AMBP
entrez
259
canonical
uniprot
P02760
canonical
ensembl
ENSG00000106927
resolver
ensp
ENSP00000265132
resolver
ensp
ENSP00000536803
resolver
ensp
ENSP00000536805
resolver
enst
ENST00000265132
resolver
enst
ENST00000866742
resolver
enst
ENST00000866746
resolver
genesymbol
AMBP
resolver
genesymbol_syn
HCP
resolver
genesymbol_syn
ITIL
resolver
hgnc
HGNC:453
resolver
uniprot
P00977
resolver
uniprot
P02759
resolver
uniprot
P78491
resolver
uniprot
Q2TU33
resolver
uniprot
Q5TBD7
resolver
uniprot
Q9UC58
resolver
uniprot
Q9UDI8
resolver
uniprot_entry
AMBP_HUMAN
resolver
uniprot_sec
P00977
resolver
uniprot_sec
P02759
resolver
uniprot_sec
P78491
resolver
uniprot_sec
Q2TU33
resolver
uniprot_sec
Q5TBD7
resolver
uniprot_sec
Q9UC58
resolver
uniprot_sec
Q9UDI8
resolver
activity_regulation
ACTIVITY REGULATION: [Inter-alpha-trypsin inhibitor light chain]: Up-regulated by TNFAIP6. In a transesterification reaction, TNFAIP6 cleaves the ester bond between the heavy chain and the chondroitin sulfate chain in I-alpha-I complex and potentiates the antiprotease function of I-alpha-I complex through release of free bikunin. {ECO:0000269|PubMed:15917224, ECO:0000269|PubMed:16873769}.
uniprot
proteins
amino_acid_sequence
MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIMDRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIFTMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPCMGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFIQLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVPGDGDEELLRFSN
uniprot
proteins
ec_number
1.6.2.-
uniprot
proteins
function
FUNCTION: [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: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). {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}.; FUNCTION: [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:20463016, PubMed:25301953). 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:10480954, PubMed:15917224, PubMed:16873769). 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}.; FUNCTION: [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}.
uniprot
proteins
mass_dalton
38999
uniprot
proteins
mutagenesis
MUTAGEN 53; /note="C->S: Impairs the reductase activity toward cytochrome c independently of the electron donnor. Decreases the reductase activity toward methemoglobin. Decreases the reductase activity toward oxidized collagen."; /evidence="ECO:0000269|PubMed:15683711, ECO:0000269|PubMed:23642167"; MUTAGEN 111; /note="K->T: Impairs the reductase activity toward cytochrome c in the presence of NADPH; when associated with T-137 and T-149. Impairs the reductase activity toward oxidized collagen; when associated with T-137 and T-149."; /evidence="ECO:0000269|PubMed:15683711, ECO:0000269|PubMed:23642167"; MUTAGEN 137; /note="K->T: Impairs the reductase activity toward cytochrome c in the presence of NADPH; when associated with T-111 and T-149. Impairs the reductase activity toward oxidized collagen; when associated with T-111 and T-149."; /evidence="ECO:0000269|PubMed:15683711, ECO:0000269|PubMed:23642167"; MUTAGEN 149; /note="K->T: Impairs the reductase activity toward cytochrome c in the presence of NADPH; when associated with T-111 and T-137. Impairs the reductase activity toward oxidized collagen; when associated with T-111 and T-137."; /evidence="ECO:0000269|PubMed:15683711, ECO:0000269|PubMed:23642167
uniprot
proteins
post_translational_modification
PTM: The precursor is proteolytically processed into separately functioning proteins. {ECO:0000305}.; PTM: [Alpha-1-microglobulin]: Proteolytically cleaved in the presence of oxyhemoglobin or MPO (PubMed:11877257, PubMed:25698971). The cleaved form t-alpha-1-microglobulin lacks the C-terminal tetrapeptide LIPR and is released from IgA-alpha-1-microglobulin complex as well as from free alpha-1-microglobulin when exposed to oxyhemoglobin or erythrocyte membranes. The cleavage of IgA-alpha-1-microglobulin complex is associated with the reduction of the covalent bond between IgA and alpha-1-microglobulin, yielding an intact IgA molecule (PubMed:11877257). The cleavage by MPO is associated with the transfer of heme group from MPO to t-alpha-1-microglobulin (PubMed:25698971). t-alpha-1-microglobulin has higher reductase activity when compared with full length protein (PubMed:15683711). {ECO:0000269|PubMed:11877257, ECO:0000269|PubMed:15683711, ECO:0000269|PubMed:25698971}.; PTM: [Alpha-1-microglobulin]: 3-hydroxykynurenine, an oxidized tryptophan metabolite that is common in biological fluids, reacts with Cys-53, Lys-111, Lys-137, and Lys-149 to form heterogeneous polycyclic chromophores including hydroxanthommatin. The reaction by alpha-1-microglobulin is autocatalytic; the human protein forms chromophore even when expressed in insect and bacterial cells. The chromophore can react with accessible cysteines forming non-reducible thioether cross-links with other molecules of alpha-1-microglobulin or with other proteins such as Ig alpha-1 chain C region 'Cys-352'. {ECO:0000269|PubMed:10631976, ECO:0000269|PubMed:1714898, ECO:0000269|PubMed:7535251}.; PTM: [Inter-alpha-trypsin inhibitor light chain]: Heavy chains are interlinked with bikunin via a chondroitin 4-sulfate bridge to the C-terminal aspartate. {ECO:0000269|PubMed:1898736, ECO:0000269|PubMed:6171497, ECO:0000269|PubMed:7682553}.; PTM: [Inter-alpha-trypsin inhibitor light chain]: Proteolytically cleaved by PRSS3 at Kunitz domain 2. {ECO:0000269|PubMed:25301953}.; PTM: N-glycosylated. N-glycan heterogeneity at Asn-115: Hex5HexNAc4 (major), Hex6HexNAc5 (minor) and dHex1Hex6HexNAc5 (minor). N-glycan at Asn-250: Hex5HexNAc4. {ECO:0000269|PubMed:1694784, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:6171497}.; PTM: O-glycosylated. O-linkage of the glycosaminoglycan, chondroitin sulfate, at Ser-215 allows cross-linking between the three polypeptide chains. {ECO:0000269|PubMed:1694784, ECO:0000269|PubMed:1898736, ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:6171497, ECO:0000269|PubMed:7682553}.
uniprot
proteins
protein_family
Calycin superfamily
uniprot
proteins
protein_family
Lipocalin family
uniprot
proteins
pubmed
10480954
uniprot
proteins
pubmed
10631976
uniprot
proteins
pubmed
11058759
uniprot
proteins
pubmed
11877257
uniprot
proteins
pubmed
1469060
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15037615
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15452109
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15683711
uniprot
proteins
pubmed
15917224
uniprot
proteins
pubmed
16140784
uniprot
proteins
pubmed
16873769
uniprot
proteins
pubmed
1694784
uniprot
proteins
pubmed
1696200
uniprot
proteins
pubmed
1708673
uniprot
proteins
pubmed
1714898
uniprot
proteins
pubmed
1898736
uniprot
proteins
pubmed
20463016
uniprot
proteins
pubmed
21356557
uniprot
proteins
pubmed
22096585
uniprot
proteins
pubmed
22171320
uniprot
proteins
pubmed
22512701
uniprot
proteins
pubmed
23157686
uniprot
proteins
pubmed
23642167
uniprot
proteins
pubmed
2408638
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2428011
uniprot
proteins
pubmed
2430261
uniprot
proteins
pubmed
2476436
uniprot
proteins
pubmed
25301953
uniprot
proteins
pubmed
25326458
uniprot
proteins
pubmed
25698971
uniprot
proteins
pubmed
32092412
uniprot
proteins
pubmed
32337544
uniprot
proteins
pubmed
32823731
uniprot
proteins
pubmed
36213313
uniprot
proteins
pubmed
37453717
uniprot
proteins
pubmed
3890890
uniprot
proteins
pubmed
6164372
uniprot
proteins
pubmed
6171497
uniprot
proteins
pubmed
6198962
uniprot
proteins
pubmed
7506257
uniprot
proteins
pubmed
7513643
uniprot
proteins
pubmed
7535251
uniprot
proteins
pubmed
7676539
uniprot
proteins
pubmed
7682553
uniprot
proteins
pubmed
9183005
uniprot
proteins
pubmed
9566199
uniprot
proteins
sequence_length
352
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Alpha-1-microglobulin]: Secreted {ECO:0000269|PubMed:11877257, ECO:0000269|PubMed:32092412, ECO:0000269|PubMed:37453717}. 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}.; SUBCELLULAR LOCATION: [Inter-alpha-trypsin inhibitor light chain]: Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313}.
uniprot
proteins