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Protein

Protein AMBP

Gene

Ambp

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. It inhibits blood coagulation factor Xa and tryptase about 100-fold more rapidly than porcine pancreatic trypsin and chymase.

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

GO - Biological processi

  • protein catabolic process Source: RGD
  • protein-chromophore linkage Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Ligandi

Chromophore

Enzyme and pathway databases

ReactomeiR-RNO-2168880. Scavenging of heme from plasma.

Protein family/group databases

MEROPSiI02.005.

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi2102. Ambp.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: Ensembl
  • cell surface Source: RGD
  • extracellular exosome Source: Ensembl
  • extracellular space Source: RGD
  • intracellular membrane-bounded organelle Source: RGD
  • 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_0000017897Add
BLAST
Chaini205 – 349145Inter-alpha-trypsin inhibitor light chainPRO_0000017898Add
BLAST
Chaini283 – 34361TrypstatinPRO_0000017899Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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.1 Publication
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

PaxDbiQ64240.
PRIDEiQ64240.

PTM databases

iPTMnetiQ64240.

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. Trypstatin is present in mast cell granules.

Gene expression databases

GenevisibleiQ64240. RN.

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 (By similarity). Alpha-1-microglobulin interacts with FN1. Trypstatin is a monomer and also occurs as a complex with tryptase in mast cells.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009248.

Structurei

3D structure databases

ProteinModelPortaliQ64240.
SMRiQ64240. Positions 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

eggNOGiKOG4295. Eukaryota.
ENOG410XQNP. LUCA.
GeneTreeiENSGT00740000114929.
HOGENOMiHOG000001572.
HOVERGENiHBG000225.
InParanoidiQ64240.
OMAiRHGPTIT.
OrthoDBiEOG73FQKT.
PhylomeDBiQ64240.
TreeFamiTF351222.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
4.10.410.10. 2 hits.
InterProiIPR002968. A1-microglobln.
IPR029856. AMBP.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002223. Kunitz_BPTI.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view]
PANTHERiPTHR10083:SF18. PTHR10083:SF18. 1 hit.
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.

Q64240-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQGLGALFLL LTACLTLKAD NVPTLPDIQV QENFNEARIY GKWFNLAVGS
60 70 80 90 100
TCPWLRRIKN KMSVSTLVLQ EGATEAEISV TSTQWRKGVC EEISGVYQKT
110 120 130 140 150
DIDGKFLYHK SKWNATLESY VVHTNYDEYA IFLTKKFSHR HGPTITAKLY
160 170 180 190 200
GREPQLRDSL LQEFREVALS VGIPENSIVF MADRGECVPG DREVESTSFA
210 220 230 240 250
RARRAVLPQE NEGSGSEPLI TGTLKKEDSC QLNYSEGPCL GMQQKYYYNG
260 270 280 290 300
ASMACETFQY GGCLGNGNNF ASEKECLQTC RTIAACNLPI VQGPCRAFAE
310 320 330 340
LWAFDAAQGK CIQFIYGGCK GNGNKFYSEK ECKEYCGVPG DGYEELTRS
Length:349
Mass (Da):38,851
Last modified:November 1, 1997 - v1
Checksum:i1B7FB7DCB0824E01
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti142 – 1421G → A in AAA41596 (PubMed:2429963).Curated
Sequence conflicti302 – 3021W → L AA sequence (PubMed:3263966).Curated
Sequence conflicti323 – 3231G → N AA sequence (PubMed:3263966).Curated
Sequence conflicti330 – 3312KE → PK AA sequence (PubMed:3263966).Curated
Sequence conflicti334 – 3341E → W AA sequence (PubMed:3263966).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S87544 mRNA. Translation: AAB21782.1.
BC088166 mRNA. Translation: AAH88166.1.
J02600 mRNA. Translation: AAA41596.1.
PIRiS21089.
RefSeqiNP_037033.1. NM_012901.1.
UniGeneiRn.18721.

Genome annotation databases

EnsembliENSRNOT00000009248; ENSRNOP00000009248; ENSRNOG00000006889.
GeneIDi25377.
KEGGirno:25377.
UCSCiRGD:2102. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S87544 mRNA. Translation: AAB21782.1.
BC088166 mRNA. Translation: AAH88166.1.
J02600 mRNA. Translation: AAA41596.1.
PIRiS21089.
RefSeqiNP_037033.1. NM_012901.1.
UniGeneiRn.18721.

3D structure databases

ProteinModelPortaliQ64240.
SMRiQ64240. Positions 229-338.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009248.

Protein family/group databases

MEROPSiI02.005.

PTM databases

iPTMnetiQ64240.

Proteomic databases

PaxDbiQ64240.
PRIDEiQ64240.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000009248; ENSRNOP00000009248; ENSRNOG00000006889.
GeneIDi25377.
KEGGirno:25377.
UCSCiRGD:2102. rat.

Organism-specific databases

CTDi259.
RGDi2102. Ambp.

Phylogenomic databases

eggNOGiKOG4295. Eukaryota.
ENOG410XQNP. LUCA.
GeneTreeiENSGT00740000114929.
HOGENOMiHOG000001572.
HOVERGENiHBG000225.
InParanoidiQ64240.
OMAiRHGPTIT.
OrthoDBiEOG73FQKT.
PhylomeDBiQ64240.
TreeFamiTF351222.

Enzyme and pathway databases

ReactomeiR-RNO-2168880. Scavenging of heme from plasma.

Miscellaneous databases

PROiQ64240.

Gene expression databases

GenevisibleiQ64240. RN.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
4.10.410.10. 2 hits.
InterProiIPR002968. A1-microglobln.
IPR029856. AMBP.
IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002223. Kunitz_BPTI.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR020901. Prtase_inh_Kunz-CS.
[Graphical view]
PANTHERiPTHR10083:SF18. PTHR10083:SF18. 1 hit.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rat alpha 1-microglobulin: co-expression in liver with the light chain of inter-alpha-trypsin inhibitor."
    Lindqvist A., Bratt T., Altieri M., Kastern W., Aakerstroem B.
    Biochim. Biophys. Acta 1130:63-67(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "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].
    Tissue: Spleen.
  3. "Developmental and tissue-specific expression of alpha 1-microglobulin mRNA in the rat."
    Kastern W., Bjoerck L., Aakerstroem B.
    J. Biol. Chem. 261:15070-15074(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 141-195.
  4. "Kunitz-type protease inhibitor found in rat mast cells. Purification, properties, and amino acid sequence."
    Kido H., Yokogoshi Y., Katunuma N.
    J. Biol. Chem. 263:18104-18107(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 283-343, CHARACTERIZATION.
    Strain: Wistar.
  5. "Isolation and characterization of fibronectin-alpha 1-microglobulin complex in rat plasma."
    Falkenberg C., Enghild J.J., Thoegersen I.B., Salvesen G., Aakerstroem B.
    Biochem. J. 301:745-751(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FN1.
  6. "Mast cell protease inhibitor, trypstatin, is a fragment of inter-alpha-trypsin inhibitor light chain."
    Itoh H., Ide H., Ishikawa N., Nawa Y.
    J. Biol. Chem. 269:3818-3822(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING.

Entry informationi

Entry nameiAMBP_RAT
AccessioniPrimary (citable) accession number: Q64240
Secondary accession number(s): P19603, Q63336
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.