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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)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

  • 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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
ChainiPRO_000001789720 – 202Alpha-1-microglobulinAdd BLAST183
ChainiPRO_0000017898205 – 349Inter-alpha-trypsin inhibitor light chainAdd BLAST145
ChainiPRO_0000017899283 – 343TrypstatinAdd BLAST61

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi90 ↔ 187PROSITE-ProRule annotation
Glycosylationi114N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi230 ↔ 280PROSITE-ProRule annotation
Glycosylationi233N-linked (GlcNAc...)Sequence 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.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.
PhosphoSitePlusiQ64240.

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

BgeeiENSRNOG00000006889.
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.
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
Contains 2 BPTI/Kunitz inhibitor domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG4295. Eukaryota.
ENOG410XQNP. LUCA.
GeneTreeiENSGT00740000114929.
HOGENOMiHOG000001572.
HOVERGENiHBG000225.
InParanoidiQ64240.
OMAiRHGPTIT.
OrthoDBiEOG091G09P2.
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)DescriptionActionsGraphical viewLength
Sequence conflicti142G → A in AAA41596 (PubMed:2429963).Curated1
Sequence conflicti302W → L AA sequence (PubMed:3263966).Curated1
Sequence conflicti323G → N AA sequence (PubMed:3263966).Curated1
Sequence conflicti330 – 331KE → PK AA sequence (PubMed:3263966).Curated2
Sequence conflicti334E → W AA sequence (PubMed:3263966).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009248.

Protein family/group databases

MEROPSiI02.005.

PTM databases

iPTMnetiQ64240.
PhosphoSitePlusiQ64240.

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.
OrthoDBiEOG091G09P2.
PhylomeDBiQ64240.
TreeFamiTF351222.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ64240.

Gene expression databases

BgeeiENSRNOG00000006889.
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...

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: November 2, 2016
This is version 138 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.