Hmdb loader
Identification
HMDB Protein ID HMDBP01676
Secondary Accession Numbers
  • 7013
Name Protein AMBP
Synonyms
  1. Alpha-1 microglycoprotein
  2. Alpha-1-microglobulin
  3. Bikunin
  4. Complex-forming glycoprotein heterogeneous in charge
  5. EDC1
  6. HI-30
  7. ITI-LC
  8. Inter-alpha-trypsin inhibitor light chain
  9. Protein HC
  10. Trypstatin
  11. Uronic-acid-rich protein
Gene Name AMBP
Protein Type Unknown
Biological Properties
General Function Involved in transporter activity
Specific Function Trypstatin is a trypsin inhibitor
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
peptidase inhibitor activity
endopeptidase inhibitor activity
serine-type endopeptidase inhibitor activity
enzyme regulator activity
enzyme inhibitor activity
transporter activity
Process
establishment of localization
transport
Cellular Location
  1. Secreted
Gene Properties
Chromosome Location Chromosome:9
Locus 9q32-q33
SNPs AMBP
Gene Sequence
>1059 bp
ATGAGGAGCCTCGGGGCCCTGCTCTTGCTGCTGAGCGCCTGCCTGGCGGTGAGCGCTGGC
CCTGTGCCAACGCCGCCCGACAACATCCAAGTGCAGGAAAACTTCAATATCTCTCGGATC
TATGGGAAGTGGTACAACCTGGCCATCGGTTCCACCTGCCCCTGGCTGAAGAAGATCATG
GACAGGATGACAGTGAGCACGCTGGTGCTGGGAGAGGGCGCTACAGAGGCGGAGATCAGC
ATGACCAGCACTCGTTGGCGGAAAGGTGTCTGTGAGGAGACGTCTGGAGCTTATGAGAAA
ACAGATACTGATGGGAAGTTTCTCTATCACAAATCCAAATGGAACATAACCATGGAGTCC
TATGTGGTCCACACCAACTATGATGAGTATGCCATTTTCCTGACCAAGAAATTCAGCCGC
CATCATGGACCCACCATTACTGCCAAGCTCTACGGGCGGGCGCCGCAGCTGAGGGAAACT
CTCCTGCAGGACTTCAGAGTGGTTGCCCAGGGTGTGGGCATCCCTGAGGACTCCATCTTC
ACCATGGCTGACCGAGGTGAATGTGTCCCTGGGGAGCAGGAACCAGAGCCCATCTTAATC
CCGAGAGTCCGGAGGGCTGTGCTACCCCAAGAAGAGGAAGGATCAGGGGGTGGGCAACTG
GTAACTGAAGTCACCAAGAAAGAAGATTCCTGCCAGCTGGGCTACTCGGCCGGTCCCTGC
ATGGGAATGACCAGCAGGTATTTCTATAATGGTACATCCATGGCCTGTGAGACTTTCCAG
TACGGCGGCTGCATGGGCAACGGTAACAACTTCGTCACAGAAAAGGAGTGTCTGCAGACC
TGCCGAACTGTGGCGGCCTGCAATCTCCCCATAGTCCGGGGCCCCTGCCGAGCCTTCATC
CAGCTCTGGGCATTTGATGCTGTCAAGGGGAAGTGCGTCCTCTTCCCCTACGGGGGCTGC
CAGGGCAACGGGAACAAGTTCTACTCAGAGAAGGAGTGCAGAGAGTACTGCGGTGTCCCT
GGTGATGGTGATGAGGAGCTGCTGCGCTTCTCCAACTGA
Protein Properties
Number of Residues 352
Molecular Weight 38999.2
Theoretical pI 6.15
Pfam Domain Function
Signals
  • 1-19
Transmembrane Regions
  • None
Protein Sequence
>Protein AMBP
MRSLGALLLLLSACLAVSAGPVPTPPDNIQVQENFNISRIYGKWYNLAIGSTCPWLKKIM
DRMTVSTLVLGEGATEAEISMTSTRWRKGVCEETSGAYEKTDTDGKFLYHKSKWNITMES
YVVHTNYDEYAIFLTKKFSRHHGPTITAKLYGRAPQLRETLLQDFRVVAQGVGIPEDSIF
TMADRGECVPGEQEPEPILIPRVRRAVLPQEEEGSGGGQLVTEVTKKEDSCQLGYSAGPC
MGMTSRYFYNGTSMACETFQYGGCMGNGNNFVTEKECLQTCRTVAACNLPIVRGPCRAFI
QLWAFDAVKGKCVLFPYGGCQGNGNKFYSEKECREYCGVPGDGDEELLRFSN
GenBank ID Protein 32047
UniProtKB/Swiss-Prot ID P02760
UniProtKB/Swiss-Prot Entry Name AMBP_HUMAN
PDB IDs
GenBank Gene ID X04225
GeneCard ID AMBP
GenAtlas ID AMBP
HGNC ID HGNC:453
References
General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
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  3. Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed:15164053 ]
  4. 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. [PubMed:2428011 ]
  5. 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. [PubMed:2430261 ]
  6. Vetr H, Gebhard W: Structure of the human alpha 1-microglobulin-bikunin gene. Biol Chem Hoppe Seyler. 1990 Dec;371(12):1185-96. [PubMed:1708673 ]
  7. 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. [PubMed:1696200 ]
  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. [PubMed:6198962 ]
  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. [PubMed:6164372 ]
  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. [PubMed:7506257 ]
  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. [PubMed:2408638 ]
  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. [PubMed:1469060 ]
  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. [PubMed:1898736 ]
  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. [PubMed:7682553 ]
  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. [PubMed:7676539 ]
  16. Morelle W, Capon C, Balduyck M, Sautiere P, Kouach M, Michalski C, Fournet B, Mizon J: Chondroitin sulphate covalently cross-links the three polypeptide chains of inter-alpha-trypsin inhibitor. Eur J Biochem. 1994 Apr 15;221(2):881-8. [PubMed:7513643 ]
  17. Hochstrasser K, Schonberger OL, Rossmanith I, Wachter E: Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, V. Attachments of carbohydrates in the human urinary trypsin inhibitor isolated by affinity chromatography. Hoppe Seylers Z Physiol Chem. 1981 Oct;362(10):1357-62. [PubMed:6171497 ]
  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. [PubMed:3890890 ]
  19. Escribano J, Lopex-Otin C, Hjerpe A, Grubb A, Mendez E: Location and characterization of the three carbohydrate prosthetic groups of human protein HC. FEBS Lett. 1990 Jun 18;266(1-2):167-70. [PubMed:1694784 ]
  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. [PubMed:1714898 ]
  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. [PubMed:10631976 ]
  22. Sala A, Campagnoli M, Perani E, Romano A, Labo S, Monzani E, Minchiotti L, Galliano M: Human alpha-1-microglobulin is covalently bound to kynurenine-derived chromophores. J Biol Chem. 2004 Dec 3;279(49):51033-41. Epub 2004 Sep 27. [PubMed:15452109 ]
  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. [PubMed:15037615 ]
  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. [PubMed:16140784 ]
  25. 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. [PubMed:9566199 ]
  26. 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. [PubMed:11058759 ]