protease involved in airway inflammation; inhibits GZMK/granzyme, a granule-stored serine protease involved in NK and T cell cytotoxic responses; and inhibits PLG/plasmin, a protease required for activation of matrix metalloproteinases (PubMed:16873769, PubMed:10480954, PubMed:15917224). As part of I-alpha-I complex, provides for the heavy chains to be transferred from I-alpha-I complex to hyaluronan in the presence of TNFAIP6, in a dynamic process that releases free bikunin and remodels extracellular matrix proteoglycan structures. Free bikunin, but not its heavy chain-bound form, acts as potent protease inhibitor in airway secretions (PubMed:16873769). Part of hyaluronan-rich extracellular matrix that surrounds oocyte during cumulus oophorus expansion, an indispensable process for proper ovulation (By similarity). Also inhibits calcium oxalate crystallization (PubMed:7676539). {ECO:0000250|UniProtKB:Q07456, ECO:0000269|PubMed:10480954, ECO:0000269|PubMed:15917224, ECO:0000269|PubMed:16873769, ECO:0000269|PubMed:20463016, ECO:0000269|PubMed:25301953, ECO:0000269|PubMed:7676539}. [Trypstatin]: Kunitz-type serine protease inhibitor. Has high catalytic efficiency for F10/blood coagulation factor Xa and may act as an anticoagulant by inhibiting prothrombin activation. Inhibits trypsin and mast cell CMA1/chymase and tryptase proteases. {ECO:0000250|UniProtKB:Q64240}. P69616 EBI-7810311 0.53 P07858 EBI-7970369 0.60 Q92569 EBI-2115171 0.00 P62993 EBI-2115716 0.00 P42336 EBI-2116612 0.00 P10176 EBI-3904736 0.37 Q9Y4D1 EBI-3908964 0.37 P40763 EBI-3926609 0.37 Q99XU0 EBI-8852714 0.35 Q13643 EBI-10193895 0.56 P14335 EBI-11422579 0.37 Q99IB8 EBI-11599534 0.35 P05067 EBI-16716791 0.40 GO:0072562 GO:0009986 GO:0062023 GO:0005829 GO:0005783 GO:0070062 GO:0005576 GO:0005615 GO:0031314 GO:0005743 GO:0031965 GO:0005886 GO:0016209 GO:0019855 GO:0046904 GO:0030246 GO:0035374 GO:0098633 GO:0020037 GO:0019862 GO:0016491 GO:0016653 GO:0042803 GO:0004867 GO:0007155 GO:0098869 GO:0034614 GO:1903606 GO:0007565 GO:0042167 GO:0020027 GO:0050777 GO:0046329 GO:0030163 Peripheral UniProt Curator Inference {ECO:0000305|PubMed:23157686} MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIMDRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIFTMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPCMGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVPGDGDEELLRFSN 352