CAA38587
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
38,999 Da
NCBI Official Full Name
alpha-1-microglobulin
NCBI Official Synonym Full Names
alpha-1-microglobulin/bikunin precursor
NCBI Official Synonym Symbols
A1M; HCP; ITI; UTI; EDC1; HI30; ITIL; IATIL; ITILC [Similar Products]
NCBI Protein Information
protein AMBP; bikunin; uristatin; protein HC; trypstatin; uronic-acid-rich protein; growth-inhibiting protein 19; inter-alpha-trypsin inhibitor light chain; complex-forming glycoprotein heterogeneous in charge
UniProt Protein Name
Protein AMBP
UniProt Synonym Protein Names
Alpha-1 microglycoprotein; Complex-forming glycoprotein heterogeneous in chargeInter-alpha-trypsin inhibitor light chain; ITI-LC; Alternative name(s):; Bikunin; EDC1; HI-30; Uronic-acid-rich protein
UniProt Synonym Gene Names
UniProt Entry Name
AMBP_HUMAN
NCBI Summary for A1-MG
This gene encodes a complex glycoprotein secreted in plasma. The precursor is proteolytically processed into distinct functioning proteins: alpha-1-microglobulin, which belongs to the superfamily of lipocalin transport proteins and may play a role in the regulation of inflammatory processes, and bikunin, which is a urinary trypsin inhibitor belonging to the superfamily of Kunitz-type protease inhibitors and plays an important role in many physiological and pathological processes. This gene is located on chromosome 9 in a cluster of lipocalin genes. [provided by RefSeq, Jul 2008]
UniProt Comments for A1-MG
Function: Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization. Ref.18Trypstatin is a trypsin inhibitor
By similarity. Ref.18
Subunit structure: I-alpha-I plasma protease inhibitors are assembled from one or two heavy chains (H1, H2 or H3) and one light chain, bikunin. Inter-alpha-inhibitor (I-alpha-I) is composed of H1, H2 and bikunin, inter-alpha-like inhibitor (I-alpha-LI) of H2 and bikunin, and pre-alpha-inhibitor (P-alpha-I) of H3 and bikunin. Alpha-1-microglobulin occurs as a monomer and also in complexes with IgA and albumin. Alpha-1-microglobulin interacts with FN1. Trypstatin is a monomer and also occurs as a complex with tryptase in mast cells
By similarity. Alpha-1-microglobulin and bikunin interact (via SH3 domain) with HEV ORF3 protein. Ref.26 Ref.27
Subcellular location: Secreted.
Tissue specificity: Expressed by the liver and secreted in plasma. Alpha-1-microglobulin occurs in many physiological fluids including plasma, urine, and cerebrospinal fluid. Inter-alpha-trypsin inhibitor is present in plasma and urine.
Post-translational modification: The precursor is proteolytically processed into separately functioning proteins.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'.Heavy chains are interlinked with bikunin via a chondroitin 4-sulfate bridge to the their C-terminal aspartate
By similarity.N- and O-glycosylated. N-glycan heterogeneity at Asn-115: Hex5HexNAc4 (major), Hex6HexNAc5 (minor) and dHex1Hex6HexNAc5 (minor). N-glycan at Asn-250: Hex5HexNAc4. O-linkage of the glycosaminoglycan, chondroitin sulfate, at Ser-215 allows cross-linking between the three polypeptide chains. Ref.16 Ref.17 Ref.20 Ref.22 Ref.28
Miscellaneous: In vitro, the first twelve residues of the amino end of the inhibitor appear to have a reactive site capable of inhibiting the activity of a number of enzymes. Its in vivo function is not known.
Sequence similarities: In the N-terminal section; belongs to the calycin superfamily. Lipocalin family.Contains 2 BPTI/Kunitz inhibitor domains.
Research Articles on A1-MG
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