Human Gene AMBP (ENST00000265132.8) from GENCODE V44
Description: Homo sapiens alpha-1-microglobulin/bikunin precursor (AMBP), mRNA. (from RefSeq NM_001633) RefSeq Summary (NM_001633): 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]. Gencode Transcript: ENST00000265132.8 Gencode Gene: ENSG00000106927.12 Transcript (Including UTRs) Position: hg38 chr9:114,060,127-114,078,300 Size: 18,174 Total Exon Count: 10 Strand: - Coding Region Position: hg38 chr9:114,060,239-114,078,209 Size: 17,971 Coding Exon Count: 10
ID:AMBP_HUMAN DESCRIPTION: RecName: Full=Protein AMBP; Contains: RecName: Full=Alpha-1-microglobulin; Short=Protein HC; AltName: Full=Alpha-1 microglycoprotein; AltName: Full=Complex-forming glycoprotein heterogeneous in charge; Contains: RecName: Full=Inter-alpha-trypsin inhibitor light chain; Short=ITI-LC; AltName: Full=Bikunin; AltName: Full=EDC1; AltName: Full=HI-30; AltName: Full=Uronic-acid-rich protein; Contains: RecName: Full=Trypstatin; Flags: Precursor; FUNCTION: Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization. FUNCTION: Trypstatin is a trypsin inhibitor (By similarity). SUBUNIT: 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. 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. PTM: The precursor is proteolytically processed into separately functioning proteins. PTM: 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'. PTM: Heavy chains are interlinked with bikunin via a chondroitin 4-sulfate bridge to the their C-terminal aspartate (By similarity). PTM: 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. 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. SIMILARITY: In the N-terminal section; belongs to the calycin superfamily. Lipocalin family. SIMILARITY: Contains 2 BPTI/Kunitz inhibitor domains.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P02760
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
US Server
