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Protein

Protein AMBP

Gene

Ambp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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)DescriptionActionsGraphical viewLength
Binding sitei52Multimeric 3-hydroxykynurenine chromophore (covalent)By similarity1
Binding sitei110Multimeric 3-hydroxykynurenine chromophore (covalent)By similarity1
Binding sitei136Multimeric 3-hydroxykynurenine chromophore (covalent)By similarity1
Binding sitei148Multimeric 3-hydroxykynurenine chromophore (covalent)By similarity1
Sitei240 – 241Inhibitory (P1) (chymotrypsin, elastase)By similarity2
Sitei296 – 297Inhibitory (P1) (trypsin)By similarity2

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionProtease inhibitor, Serine protease inhibitor
LigandChromophore

Enzyme and pathway databases

ReactomeiR-MMU-2168880 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:88002 Ambp

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
ChainiPRO_000001789320 – 202Alpha-1-microglobulinAdd BLAST183
ChainiPRO_0000017894205 – 349Inter-alpha-trypsin inhibitor light chainAdd BLAST145
ChainiPRO_0000318928283 – 343TrypstatinBy similarityAdd BLAST61

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi33N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi90 ↔ 187PROSITE-ProRule annotation
Glycosylationi114N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi230 ↔ 280PROSITE-ProRule annotation
Glycosylationi233N-linked (GlcNAc...) asparagineSequence analysis1
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
PeptideAtlasiQ07456
PRIDEiQ07456

PTM databases

GlyConnecti739
iPTMnetiQ07456
PhosphoSitePlusiQ07456

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

BgeeiENSMUSG00000028356
CleanExiMM_AMBP
ExpressionAtlasiQ07456 baseline and differential
GenevisibleiQ07456 MM

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

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000030041

Structurei

3D structure databases

ProteinModelPortaliQ07456
SMRiQ07456
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini230 – 280BPTI/Kunitz inhibitor 1PROSITE-ProRule annotationAdd BLAST51
Domaini286 – 336BPTI/Kunitz inhibitor 2PROSITE-ProRule annotationAdd BLAST51

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG4295 Eukaryota
ENOG410XQNP LUCA
GeneTreeiENSGT00740000114929
HOGENOMiHOG000001572
HOVERGENiHBG000225
InParanoidiQ07456
OMAiRHGPTIT
OrthoDBiEOG091G09P2
PhylomeDBiQ07456
TreeFamiTF351222

Family and domain databases

CDDicd00109 KU, 2 hits
Gene3Di2.40.128.20, 1 hit
4.10.410.10, 2 hits
InterProiView protein in InterPro
IPR002968 A1-microglobln
IPR029856 AMBP
IPR012674 Calycin
IPR002223 Kunitz_BPTI
IPR036880 Kunitz_BPTI_sf
IPR022272 Lipocalin_CS
IPR000566 Lipocln_cytosolic_FA-bd_dom
IPR020901 Prtase_inh_Kunz-CS
PANTHERiPTHR10083:SF18 PTHR10083:SF18, 1 hit
PfamiView protein in Pfam
PF00014 Kunitz_BPTI, 2 hits
PF00061 Lipocalin, 1 hit
PRINTSiPR01215 A1MCGLOBULIN
PR00759 BASICPTASE
SMARTiView protein in SMART
SM00131 KU, 2 hits
SUPFAMiSSF50814 SSF50814, 1 hit
SSF57362 SSF57362, 2 hits
PROSITEiView protein in PROSITE
PS00280 BPTI_KUNITZ_1, 2 hits
PS50279 BPTI_KUNITZ_2, 2 hits
PS00213 LIPOCALIN, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti65S → Q in CAA48640 (PubMed:7689339).Curated1
Sequence conflicti185G → E in BAB23659 (PubMed:16141072).Curated1

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_007443.4
UniGeneiMm.2197

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiAMBP_MOUSE
AccessioniPrimary (citable) accession number: Q07456
Secondary accession number(s): Q61294, Q925W1, Q9DBJ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 26, 2008
Last modified: April 25, 2018
This is version 156 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health