Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q07456

- AMBP_MOUSE

UniProt

Q07456 - AMBP_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Protein AMBP

Gene

Ambp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization (By similarity).By similarity
Trypstatin is a trypsin inhibitor.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei52 – 521Multimeric 3-hydroxykynurenine chromophore (covalent)By similarity
Binding sitei110 – 1101Multimeric 3-hydroxykynurenine chromophore (covalent)By similarity
Binding sitei136 – 1361Multimeric 3-hydroxykynurenine chromophore (covalent)By similarity
Binding sitei148 – 1481Multimeric 3-hydroxykynurenine chromophore (covalent)By similarity
Sitei240 – 2412Inhibitory (P1) (chymotrypsin, elastase)By similarity
Sitei296 – 2972Inhibitory (P1) (trypsin)By similarity

GO - Molecular functioni

  1. heme binding Source: UniProtKB
  2. IgA binding Source: UniProtKB
  3. protein homodimerization activity Source: UniProtKB
  4. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW
  5. small molecule binding Source: InterPro

GO - Biological processi

  1. protein catabolic process Source: Ensembl
  2. protein-chromophore linkage Source: UniProtKB-KW
  3. protein maturation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Ligandi

Chromophore

Enzyme and pathway databases

ReactomeiREACT_196575. Scavenging of heme from plasma.

Protein family/group databases

MEROPSiI02.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein AMBP
Cleaved into the following 3 chains:
Alternative name(s):
Bikunin
HI-30
Gene namesi
Name:Ambp
Synonyms:Itil
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:88002. Ambp.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: Ensembl
  2. cell surface Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. intracellular membrane-bounded organelle Source: Ensembl
  5. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 202183Alpha-1-microglobulinPRO_0000017893Add
BLAST
Chaini205 – 349145Inter-alpha-trypsin inhibitor light chainPRO_0000017894Add
BLAST
Chaini283 – 34361TrypstatinBy similarityPRO_0000318928Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi33 – 331N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi90 ↔ 187PROSITE-ProRule annotation
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi230 ↔ 280PROSITE-ProRule annotation
Glycosylationi233 – 2331N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi239 ↔ 263PROSITE-ProRule annotation
Disulfide bondi255 ↔ 276PROSITE-ProRule annotation
Disulfide bondi286 ↔ 336PROSITE-ProRule annotation
Disulfide bondi295 ↔ 319PROSITE-ProRule annotation
Disulfide bondi311 ↔ 332PROSITE-ProRule annotation

Post-translational modificationi

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

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ07456.
PaxDbiQ07456.
PRIDEiQ07456.

PTM databases

PhosphoSiteiQ07456.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiQ07456.
CleanExiMM_AMBP.
ExpressionAtlasiQ07456. baseline and differential.
GenevestigatoriQ07456.

Interactioni

Subunit structurei

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).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ07456.
SMRiQ07456. Positions 27-192, 229-338.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini230 – 28051BPTI/Kunitz inhibitor 1PROSITE-ProRule annotationAdd
BLAST
Domaini286 – 33651BPTI/Kunitz inhibitor 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the calycin superfamily. Lipocalin family.Curated
Contains 2 BPTI/Kunitz inhibitor domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG328322.
GeneTreeiENSGT00740000114929.
HOGENOMiHOG000001572.
HOVERGENiHBG000225.
InParanoidiQ07456.
OMAiGTSMACE.
OrthoDBiEOG73FQKT.
PhylomeDBiQ07456.
TreeFamiTF351222.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
4.10.410.10. 2 hits.
InterProiIPR002968. 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]
PfamiPF00014. Kunitz_BPTI. 2 hits.
PF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR01215. A1MCGLOBULIN.
PR00759. BASICPTASE.
PR00179. LIPOCALIN.
SMARTiSM00131. KU. 2 hits.
[Graphical view]
SUPFAMiSSF50814. SSF50814. 1 hit.
SSF57362. SSF57362. 2 hits.
PROSITEiPS00280. BPTI_KUNITZ_1. 2 hits.
PS50279. BPTI_KUNITZ_2. 2 hits.
PS00213. LIPOCALIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q07456-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQGLRTLFLL LTACLASRAD PASTLPDIQV QENFSESRIY GKWYNLAVGS
60 70 80 90 100
TCPWLSRIKD KMSVSTLVLQ EGATETEISM TSTRWRRGVC EEITGAYQKT
110 120 130 140 150
DIDGKFLYHK SKWNITLESY VVHTNYDEYA IFLTKKSSHH HGLTITAKLY
160 170 180 190 200
GREPQLRDSL LQEFKDVALN VGISENSIIF MPDRGECVPG DREVEPTSIA
210 220 230 240 250
RARRAVLPQE SEGSGTEPLI TGTLKKEDSC QLNYSEGPCL GMQERYYYNG
260 270 280 290 300
ASMACETFQY GGCLGNGNNF ISEKDCLQTC RTIAACNLPI VQGPCRAFIK
310 320 330 340
LWAFDAAQGK CIQFHYGGCK GNGNKFYSEK ECKEYCGVPG DGYEELIRS
Length:349
Mass (Da):39,029
Last modified:February 26, 2008 - v2
Checksum:iCFB9208D37DF0021
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651S → Q in CAA48640. (PubMed:7689339)Curated
Sequence conflicti185 – 1851G → E in BAB23659. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS18248.1.
PIRiS35708.
RefSeqiNP_031469.1. NM_007443.3.
UniGeneiMm.2197.

Genome annotation databases

EnsembliENSMUST00000030041; ENSMUSP00000030041; ENSMUSG00000028356.
GeneIDi11699.
KEGGimmu:11699.
UCSCiuc008tfp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS18248.1.
PIRi S35708.
RefSeqi NP_031469.1. NM_007443.3.
UniGenei Mm.2197.

3D structure databases

ProteinModelPortali Q07456.
SMRi Q07456. Positions 27-192, 229-338.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi I02.006.

PTM databases

PhosphoSitei Q07456.

Proteomic databases

MaxQBi Q07456.
PaxDbi Q07456.
PRIDEi Q07456.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030041 ; ENSMUSP00000030041 ; ENSMUSG00000028356 .
GeneIDi 11699.
KEGGi mmu:11699.
UCSCi uc008tfp.1. mouse.

Organism-specific databases

CTDi 259.
MGIi MGI:88002. Ambp.

Phylogenomic databases

eggNOGi NOG328322.
GeneTreei ENSGT00740000114929.
HOGENOMi HOG000001572.
HOVERGENi HBG000225.
InParanoidi Q07456.
OMAi GTSMACE.
OrthoDBi EOG73FQKT.
PhylomeDBi Q07456.
TreeFami TF351222.

Enzyme and pathway databases

Reactomei REACT_196575. Scavenging of heme from plasma.

Miscellaneous databases

NextBioi 279367.
PROi Q07456.
SOURCEi Search...

Gene expression databases

Bgeei Q07456.
CleanExi MM_AMBP.
ExpressionAtlasi Q07456. baseline and differential.
Genevestigatori Q07456.

Family and domain databases

Gene3Di 2.40.128.20. 1 hit.
4.10.410.10. 2 hits.
InterProi IPR002968. 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 ]
Pfami PF00014. Kunitz_BPTI. 2 hits.
PF00061. Lipocalin. 1 hit.
[Graphical view ]
PRINTSi PR01215. A1MCGLOBULIN.
PR00759. BASICPTASE.
PR00179. LIPOCALIN.
SMARTi SM00131. KU. 2 hits.
[Graphical view ]
SUPFAMi SSF50814. SSF50814. 1 hit.
SSF57362. SSF57362. 2 hits.
PROSITEi PS00280. BPTI_KUNITZ_1. 2 hits.
PS50279. BPTI_KUNITZ_2. 2 hits.
PS00213. LIPOCALIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiAMBP_MOUSE
AccessioniPrimary (citable) accession number: Q07456
Secondary accession number(s): Q61294, Q925W1, Q9DBJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 26, 2008
Last modified: October 29, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3