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Q07456 (AMBP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein AMBP

Cleaved into the following 3 chains:

  1. Alpha-1-microglobulin
  2. Inter-alpha-trypsin inhibitor light chain
    Short name=ITI-LC
    Alternative name(s):
    Bikunin
    HI-30
  3. Trypstatin
Gene names
Name:Ambp
Synonyms:Itil
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length349 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization By similarity.

Trypstatin is a trypsin inhibitor By similarity.

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.

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-52, Lys-110, Lys-136, and Lys-148 to form heterogeneous polycyclic chromophores including hydroxanthommatin. The reaction by alpha-1-microglobulin is autocatalytic. 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 By similarity.

Heavy chains are interlinked with bikunin via a chondroitin 4-sulfate bridge to the their C-terminal aspartate By similarity.

Sequence similarities

In the N-terminal section; belongs to the calycin superfamily. Lipocalin family.

Contains 2 BPTI/Kunitz inhibitor domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 202183Alpha-1-microglobulin
PRO_0000017893
Chain205 – 349145Inter-alpha-trypsin inhibitor light chain
PRO_0000017894
Chain283 – 34361Trypstatin By similarity
PRO_0000318928

Regions

Domain230 – 28051BPTI/Kunitz inhibitor 1
Domain286 – 33651BPTI/Kunitz inhibitor 2

Sites

Binding site521Multimeric 3-hydroxykynurenine chromophore (covalent) By similarity
Binding site1101Multimeric 3-hydroxykynurenine chromophore (covalent) By similarity
Binding site1361Multimeric 3-hydroxykynurenine chromophore (covalent) By similarity
Binding site1481Multimeric 3-hydroxykynurenine chromophore (covalent) By similarity
Site240 – 2412Inhibitory (P1) (chymotrypsin, elastase) By similarity
Site296 – 2972Inhibitory (P1) (trypsin) By similarity

Amino acid modifications

Glycosylation331N-linked (GlcNAc...) Potential
Glycosylation1141N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Disulfide bond90 ↔ 187 By similarity
Disulfide bond230 ↔ 280 By similarity
Disulfide bond239 ↔ 263 By similarity
Disulfide bond255 ↔ 276 By similarity
Disulfide bond286 ↔ 336 By similarity
Disulfide bond295 ↔ 319 By similarity
Disulfide bond311 ↔ 332 By similarity

Experimental info

Sequence conflict651S → Q in CAA48640. Ref.1
Sequence conflict1851G → E in BAB23659. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q07456 [UniParc].

Last modified February 26, 2008. Version 2.
Checksum: CFB9208D37DF0021

FASTA34939,029
        10         20         30         40         50         60 
MQGLRTLFLL LTACLASRAD PASTLPDIQV QENFSESRIY GKWYNLAVGS TCPWLSRIKD 

        70         80         90        100        110        120 
KMSVSTLVLQ EGATETEISM TSTRWRRGVC EEITGAYQKT DIDGKFLYHK SKWNITLESY 

       130        140        150        160        170        180 
VVHTNYDEYA IFLTKKSSHH HGLTITAKLY GREPQLRDSL LQEFKDVALN VGISENSIIF 

       190        200        210        220        230        240 
MPDRGECVPG DREVEPTSIA RARRAVLPQE SEGSGTEPLI TGTLKKEDSC QLNYSEGPCL 

       250        260        270        280        290        300 
GMQERYYYNG ASMACETFQY GGCLGNGNNF ISEKDCLQTC RTIAACNLPI VQGPCRAFIK 

       310        320        330        340 
LWAFDAAQGK CIQFHYGGCK GNGNKFYSEK ECKEYCGVPG DGYEELIRS 

« Hide

References

« Hide 'large scale' references
[1]"Mouse alpha-1-microglobulin/bikunin precursor: cDNA analysis, gene evolution and physical assignment of the gene next to the orosomucoid locus."
Chan P., Salier J.-P.
Biochim. Biophys. Acta 1174:195-200(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[2]"cDNA sequencing of mouse alpha 1-microglobulin/inter-alpha-trypsin inhibitor light chain and its expression in acute inflammation."
Itoh H., Ide H., Kataoka H., Tomita M., Yoshihara H., Nawa Y.
J. Biochem. 116:767-772(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Liver.
[3]"The alpha1-microglobulin/bikunin gene: characterization in mouse and evolution."
Lindqvist A., Rouet P., Salier J.-P., Aakerstroem B.
Gene 234:329-336(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Salivary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X68680 mRNA. Translation: CAA48640.1.
D28812 mRNA. Translation: BAA05973.1.
AF034692 Genomic DNA. Translation: AAD01995.1.
AK004907 mRNA. Translation: BAB23659.1.
BC021660 mRNA. Translation: AAH21660.1.
PIRS35708.
RefSeqNP_031469.1. NM_007443.3.
UniGeneMm.2197.

3D structure databases

ProteinModelPortalQ07456.
SMRQ07456. Positions 27-192, 229-338.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSI02.006.

PTM databases

PhosphoSiteQ07456.

Proteomic databases

PaxDbQ07456.
PRIDEQ07456.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030041; ENSMUSP00000030041; ENSMUSG00000028356.
GeneID11699.
KEGGmmu:11699.
UCSCuc008tfp.1. mouse.

Organism-specific databases

CTD259.
MGIMGI:88002. Ambp.

Phylogenomic databases

eggNOGNOG328322.
GeneTreeENSGT00740000114929.
HOGENOMHOG000001572.
HOVERGENHBG000225.
InParanoidQ07456.
OMAGSTCPWL.
OrthoDBEOG73FQKT.
PhylomeDBQ07456.
TreeFamTF351222.

Gene expression databases

ArrayExpressQ07456.
BgeeQ07456.
CleanExMM_AMBP.
GenevestigatorQ07456.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
4.10.410.10. 2 hits.
InterProIPR002968. A1-microglobln.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002223. Prot_inh_Kunz-m.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view]
PfamPF00014. Kunitz_BPTI. 2 hits.
PF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR01215. A1MCGLOBULIN.
PR00759. BASICPTASE.
PR00179. LIPOCALIN.
SMARTSM00131. KU. 2 hits.
[Graphical view]
SUPFAMSSF50814. SSF50814. 1 hit.
SSF57362. SSF57362. 2 hits.
PROSITEPS00280. BPTI_KUNITZ_1. 2 hits.
PS50279. BPTI_KUNITZ_2. 2 hits.
PS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279367.
PROQ07456.
SOURCESearch...

Entry information

Entry nameAMBP_MOUSE
AccessionPrimary (citable) accession number: Q07456
Secondary accession number(s): Q61294, Q925W1, Q9DBJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 26, 2008
Last modified: April 16, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot