Reviewed, UniProtKB/Swiss-Prot Q07456 (AMBP_MOUSE)

Names and originHide

Protein names

Recommended name:
Protein AMBP

Cleaved into the following 3 chains:

1. Alpha-1-microglobulin
2. Inter-alpha-trypsin inhibitor light chain
   Short name=ITI-LC
   Alternative name(s):
   Bikunin
   HI-30
3. Trypstatin

Gene names

Name:	Ambp
Synonyms:	Itil

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributesHide

Sequence length	349 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)Hide

Function	Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization By similarity. Trypstatin is a trypsin inhibitor By similarity.
Subunit structure	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.
Subcellular location	Secreted.
Tissue specificity	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.
Post-translational modification	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. Heavy chains are interlinked with bikunin via a chondroitin 4-sulfate bridge to the their C-terminal aspartate By similarity.
Sequence similarities	In the N-terminal section; belongs to the calycin superfamily. Lipocalin family. Contains 2 BPTI/Kunitz inhibitor domains.

OntologiesHide

Keywords
Cellular component	Secreted
Domain	Repeat Signal
Ligand	Chromophore
Molecular function	Protease inhibitor Serine protease inhibitor
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	IgA binding Inferred from sequence or structural similarity. Source: UniProtKB heme binding Inferred from sequence or structural similarity. Source: UniProtKB protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB serine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)Hide

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 19	19	By similarity
	Chain	20 – 202	183	Alpha-1-microglobulin		PRO_0000017893
	Chain	205 – 349	145	Inter-alpha-trypsin inhibitor light chain		PRO_0000017894
	Chain	283 – 343	61	Trypstatin By similarity		PRO_0000318928
Regions
	Domain	230 – 280	51	BPTI/Kunitz inhibitor 1
	Domain	286 – 336	51	BPTI/Kunitz inhibitor 2
Sites
	Binding site	52	1	Multimeric 3-hydroxykynurenine chromophore (covalent) By similarity
	Binding site	110	1	Multimeric 3-hydroxykynurenine chromophore (covalent) By similarity
	Binding site	136	1	Multimeric 3-hydroxykynurenine chromophore (covalent) By similarity
	Binding site	148	1	Multimeric 3-hydroxykynurenine chromophore (covalent) By similarity
	Site	240 – 241	2	Inhibitory (P1) (chymotrypsin, elastase) By similarity
	Site	296 – 297	2	Inhibitory (P1) (trypsin) By similarity
Amino acid modifications
	Modified residue	197	1	Phosphothreonine Ref.6
	Glycosylation	33	1	N-linked (GlcNAc...) Potential
	Glycosylation	114	1	N-linked (GlcNAc...) Potential
	Glycosylation	233	1	N-linked (GlcNAc...) Potential
	Disulfide bond	90 ↔ 187		By similarity
	Disulfide bond	230 ↔ 280		By similarity
	Disulfide bond	239 ↔ 263		By similarity
	Disulfide bond	255 ↔ 276		By similarity
	Disulfide bond	286 ↔ 336		By similarity
	Disulfide bond	295 ↔ 319		By similarity
	Disulfide bond	311 ↔ 332		By similarity
Experimental info
	Sequence conflict	65	1	S → Q in CAA48640. Ref.1
	Sequence conflict	185	1	G → E in BAB23659. Ref.4

SequencesHide

	Sequence		Length	Mass (Da)
	Q07456-1 [UniParc]. Last modified February 26, 2008. Version 2. Checksum: CFB9208D37DF0021	FASTA	349	39,029
	10 20 30 40 50 60 MQGLRTLFLL LTACLASRAD PASTLPDIQV QENFSESRIY GKWYNLAVGS TCPWLSRIKD 70 80 90 100 110 120 KMSVSTLVLQ EGATETEISM TSTRWRRGVC EEITGAYQKT DIDGKFLYHK SKWNITLESY 130 140 150 160 170 180 VVHTNYDEYA IFLTKKSSHH HGLTITAKLY GREPQLRDSL LQEFKDVALN VGISENSIIF 190 200 210 220 230 240 MPDRGECVPG DREVEPTSIA RARRAVLPQE SEGSGTEPLI TGTLKKEDSC QLNYSEGPCL 250 260 270 280 290 300 GMQERYYYNG ASMACETFQY GGCLGNGNNF ISEKDCLQTC RTIAACNLPI VQGPCRAFIK 310 320 330 340 LWAFDAAQGK CIQFHYGGCK GNGNKFYSEK ECKEYCGVPG DGYEELIRS

ReferencesHide

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7689339] [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: 7533761] [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: 10395906] [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: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Salivary gland.
[6]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-197, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-referencesHide

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00127352.
PIR	S35708.
RefSeq	NP_031469.1.
UniGene	Mm.2197
3D structure databases
SMR	Q07456. Positions 22-194, 229-338.
ModBase	Search...
Protein-protein interaction databases
STRING	Q07456.
Protein family/group databases
MEROPS	I02.006.
PTM databases
PhosphoSite	Q07456.
Proteomic databases
PRIDE	Q07456.
Genome annotation databases
Ensembl	ENSMUST00000030041; ENSMUSP00000030041; ENSMUSG00000028356; Mus musculus. [Genome view]
GeneID	11699.
KEGG	mmu:11699.
Organism-specific databases
CTD	11699.
MGI	MGI:88002. Ambp.
Phylogenomic databases
eggNOG	roNOG12243.
HOGENOM	HBG715490.
HOVERGEN	HBG000225.
InParanoid	Q07456.
OMA	GKFLYHK.
OrthoDB	EOG9G7FHK.
PhylomeDB	Q07456.
Gene expression databases
ArrayExpress	Q07456.
Bgee	Q07456.
CleanEx	MM_AMBP.
Genevestigator	Q07456.
GermOnline	ENSMUSG00000028356. Mus musculus.
Family and domain databases
InterPro	IPR002968. A1-microglobln. IPR012674. Calycin. IPR011038. Calycin-like. IPR002345. Lipocalin. IPR022272. Lipocalin_CS. IPR000566. Lipocln_cytosolic_FA-bd. IPR002223. Prot_inh_Kunz-m. IPR020901. Prtase_inh_Kunz-CS. [Graphical view]
Gene3D	G3DSA:2.40.128.20. Calycin. 1 hit. G3DSA:4.10.410.10. Prot_inh_Kunz-m. 1 hit.
Pfam	PF00014. Kunitz_BPTI. 2 hits. PF00061. Lipocalin. 1 hit. [Graphical view]
PRINTS	PR01215. A1MCGLOBULIN. PR00759. BASICPTASE. PR00179. LIPOCALIN.
SMART	SM00131. KU. 2 hits. [Graphical view]
SUPFAM	SSF50814. Calycin. 1 hit. SSF57362. Prot_inh_Kunz-m. 2 hits.
PROSITE	PS00280. BPTI_KUNITZ_1. 2 hits. PS50279. BPTI_KUNITZ_2. 2 hits. PS00213. LIPOCALIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	279367.
SOURCE	Search...

Entry informationHide

Entry name

AMBP_MOUSE

Accession

Primary (citable) accession number: Q07456
Secondary accession number(s): Q61294, Q925W1, Q9DBJ9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	February 26, 2008
Last modified:	July 13, 2010
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)