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Protein AMBP [Cleaved into: Alpha-1-microglobulin; Inter-alpha-trypsin inhibitor light chain (ITI-LC) (Bikunin) (HI-30); Trypstatin]

 AMBP_RAT                Reviewed;         349 AA.
Q64240; P19603; Q63336;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
30-AUG-2017, entry version 143.
RecName: Full=Protein AMBP;
Contains:
RecName: Full=Alpha-1-microglobulin;
Contains:
RecName: Full=Inter-alpha-trypsin inhibitor light chain;
Short=ITI-LC;
AltName: Full=Bikunin;
AltName: Full=HI-30;
Contains:
RecName: Full=Trypstatin;
Flags: Precursor;
Name=Ambp; Synonyms=Itil;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=1371936; DOI=10.1016/0167-4781(92)90462-9;
Lindqvist A., Bratt T., Altieri M., Kastern W., Aakerstroem B.;
"Rat alpha 1-microglobulin: co-expression in liver with the light
chain of inter-alpha-trypsin inhibitor.";
Biochim. Biophys. Acta 1130:63-67(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Spleen;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 141-195.
PubMed=2429963;
Kastern W., Bjoerck L., Aakerstroem B.;
"Developmental and tissue-specific expression of alpha 1-microglobulin
mRNA in the rat.";
J. Biol. Chem. 261:15070-15074(1986).
[4]
PROTEIN SEQUENCE OF 283-343, AND CHARACTERIZATION.
STRAIN=Wistar;
PubMed=3263966;
Kido H., Yokogoshi Y., Katunuma N.;
"Kunitz-type protease inhibitor found in rat mast cells. Purification,
properties, and amino acid sequence.";
J. Biol. Chem. 263:18104-18107(1988).
[5]
INTERACTION WITH FN1.
PubMed=7519849; DOI=10.1042/bj3010745;
Falkenberg C., Enghild J.J., Thoegersen I.B., Salvesen G.,
Aakerstroem B.;
"Isolation and characterization of fibronectin-alpha 1-microglobulin
complex in rat plasma.";
Biochem. J. 301:745-751(1994).
[6]
PROTEOLYTIC PROCESSING.
PubMed=7508921;
Itoh H., Ide H., Ishikawa N., Nawa Y.;
"Mast cell protease inhibitor, trypstatin, is a fragment of inter-
alpha-trypsin inhibitor light chain.";
J. Biol. Chem. 269:3818-3822(1994).
-!- FUNCTION: Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin,
and lysosomal granulocytic elastase. Inhibits calcium oxalate
crystallization (By similarity). {ECO:0000250}.
-!- FUNCTION: Trypstatin is a trypsin inhibitor. It inhibits blood
coagulation factor Xa and tryptase about 100-fold more rapidly
than porcine pancreatic trypsin and chymase.
-!- SUBUNIT: 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. {ECO:0000250,
ECO:0000269|PubMed:7519849}.
-!- 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. Trypstatin is
present in mast cell granules.
-!- PTM: The precursor is proteolytically processed into separately
functioning proteins. {ECO:0000269|PubMed:7508921}.
-!- PTM: 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). {ECO:0000250}.
-!- PTM: Heavy chains are interlinked with bikunin via a chondroitin
4-sulfate bridge to the their C-terminal aspartate. {ECO:0000250}.
-!- SIMILARITY: In the N-terminal section; belongs to the calycin
superfamily. Lipocalin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; S87544; AAB21782.1; -; mRNA.
EMBL; BC088166; AAH88166.1; -; mRNA.
EMBL; J02600; AAA41596.1; -; mRNA.
PIR; S21089; S21089.
RefSeq; NP_037033.1; NM_012901.1.
UniGene; Rn.18721; -.
ProteinModelPortal; Q64240; -.
SMR; Q64240; -.
STRING; 10116.ENSRNOP00000009248; -.
MEROPS; I02.005; -.
iPTMnet; Q64240; -.
PhosphoSitePlus; Q64240; -.
PaxDb; Q64240; -.
PRIDE; Q64240; -.
Ensembl; ENSRNOT00000009248; ENSRNOP00000009248; ENSRNOG00000006889.
GeneID; 25377; -.
KEGG; rno:25377; -.
UCSC; RGD:2102; rat.
CTD; 259; -.
RGD; 2102; Ambp.
eggNOG; KOG4295; Eukaryota.
eggNOG; ENOG410XQNP; LUCA.
GeneTree; ENSGT00740000114929; -.
HOGENOM; HOG000001572; -.
HOVERGEN; HBG000225; -.
InParanoid; Q64240; -.
OMA; RHGPTIT; -.
OrthoDB; EOG091G09P2; -.
PhylomeDB; Q64240; -.
TreeFam; TF351222; -.
Reactome; R-RNO-2168880; Scavenging of heme from plasma.
PRO; PR:Q64240; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000006889; -.
Genevisible; Q64240; RN.
GO; GO:0072562; C:blood microparticle; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0019862; F:IgA binding; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:RGD.
GO; GO:0036094; F:small molecule binding; IEA:InterPro.
GO; GO:0030163; P:protein catabolic process; IDA:RGD.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
CDD; cd00109; KU; 2.
Gene3D; 2.40.128.20; -; 1.
Gene3D; 4.10.410.10; -; 2.
InterPro; IPR002968; A1-microglobln.
InterPro; IPR029856; AMBP.
InterPro; IPR012674; Calycin.
InterPro; IPR002223; Kunitz_BPTI.
InterPro; IPR002345; Lipocalin.
InterPro; IPR022272; Lipocalin_CS.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
PANTHER; PTHR10083:SF281; PTHR10083:SF281; 1.
Pfam; PF00014; Kunitz_BPTI; 2.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR01215; A1MCGLOBULIN.
PRINTS; PR00759; BASICPTASE.
PRINTS; PR00179; LIPOCALIN.
SMART; SM00131; KU; 2.
SUPFAM; SSF50814; SSF50814; 1.
SUPFAM; SSF57362; SSF57362; 2.
PROSITE; PS00280; BPTI_KUNITZ_1; 2.
PROSITE; PS50279; BPTI_KUNITZ_2; 2.
PROSITE; PS00213; LIPOCALIN; 1.
1: Evidence at protein level;
Chromophore; Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Protease inhibitor; Reference proteome; Repeat; Secreted;
Serine protease inhibitor; Signal.
SIGNAL 1 19 {ECO:0000250}.
CHAIN 20 202 Alpha-1-microglobulin.
/FTId=PRO_0000017897.
CHAIN 205 349 Inter-alpha-trypsin inhibitor light
chain.
/FTId=PRO_0000017898.
CHAIN 283 343 Trypstatin.
/FTId=PRO_0000017899.
DOMAIN 230 280 BPTI/Kunitz inhibitor 1.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
DOMAIN 286 336 BPTI/Kunitz inhibitor 2.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
BINDING 52 52 Multimeric 3-hydroxykynurenine
chromophore (covalent). {ECO:0000250}.
BINDING 110 110 Multimeric 3-hydroxykynurenine
chromophore (covalent). {ECO:0000250}.
BINDING 136 136 Multimeric 3-hydroxykynurenine
chromophore (covalent). {ECO:0000250}.
BINDING 148 148 Multimeric 3-hydroxykynurenine
chromophore (covalent). {ECO:0000250}.
SITE 240 241 Inhibitory (P1) (chymotrypsin, elastase).
{ECO:0000250}.
SITE 296 297 Inhibitory (P1) (trypsin). {ECO:0000250}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 233 233 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 90 187 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 230 280 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 239 263 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 255 276 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 286 336 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 295 319 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 311 332 {ECO:0000255|PROSITE-ProRule:PRU00031}.
CONFLICT 142 142 G -> A (in Ref. 3; AAA41596).
{ECO:0000305}.
CONFLICT 302 302 W -> L (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 323 323 G -> N (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 330 331 KE -> PK (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 334 334 E -> W (in Ref. 4; AA sequence).
{ECO:0000305}.
SEQUENCE 349 AA; 38851 MW; 1B7FB7DCB0824E01 CRC64;
MQGLGALFLL LTACLTLKAD NVPTLPDIQV QENFNEARIY GKWFNLAVGS TCPWLRRIKN
KMSVSTLVLQ EGATEAEISV TSTQWRKGVC EEISGVYQKT DIDGKFLYHK SKWNATLESY
VVHTNYDEYA IFLTKKFSHR HGPTITAKLY GREPQLRDSL LQEFREVALS VGIPENSIVF
MADRGECVPG DREVESTSFA RARRAVLPQE NEGSGSEPLI TGTLKKEDSC QLNYSEGPCL
GMQQKYYYNG ASMACETFQY GGCLGNGNNF ASEKECLQTC RTIAACNLPI VQGPCRAFAE
LWAFDAAQGK CIQFIYGGCK GNGNKFYSEK ECKEYCGVPG DGYEELTRS


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