Protein AMBP

Details

Name
Protein AMBP
Synonyms
  • HCP
  • ITIL
Gene Name
AMBP
Organism
Humans
Amino acid sequence
>lcl|BSEQ0010654|Protein AMBP
MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIM
DRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMES
YVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIF
TMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPC
MGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFI
QLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVPGDGDEELLRFSN
Number of residues
352
Molecular Weight
38999.215
Theoretical pI
6.15
GO Classification
Functions
calcium channel inhibitor activity / calcium oxalate binding / heme binding / IgA binding / protein homodimerization activity / serine-type endopeptidase inhibitor activity / small molecule binding
Processes
cell adhesion / female pregnancy / heme catabolic process / negative regulation of endopeptidase activity / negative regulation of immune response / negative regulation of JNK cascade / protein catabolic process / protein-chromophore linkage / receptor-mediated endocytosis / viral process
Components
blood microparticle / cell surface / extracellular exosome / extracellular region / extracellular space / intracellular membrane-bounded organelle / plasma membrane
General Function
Small molecule binding
Specific Function
Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization.Trypstatin is a trypsin inhibitor.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0010655|Protein AMBP (AMBP)
ATGAGGAGCCTCGGGGCCCTGCTCTTGCTGCTGAGCGCCTGCCTGGCGGTGAGCGCTGGC
CCTGTGCCAACGCCGCCCGACAACATCCAAGTGCAGGAAAACTTCAATATCTCTCGGATC
TATGGGAAGTGGTACAACCTGGCCATCGGTTCCACCTGCCCCTGGCTGAAGAAGATCATG
GACAGGATGACAGTGAGCACGCTGGTGCTGGGAGAGGGCGCTACAGAGGCGGAGATCAGC
ATGACCAGCACTCGTTGGCGGAAAGGTGTCTGTGAGGAGACGTCTGGAGCTTATGAGAAA
ACAGATACTGATGGGAAGTTTCTCTATCACAAATCCAAATGGAACATAACCATGGAGTCC
TATGTGGTCCACACCAACTATGATGAGTATGCCATTTTCCTGACCAAGAAATTCAGCCGC
CATCATGGACCCACCATTACTGCCAAGCTCTACGGGCGGGCGCCGCAGCTGAGGGAAACT
CTCCTGCAGGACTTCAGAGTGGTTGCCCAGGGTGTGGGCATCCCTGAGGACTCCATCTTC
ACCATGGCTGACCGAGGTGAATGTGTCCCTGGGGAGCAGGAACCAGAGCCCATCTTAATC
CCGAGAGTCCGGAGGGCTGTGCTACCCCAAGAAGAGGAAGGATCAGGGGGTGGGCAACTG
GTAACTGAAGTCACCAAGAAAGAAGATTCCTGCCAGCTGGGCTACTCGGCCGGTCCCTGC
ATGGGAATGACCAGCAGGTATTTCTATAATGGTACATCCATGGCCTGTGAGACTTTCCAG
TACGGCGGCTGCATGGGCAACGGTAACAACTTCGTCACAGAAAAGGAGTGTCTGCAGACC
TGCCGAACTGTGGCGGCCTGCAATCTCCCCATAGTCCGGGGCCCCTGCCGAGCCTTCATC
CAGCTCTGGGCATTTGATGCTGTCAAGGGGAAGTGCGTCCTCTTCCCCTACGGGGGCTGC
CAGGGCAACGGGAACAAGTTCTACTCAGAGAAGGAGTGCAGAGAGTACTGCGGTGTCCCT
GGTGATGGTGATGAGGAGCTGCTGCGCTTCTCCAACTGA
Chromosome Location
9
Locus
9q32-q33
External Identifiers
ResourceLink
UniProtKB IDP02760
UniProtKB Entry NameAMBP_HUMAN
GenBank Protein ID825614
GenBank Gene IDX54816
GenAtlas IDAMBP
HGNC IDHGNC:453
General References
  1. Traboni C, Cortese R: Sequence of a full length cDNA coding for human protein HC (alpha 1 microglobulin). Nucleic Acids Res. 1986 Aug 11;14(15):6340. [Article]
  2. Kaumeyer JF, Polazzi JO, Kotick MP: The mRNA for a proteinase inhibitor related to the HI-30 domain of inter-alpha-trypsin inhibitor also encodes alpha-1-microglobulin (protein HC). Nucleic Acids Res. 1986 Oct 24;14(20):7839-50. [Article]
  3. Vetr H, Gebhard W: Structure of the human alpha 1-microglobulin-bikunin gene. Biol Chem Hoppe Seyler. 1990 Dec;371(12):1185-96. [Article]
  4. Diarra-Mehrpour M, Bourguignon J, Sesboue R, Salier JP, Leveillard T, Martin JP: Structural analysis of the human inter-alpha-trypsin inhibitor light-chain gene. Eur J Biochem. 1990 Jul 20;191(1):131-9. [Article]
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  8. Lopez Otin C, Grubb AO, Mendez E: The complete amino acid sequence of human complex-forming glycoprotein heterogeneous in charge (protein HC) from one individual. Arch Biochem Biophys. 1984 Feb 1;228(2):544-54. [Article]
  9. Takagi T, Takagi K, Kawai T: Complete amino acid sequence of human alpha 1-microglobulin. Biochem Biophys Res Commun. 1981 Feb 27;98(4):997-1001. [Article]
  10. Calero M, Escribano J, Grubb A, Mendez E: Location of a novel type of interpolypeptide chain linkage in the human protein HC-IgA complex (HC-IgA) and identification of a heterogeneous chromophore associated with the complex. J Biol Chem. 1994 Jan 7;269(1):384-9. [Article]
  11. Reisinger P, Hochstrasser K, Albrecht GJ, Lempart K, Salier JP: Human inter-alpha-trypsin inhibitor: localization of the Kunitz-type domains in the N-terminal part of the molecule and their release by a trypsin-like proteinase. Biol Chem Hoppe Seyler. 1985 May;366(5):479-83. [Article]
  12. Chawla RK, Lawson DH, Ahmad M, Travis J: Cancer-related urinary proteinase inhibitor, EDC1: a new method for its isolation and evidence for multiple forms. J Cell Biochem. 1992 Nov;50(3):227-36. [Article]
  13. Enghild JJ, Salvesen G, Hefta SA, Thogersen IB, Rutherfurd S, Pizzo SV: Chondroitin 4-sulfate covalently cross-links the chains of the human blood protein pre-alpha-inhibitor. J Biol Chem. 1991 Jan 15;266(2):747-51. [Article]
  14. Enghild JJ, Salvesen G, Thogersen IB, Valnickova Z, Pizzo SV, Hefta SA: Presence of the protein-glycosaminoglycan-protein covalent cross-link in the inter-alpha-inhibitor-related proteinase inhibitor heavy chain 2/bikunin. J Biol Chem. 1993 Apr 25;268(12):8711-6. [Article]
  15. Atmani F, Khan SR: Characterization of uronic-acid-rich inhibitor of calcium oxalate crystallization isolated from rat urine. Urol Res. 1995;23(2):95-101. [Article]
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  18. Morii M, Travis J: The reactive site of human inter-alpha-trypsin inhibitor is in the amino-terminal half of the protein. Biol Chem Hoppe Seyler. 1985 Jan;366(1):19-21. [Article]
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  20. Escribano J, Grubb A, Calero M, Mendez E: The protein HC chromophore is linked to the cysteine residue at position 34 of the polypeptide chain by a reduction-resistant bond and causes the charge heterogeneity of protein HC. J Biol Chem. 1991 Aug 25;266(24):15758-63. [Article]
  21. Berggard T, Cohen A, Persson P, Lindqvist A, Cedervall T, Silow M, Thogersen IB, Jonsson JA, Enghild JJ, Akerstrom B: Alpha1-microglobulin chromophores are located to three lysine residues semiburied in the lipocalin pocket and associated with a novel lipophilic compound. Protein Sci. 1999 Dec;8(12):2611-20. [Article]
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  23. Tyagi S, Surjit M, Roy AK, Jameel S, Lal SK: The ORF3 protein of hepatitis E virus interacts with liver-specific alpha1-microglobulin and its precursor alpha1-microglobulin/bikunin precursor (AMBP) and expedites their export from the hepatocyte. J Biol Chem. 2004 Jul 9;279(28):29308-19. Epub 2004 Mar 22. [Article]
  24. Tyagi S, Surjit M, Lal SK: The 41-amino-acid C-terminal region of the hepatitis E virus ORF3 protein interacts with bikunin, a kunitz-type serine protease inhibitor. J Virol. 2005 Sep;79(18):12081-7. [Article]
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  27. Xu Y, Carr PD, Guss JM, Ollis DL: The crystal structure of bikunin from the inter-alpha-inhibitor complex: a serine protease inhibitor with two Kunitz domains. J Mol Biol. 1998 Mar 13;276(5):955-66. [Article]
  28. Akerstrom B, Logdberg L, Berggard T, Osmark P, Lindqvist A: alpha(1)-Microglobulin: a yellow-brown lipocalin. Biochim Biophys Acta. 2000 Oct 18;1482(1-2):172-84. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails