GENTAUR Molecular Products.

 AMBP_HUMAN              Reviewed;         352 AA.
 P02760; P00977; P02759; P78491; Q2TU33; Q5TBD7; Q9UC58; Q9UDI8;
 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
 13-AUG-1987, sequence version 1.
 27-SEP-2017, entry version 204.
 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;
 Name=AMBP; Synonyms=HCP, ITIL;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 PubMed=2428011; DOI=10.1093/nar/14.15.6340;
 Traboni C., Cortese R.;
 "Sequence of a full length cDNA coding for human protein HC (alpha 1
 microglobulin).";
 Nucleic Acids Res. 14:6340-6340(1986).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA].
 TISSUE=Liver;
 PubMed=2430261; DOI=10.1093/nar/14.20.7839;
 Kaumeyer J.F., Polazzi J.O., Kotick M.P.;
 "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. 14:7839-7850(1986).
 [3]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
 PubMed=1708673;
 Vetr H., Gebhard W.;
 "Structure of the human alpha 1-microglobulin-bikunin gene.";
 Biol. Chem. Hoppe-Seyler 371:1185-1196(1990).
 [4]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
 TISSUE=Liver;
 PubMed=1696200; DOI=10.1111/j.1432-1033.1990.tb19102.x;
 Diarra-Mehrpour M., Bourguignon J., Sesboue R., Salier J.-P.,
 Leveillard T., Martin J.-P.;
 "Structural analysis of the human inter-alpha-trypsin inhibitor light-
 chain gene.";
 Eur. J. Biochem. 191:131-139(1990).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 Kim J.W.;
 "Identification of a human cell growth inhibition gene.";
 Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
 [6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 TISSUE=Liver;
 PubMed=14702039; DOI=10.1038/ng1285;
 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 T.-O., 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. 36:40-45(2004).
 [7]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=15164053; DOI=10.1038/nature02465;
 Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
 Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
 Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
 Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
 Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
 Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
 Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
 Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
 Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
 Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
 Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
 Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
 Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
 Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
 Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
 Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
 Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
 Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
 Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
 McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
 Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
 Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
 Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
 Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
 Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
 Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
 Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
 Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
 Rogers J., Dunham I.;
 "DNA sequence and analysis of human chromosome 9.";
 Nature 429:369-374(2004).
 [8]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
 Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
 Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
 Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
 Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
 Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
 Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
 Venter J.C.;
 Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
 [9]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 TISSUE=Liver;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [10]
 PROTEIN SEQUENCE OF 20-202.
 PubMed=6198962; DOI=10.1016/0003-9861(84)90021-3;
 Lopez C., Grubb A.O., Mendez E.;
 "The complete amino acid sequence of human complex-forming
 glycoprotein heterogeneous in charge (protein HC) from one
 individual.";
 Arch. Biochem. Biophys. 228:544-554(1984).
 [11]
 PROTEIN SEQUENCE OF 20-198.
 PubMed=6164372; DOI=10.1016/0006-291X(81)91209-2;
 Takagi T., Takagi K., Kawai T.;
 "Complete amino acid sequence of human alpha 1-microglobulin.";
 Biochem. Biophys. Res. Commun. 98:997-1001(1981).
 [12]
 PROTEIN SEQUENCE OF 20-198.
 Lopez C., Grubb A.O., Mendez E.;
 "Human protein HC displays variability in its carboxyl-terminal amino
 acid sequence.";
 FEBS Lett. 144:349-353(1982).
 [13]
 PROTEIN SEQUENCE OF 44-57, AND BINDING TO CHROMOPHORE.
 PubMed=7506257;
 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. 269:384-389(1994).
 [14]
 PROTEIN SEQUENCE OF 206-350.
 PubMed=2408638;
 Reisinger P., Hochstrasser K., Albrecht G.J., Lempart K.,
 Salier J.-P.;
 "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 366:479-483(1985).
 [15]
 PROTEIN SEQUENCE OF 206-243 AND 275-303.
 TISSUE=Urine;
 PubMed=1469060; DOI=10.1002/jcb.240500303;
 Chawla R.K., Lawson D.H., Ahmad M., Travis J.;
 "Cancer-related urinary proteinase inhibitor, EDC1: a new method for
 its isolation and evidence for multiple forms.";
 J. Cell. Biochem. 50:227-236(1992).
 [16]
 PROTEIN SEQUENCE OF 206-223, GLYCOSYLATION AT SER-215, AND CROSS-LINK
 SITE TO HC3.
 PubMed=1898736;
 Enghild J.J., Salvesen G., Hefta S.A., Thoegersen I.B., Rutherfurd S.,
 Pizzo S.V.;
 "Chondroitin 4-sulfate covalently cross-links the chains of the human
 blood protein pre-alpha-inhibitor.";
 J. Biol. Chem. 266:747-751(1991).
 [17]
 PROTEIN SEQUENCE OF 206-223, GLYCOSYLATION AT SER-215, AND CROSS-LINK
 SITE TO HC2.
 PubMed=7682553;
 Enghild J.J., Salvesen G., Thoegersen I.B., Valnickova Z., Pizzo S.V.,
 Hefta S.A.;
 "Presence of the protein-glycosaminoglycan-protein covalent cross-link
 in the inter-alpha-inhibitor-related proteinase inhibitor heavy chain
 2/bikunin.";
 J. Biol. Chem. 268:8711-8716(1993).
 [18]
 PROTEIN SEQUENCE OF 206-223, AND FUNCTION.
 TISSUE=Urine;
 PubMed=7676539; DOI=10.1007/BF00307939;
 Atmani F., Khan S.R.;
 "Characterization of uronic-acid-rich inhibitor of calcium oxalate
 crystallization isolated from rat urine.";
 Urol. Res. 23:95-101(1995).
 [19]
 PROTEIN SEQUENCE OF 206-219, AND COVALENT LINKAGE WITH CHONDROITIN
 SULFATE.
 TISSUE=Plasma;
 PubMed=7513643; DOI=10.1111/j.1432-1033.1994.tb18803.x;
 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. 221:881-888(1994).
 [20]
 GLYCOSYLATION AT SER-215 AND ASN-250, AND STRUCTURE OF CARBOHYDRATES.
 PubMed=6171497;
 Hochstrasser K., Schoenberger O.L., 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-Seyler's Z. Physiol. Chem. 362:1357-1362(1981).
 [21]
 INHIBITORY SITE.
 PubMed=3890890; DOI=10.1515/bchm3.1985.366.1.19;
 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 366:19-21(1985).
 [22]
 GLYCOSYLATION AT THR-24; ASN-36 AND ASN-115, AND STRUCTURE OF
 CARBOHYDRATES.
 PubMed=1694784; DOI=10.1016/0014-5793(90)81531-R;
 Escribano J., Lopex-Otin C., Hjerpe A., Grubb A.O., Mendez E.;
 "Location and characterization of the three carbohydrate prosthetic
 groups of human protein HC.";
 FEBS Lett. 266:167-170(1990).
 [23]
 BINDING TO CHROMOPHORE.
 TISSUE=Urine;
 PubMed=1714898;
 Escribano J., Grubb A.O., 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. 266:15758-15763(1991).
 [24]
 BINDING TO CHROMOPHORE.
 PubMed=10631976; DOI=10.1110/ps.8.12.2611;
 Berggaard T., Cohen A., Persson P., Lindqvist A., Cedervall T.,
 Silow M., Thoegersen I.B., Joensson J.A., Enghild J.J.,
 Aakerstroem B.;
 "Alpha1-microglobulin chromophores are located to three lysine
 residues semiburied in the lipocalin pocket and associated with a
 novel lipophilic compound.";
 Protein Sci. 8:2611-2620(1999).
 [25]
 CHROMOPHORE CHARACTERIZATION.
 PubMed=15452109; DOI=10.1074/jbc.M408242200;
 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. 279:51033-51041(2004).
 [26]
 INTERACTION OF ALPHA-1-MICROGLOBULIN WITH HEV ORF3 PROTEIN.
 PubMed=15037615; DOI=10.1074/jbc.M402017200;
 Tyagi S., Surjit M., Roy A.K., Jameel S., Lal S.K.;
 "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. 279:29308-29319(2004).
 [27]
 INTERACTION OF BIKUNIN WITH HEV ORF3 PROTEIN.
 PubMed=16140784; DOI=10.1128/JVI.79.18.12081-12087.2005;
 Tyagi S., Surjit M., Lal S.K.;
 "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. 79:12081-12087(2005).
 [28]
 GLYCOSYLATION AT ASN-115 AND ASN-250, STRUCTURE OF CARBOHYDRATES, AND
 IDENTIFICATION BY MASS SPECTROMETRY.
 PubMed=22171320; DOI=10.1074/mcp.M111.013649;
 Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
 "Human urinary glycoproteomics; attachment site specific analysis of
 N-and O-linked glycosylations by CID and ECD.";
 Mol. Cell. Proteomics 0:0-0(2011).
 [29]
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 TISSUE=Liver;
 PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
 Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
 Wang L., Ye M., Zou H.;
 "An enzyme assisted RP-RPLC approach for in-depth analysis of human
 liver phosphoproteome.";
 J. Proteomics 96:253-262(2014).
 [30]
 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 230-339.
 PubMed=9566199; DOI=10.1006/jmbi.1997.1582;
 Xu Y., Carr P.D., Guss J.M., Ollis D.L.;
 "The crystal structure of bikunin from the inter-alpha-inhibitor
 complex: a serine protease inhibitor with two Kunitz domains.";
 J. Mol. Biol. 276:955-966(1998).
 [31]
 REVIEW.
 PubMed=11058759;
 Aakerstroem B., Loegdberg L., Berggaard T., Osmark P., Lindqvist A.;
 "Alpha(1)-microglobulin: a yellow-brown lipocalin.";
 Biochim. Biophys. Acta 1482:172-184(2000).
 -!- FUNCTION: Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin,
     and lysosomal granulocytic elastase. Inhibits calcium oxalate
     crystallization. {ECO:0000269|PubMed:7676539}.
 -!- FUNCTION: Trypstatin is a trypsin inhibitor. {ECO:0000250}.
 -!- 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. {ECO:0000250,
     ECO:0000269|PubMed:15037615, ECO:0000269|PubMed:16140784}.
 -!- INTERACTION:
     P07858:CTSB; NbExp=4; IntAct=EBI-2115136, EBI-715062;
     Q13643:FHL3; NbExp=3; IntAct=EBI-2115136, EBI-741101;
     P69616:ORF3 (xeno); NbExp=4; IntAct=EBI-2115136, EBI-7810260;
 -!- 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. {ECO:0000250}.
 -!- 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.
     {ECO:0000269|PubMed:1694784, ECO:0000269|PubMed:1898736,
     ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:6171497,
     ECO:0000269|PubMed:7682553}.
 -!- 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. {ECO:0000305}.
 -----------------------------------------------------------------------
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 EMBL; X04225; CAA27803.1; -; mRNA.
 EMBL; X04494; CAA28182.1; -; mRNA.
 EMBL; X54816; CAA38585.1; -; Genomic_DNA.
 EMBL; X54817; CAA38585.1; JOINED; Genomic_DNA.
 EMBL; X54818; CAA38585.1; JOINED; Genomic_DNA.
 EMBL; X54817; CAA38586.1; -; Genomic_DNA.
 EMBL; X54818; CAA38587.1; -; Genomic_DNA.
 EMBL; M88249; AAA59196.1; -; Genomic_DNA.
 EMBL; M88165; AAA59196.1; JOINED; Genomic_DNA.
 EMBL; M88243; AAA59196.1; JOINED; Genomic_DNA.
 EMBL; M88244; AAA59196.1; JOINED; Genomic_DNA.
 EMBL; M88246; AAA59196.1; JOINED; Genomic_DNA.
 EMBL; M88247; AAA59196.1; JOINED; Genomic_DNA.
 EMBL; AY544123; AAT11154.1; -; mRNA.
 EMBL; AK290837; BAF83526.1; -; mRNA.
 EMBL; AL137850; CAI15899.1; -; Genomic_DNA.
 EMBL; CH471090; EAW87404.1; -; Genomic_DNA.
 EMBL; BC041593; AAH41593.1; -; mRNA.
 CCDS; CCDS6800.1; -.
 PIR; S13433; HCHU.
 RefSeq; NP_001624.1; NM_001633.3.
 UniGene; Hs.436911; -.
 PDB; 1BIK; X-ray; 2.50 A; A=206-352.
 PDB; 3QKG; X-ray; 2.30 A; A=20-202.
 PDB; 4ES7; X-ray; 2.00 A; A=27-193.
 PDB; 4U30; X-ray; 2.50 A; W/X/Y/Z=283-340.
 PDBsum; 1BIK; -.
 PDBsum; 3QKG; -.
 PDBsum; 4ES7; -.
 PDBsum; 4U30; -.
 ProteinModelPortal; P02760; -.
 SMR; P02760; -.
 BioGrid; 106757; 13.
 IntAct; P02760; 12.
 MINT; MINT-1367019; -.
 STRING; 9606.ENSP00000265132; -.
 DrugBank; DB00062; Human Serum Albumin.
 DrugBank; DB00064; Serum albumin iodonated.
 MEROPS; I02.005; -.
 iPTMnet; P02760; -.
 PhosphoSitePlus; P02760; -.
 UniCarbKB; P02760; -.
 BioMuta; AMBP; -.
 DMDM; 122801; -.
 SWISS-2DPAGE; P02760; -.
 MaxQB; P02760; -.
 PaxDb; P02760; -.
 PeptideAtlas; P02760; -.
 PRIDE; P02760; -.
 DNASU; 259; -.
 Ensembl; ENST00000265132; ENSP00000265132; ENSG00000106927.
 GeneID; 259; -.
 KEGG; hsa:259; -.
 UCSC; uc004bie.5; human.
 CTD; 259; -.
 DisGeNET; 259; -.
 EuPathDB; HostDB:ENSG00000106927.11; -.
 GeneCards; AMBP; -.
 HGNC; HGNC:453; AMBP.
 HPA; CAB069436; -.
 HPA; HPA001497; -.
 MIM; 176870; gene.
 neXtProt; NX_P02760; -.
 OpenTargets; ENSG00000106927; -.
 PharmGKB; PA24759; -.
 eggNOG; KOG4295; Eukaryota.
 eggNOG; ENOG410XQNP; LUCA.
 GeneTree; ENSGT00740000114929; -.
 HOVERGEN; HBG000225; -.
 InParanoid; P02760; -.
 OrthoDB; EOG091G09P2; -.
 PhylomeDB; P02760; -.
 TreeFam; TF351222; -.
 Reactome; R-HSA-2168880; Scavenging of heme from plasma.
 EvolutionaryTrace; P02760; -.
 GeneWiki; Alpha-1-microglobulin/bikunin_precursor; -.
 GenomeRNAi; 259; -.
 PMAP-CutDB; P02760; -.
 PRO; PR:P02760; -.
 Proteomes; UP000005640; Chromosome 9.
 Bgee; ENSG00000106927; -.
 CleanEx; HS_AMBP; -.
 ExpressionAtlas; P02760; baseline and differential.
 Genevisible; P02760; HS.
 GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
 GO; GO:0009986; C:cell surface; IEA:Ensembl.
 GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
 GO; GO:0005576; C:extracellular region; TAS:Reactome.
 GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
 GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO; GO:0019855; F:calcium channel inhibitor activity; NAS:UniProtKB.
 GO; GO:0046904; F:calcium oxalate binding; NAS:UniProtKB.
 GO; GO:0020037; F:heme binding; IDA:UniProtKB.
 GO; GO:0019862; F:IgA binding; IDA:UniProtKB.
 GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
 GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; TAS:UniProtKB.
 GO; GO:0036094; F:small molecule binding; IEA:InterPro.
 GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
 GO; GO:0007565; P:female pregnancy; NAS:UniProtKB.
 GO; GO:0042167; P:heme catabolic process; NAS:UniProtKB.
 GO; GO:0050777; P:negative regulation of immune response; NAS:UniProtKB.
 GO; GO:0046329; P:negative regulation of JNK cascade; TAS:UniProtKB.
 GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
 GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
 GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
 GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
 CDD; cd00109; KU; 2.
 Gene3D; 2.40.128.20; -; 1.
 Gene3D; 4.10.410.10; -; 2.
 InterPro; IPR002968; A1-microglobln.
 InterPro; IPR029856; AMBP.
 InterPro; IPR012674; Calycin.
 InterPro; IPR002223; Kunitz_BPTI.
 InterPro; IPR002345; Lipocalin.
 InterPro; IPR022272; Lipocalin_CS.
 InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
 InterPro; IPR020901; Prtase_inh_Kunz-CS.
 PANTHER; PTHR10083:SF281; PTHR10083:SF281; 1.
 Pfam; PF00014; Kunitz_BPTI; 2.
 Pfam; PF00061; Lipocalin; 1.
 PRINTS; PR01215; A1MCGLOBULIN.
 PRINTS; PR00759; BASICPTASE.
 PRINTS; PR00179; LIPOCALIN.
 SMART; SM00131; KU; 2.
 SUPFAM; SSF50814; SSF50814; 1.
 SUPFAM; SSF57362; SSF57362; 2.
 PROSITE; PS00280; BPTI_KUNITZ_1; 2.
 PROSITE; PS50279; BPTI_KUNITZ_2; 2.
 PROSITE; PS00213; LIPOCALIN; 1.
 1: Evidence at protein level;
 3D-structure; Chromophore; Cleavage on pair of basic residues;
 Complete proteome; Direct protein sequencing; Disulfide bond;
 Glycoprotein; Host-virus interaction; Protease inhibitor;
 Proteoglycan; Reference proteome; Repeat; Secreted;
 Serine protease inhibitor; Signal.
 SIGNAL        1     19       {ECO:0000269|PubMed:6164372,
                              ECO:0000269|PubMed:6198962,
                              ECO:0000269|Ref.12}.
 CHAIN        20    203       Alpha-1-microglobulin.
                              /FTId=PRO_0000017886.
 CHAIN       206    352       Inter-alpha-trypsin inhibitor light
                              chain.
                              /FTId=PRO_0000017887.
 CHAIN       284    344       Trypstatin. {ECO:0000250}.
                              /FTId=PRO_0000318926.
 DOMAIN      231    281       BPTI/Kunitz inhibitor 1.
                              {ECO:0000255|PROSITE-ProRule:PRU00031}.
 DOMAIN      287    337       BPTI/Kunitz inhibitor 2.
                              {ECO:0000255|PROSITE-ProRule:PRU00031}.
 REGION      206    226       Glycopeptide (secretory piece).
 BINDING      53     53       Multimeric 3-hydroxykynurenine
                              chromophore (covalent).
 BINDING     111    111       Multimeric 3-hydroxykynurenine
                              chromophore (covalent).
 BINDING     137    137       Multimeric 3-hydroxykynurenine
                              chromophore (covalent).
 BINDING     149    149       Multimeric 3-hydroxykynurenine
                              chromophore (covalent).
 SITE        241    242       Inhibitory (P1) (chymotrypsin, elastase).
                              {ECO:0000250}.
 SITE        297    298       Inhibitory (P1) (trypsin). {ECO:0000250}.
 CARBOHYD     24     24       O-linked (GalNAc...) threonine.
                              {ECO:0000269|PubMed:1694784}.
                              /FTId=CAR_000172.
 CARBOHYD     36     36       N-linked (GlcNAc...) (complex)
                              asparagine. {ECO:0000269|PubMed:1694784}.
 CARBOHYD    115    115       N-linked (GlcNAc...) (complex)
                              asparagine. {ECO:0000269|PubMed:1694784,
                              ECO:0000269|PubMed:22171320}.
 CARBOHYD    215    215       O-linked (Xyl...) (chondroitin sulfate)
                              serine. {ECO:0000269|PubMed:1898736,
                              ECO:0000269|PubMed:6171497,
                              ECO:0000269|PubMed:7682553}.
 CARBOHYD    250    250       N-linked (GlcNAc...) (complex)
                              asparagine. {ECO:0000269|PubMed:22171320,
                              ECO:0000269|PubMed:6171497}.
 DISULFID     91    188
 DISULFID    231    281
 DISULFID    240    264
 DISULFID    256    277
 DISULFID    287    337
 DISULFID    296    320
 DISULFID    312    333
 CONFLICT     48     57       Missing (in Ref. 11; AA sequence).
                              {ECO:0000305}.
 CONFLICT     57     57       Missing (in Ref. 10; AA sequence and 12;
                              AA sequence). {ECO:0000305}.
 CONFLICT    137    137       Missing (in Ref. 11; AA sequence).
                              {ECO:0000305}.
 CONFLICT    142    142       H -> T (in Ref. 11; AA sequence).
                              {ECO:0000305}.
 CONFLICT    145    145       Missing (in Ref. 11; AA sequence).
                              {ECO:0000305}.
 CONFLICT    194    194       E -> Q (in Ref. 11; AA sequence).
                              {ECO:0000305}.
 CONFLICT    215    215       S -> T (in Ref. 18; AA sequence).
                              {ECO:0000305}.
 CONFLICT    218    218       G -> T (in Ref. 18; AA sequence).
                              {ECO:0000305}.
 CONFLICT    291    292       IV -> VI (in Ref. 14; AA sequence and 15;
                              AA sequence). {ECO:0000305}.
 CONFLICT    295    295       Missing (in Ref. 15; AA sequence).
                              {ECO:0000305}.
 CONFLICT    343    343       G -> E (in Ref. 14; AA sequence).
                              {ECO:0000305}.
 HELIX        37     39       {ECO:0000244|PDB:4ES7}.
 STRAND       42     51       {ECO:0000244|PDB:4ES7}.
 HELIX        54     59       {ECO:0000244|PDB:4ES7}.
 HELIX        60     62       {ECO:0000244|PDB:4ES7}.
 STRAND       66     72       {ECO:0000244|PDB:4ES7}.
 STRAND       78     87       {ECO:0000244|PDB:4ES7}.
 STRAND       90    100       {ECO:0000244|PDB:4ES7}.
 STRAND      106    111       {ECO:0000244|PDB:4ES7}.
 TURN        112    115       {ECO:0000244|PDB:4ES7}.
 STRAND      116    125       {ECO:0000244|PDB:4ES7}.
 STRAND      127    142       {ECO:0000244|PDB:4ES7}.
 STRAND      145    155       {ECO:0000244|PDB:4ES7}.
 HELIX       159    170       {ECO:0000244|PDB:4ES7}.
 TURN        171    173       {ECO:0000244|PDB:4ES7}.
 HELIX       176    178       {ECO:0000244|PDB:4ES7}.
 STRAND      179    181       {ECO:0000244|PDB:4ES7}.
 STRAND      244    250       {ECO:0000244|PDB:1BIK}.
 TURN        251    254       {ECO:0000244|PDB:1BIK}.
 STRAND      255    261       {ECO:0000244|PDB:1BIK}.
 STRAND      263    265       {ECO:0000244|PDB:1BIK}.
 STRAND      271    273       {ECO:0000244|PDB:1BIK}.
 HELIX       274    281       {ECO:0000244|PDB:1BIK}.
 HELIX       284    288       {ECO:0000244|PDB:1BIK}.
 STRAND      300    306       {ECO:0000244|PDB:1BIK}.
 TURN        307    310       {ECO:0000244|PDB:1BIK}.
 STRAND      311    317       {ECO:0000244|PDB:1BIK}.
 STRAND      319    321       {ECO:0000244|PDB:1BIK}.
 STRAND      327    329       {ECO:0000244|PDB:1BIK}.
 HELIX       330    337       {ECO:0000244|PDB:1BIK}.
 SEQUENCE   352 AA;  38999 MW;  BC001780094CBD06 CRC64;
 MRSLGALLLL LSACLAVSAG PVPTPPDNIQ VQENFNISRI YGKWYNLAIG STCPWLKKIM
 DRMTVSTLVL GEGATEAEIS MTSTRWRKGV CEETSGAYEK TDTDGKFLYH KSKWNITMES
 YVVHTNYDEY AIFLTKKFSR HHGPTITAKL YGRAPQLRET LLQDFRVVAQ GVGIPEDSIF
 TMADRGECVP GEQEPEPILI PRVRRAVLPQ EEEGSGGGQL VTEVTKKEDS CQLGYSAGPC
 MGMTSRYFYN GTSMACETFQ YGGCMGNGNN FVTEKECLQT CRTVAACNLP IVRGPCRAFI
 QLWAFDAVKG KCVLFPYGGC QGNGNKFYSE KECREYCGVP GDGDEELLRF SN

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