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Protein

Protein AMBP

Gene

AMBP

Organism
Bos taurus (Bovine)
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.
Trypstatin is a trypsin inhibitor.By similarity
May diffuse into follicular fluid after an ovulatory stimulus to act as a structural linker that ensures normal cumulus expansion, through stabilization of the cumulus extracellular matrix, thus supporting the process of ovulation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531Multimeric 3-hydroxykynurenine chromophore (covalent)By similarity
Binding sitei111 – 1111Multimeric 3-hydroxykynurenine chromophore (covalent)By similarity
Binding sitei137 – 1371Multimeric 3-hydroxykynurenine chromophore (covalent)By similarity
Binding sitei149 – 1491Multimeric 3-hydroxykynurenine chromophore (covalent)By similarity
Sitei241 – 2422Inhibitory (P1) (chymotrypsin, elastase)
Sitei297 – 2982Inhibitory (P1) (trypsin)

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Serine protease inhibitor

Keywords - Ligandi

Chromophore

Protein family/group databases

MEROPSiI02.006.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein AMBP
Cleaved into the following 3 chains:
Alternative name(s):
BI-14
Bikunin
Cumulus extracellular matrix-stabilizing factor
Short name:
ESF
HI-30
Gene namesi
Name:AMBP
Synonyms:ITIL
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 203184Alpha-1-microglobulinPRO_0000017884Add
BLAST
Chaini206 – 352147Inter-alpha-trypsin inhibitor light chainPRO_0000017885Add
BLAST
Chaini284 – 34461TrypstatinBy similarityPRO_0000318925Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi91 ↔ 188PROSITE-ProRule annotation
Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence analysis
Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence analysis
Disulfide bondi231 ↔ 281PROSITE-ProRule annotation
Disulfide bondi240 ↔ 264PROSITE-ProRule annotation
Glycosylationi250 – 2501N-linked (GlcNAc...)1 Publication
Disulfide bondi256 ↔ 277PROSITE-ProRule annotation
Disulfide bondi287 ↔ 337PROSITE-ProRule annotation
Disulfide bondi296 ↔ 320PROSITE-ProRule annotation
Disulfide bondi312 ↔ 333PROSITE-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-53, Lys-111, Lys-137, and Lys-149 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

PaxDbiP00978.
PRIDEiP00978.

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.

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

STRINGi9913.ENSBTAP00000020817.

Structurei

3D structure databases

ProteinModelPortaliP00978.
SMRiP00978. Positions 230-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini231 – 28151BPTI/Kunitz inhibitor 1PROSITE-ProRule annotationAdd
BLAST
Domaini287 – 33751BPTI/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.
HOGENOMiHOG000001572.
HOVERGENiHBG000225.
InParanoidiP00978.

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.

P00978-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSLSGLLLL LTACLAVNAS SVPTLPDDIQ VQENFDLSRI YGKWFNVAVG
60 70 80 90 100
STCPWLKRFK EKMTMSTVVL IAGPTSKEIS VTNTHRRKGV CESISGTYEK
110 120 130 140 150
TSADGKFLYH KAKWNITMES YVVHTNYDEY AIFLTKKLSR RHGPTITVKL
160 170 180 190 200
YGREPQLRES LLEEFREVAL GVGIPEDAIF TMPDRGECVP GEQDPVPTPL
210 220 230 240 250
SRARRAVLTQ EEEGSGAGQP VTNFSKKADS CQLDYSQGPC LGLFKRYFYN
260 270 280 290 300
GTSMACETFL YGGCMGNGNN FLSEKECLQT CRTVEACNLP IVQGPCRSYI
310 320 330 340 350
QLWAFDAVKG KCVRFSYGGC KGNGNKFYSE KECKEYCGIP GEADEELLRF

SN
Length:352
Mass (Da):39,235
Last modified:November 1, 1997 - v2
Checksum:iED31C5CA02E70B19
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711I → K in AAI02638 (Ref. 2) Curated
Sequence conflicti103 – 1031A → T in AAI02638 (Ref. 2) Curated
Sequence conflicti200 – 2001L → V in AAI02638 (Ref. 2) Curated
Sequence conflicti209 – 2091T → G AA sequence (PubMed:1376324).Curated
Sequence conflicti217 – 2171A → D AA sequence (PubMed:1376324).Curated
Sequence conflicti268 – 2681G → L AA sequence (PubMed:2408637).Curated
Sequence conflicti268 – 2681G → L AA sequence (PubMed:6199275).Curated
Sequence conflicti274 – 2741E → Q AA sequence (PubMed:2408637).Curated
Sequence conflicti274 – 2741E → Q AA sequence (PubMed:6199275).Curated
Sequence conflicti298 – 2992SY → AF AA sequence (PubMed:2408637).Curated
Sequence conflicti298 – 2992SY → AF AA sequence (PubMed:6199275).Curated
Sequence conflicti305 – 3051F → I in AAI02638 (Ref. 2) Curated
Sequence conflicti330 – 3301E → Q AA sequence (PubMed:2408637).Curated
Sequence conflicti330 – 3301E → Q AA sequence (PubMed:6199275).Curated
Sequence conflicti346 – 3461E → R AA sequence (PubMed:2408637).Curated
Sequence conflicti346 – 3461E → R AA sequence (PubMed:6199275).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35642 mRNA. Translation: AAB07599.1.
BC102637 mRNA. Translation: AAI02638.1.
PIRiS68149. TIBOBI.
RefSeqiNP_776414.1. NM_173989.3.
UniGeneiBt.39060.

Genome annotation databases

GeneIDi280996.
KEGGibta:280996.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35642 mRNA. Translation: AAB07599.1.
BC102637 mRNA. Translation: AAI02638.1.
PIRiS68149. TIBOBI.
RefSeqiNP_776414.1. NM_173989.3.
UniGeneiBt.39060.

3D structure databases

ProteinModelPortaliP00978.
SMRiP00978. Positions 230-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000020817.

Protein family/group databases

MEROPSiI02.006.

Proteomic databases

PaxDbiP00978.
PRIDEiP00978.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi280996.
KEGGibta:280996.

Organism-specific databases

CTDi259.

Phylogenomic databases

eggNOGiKOG4295. Eukaryota.
ENOG410XQNP. LUCA.
HOGENOMiHOG000001572.
HOVERGENiHBG000225.
InParanoidiP00978.

Miscellaneous databases

NextBioi20805096.

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. "Bovine alpha 1-microglobulin/bikunin. Isolation and characterization of liver cDNA and urinary alpha 1-microglobulin."
    Lindqvist A., Aakerstroem B.
    Biochim. Biophys. Acta 1306:98-106(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Testis.
  3. "Identification of a factor in fetal bovine serum that stabilizes the cumulus extracellular matrix. A role for a member of the inter-alpha-trypsin inhibitor family."
    Chen L., Mao S.J.T., Larsen W.J.
    J. Biol. Chem. 267:12380-12386(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 206-219.
    Tissue: Fetal serum.
  4. "Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, X. The amino-acid sequences of the trypsin-released inhibitors from horse and pig inter-alpha-trypsin inhibitors."
    Hochstrasser K., Wachter E., Albrecht G.J., Reisinger P.
    Biol. Chem. Hoppe-Seyler 366:473-478(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 227-349.
  5. "Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, VII. Determination of the amino-acid sequence of the trypsin-released inhibitor from bovine inter-alpha-trypsin inhibitor."
    Hochstrasser K., Wachter E.
    Hoppe-Seyler's Z. Physiol. Chem. 364:1679-1687(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 227-348.
  6. "Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, VII. Characterization of the bovine inhibitor as double-headed trypsin-elastase inhibitor."
    Hochstrasser K., Albrecht G.J., Schoenberger O.L., Wachter E.
    Hoppe-Seyler's Z. Physiol. Chem. 364:1689-1696(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: REACTIVE SITES.

Entry informationi

Entry nameiAMBP_BOVIN
AccessioniPrimary (citable) accession number: P00978
Secondary accession number(s): P35420, Q28020, Q3SZZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: November 11, 2015
This is version 128 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, 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.