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Protein AMBP [Cleaved into: Alpha-1-microglobulin; Inter-alpha-trypsin inhibitor light chain (ITI-LC) (BI-14) (Bikunin) (Cumulus extracellular matrix-stabilizing factor) (ESF) (HI-30); Trypstatin]

 AMBP_BOVIN              Reviewed;         352 AA.
P00978; P35420; Q28020; Q3SZZ4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
28-FEB-2018, entry version 138.
RecName: Full=Protein AMBP;
Contains:
RecName: Full=Alpha-1-microglobulin;
Contains:
RecName: Full=Inter-alpha-trypsin inhibitor light chain;
Short=ITI-LC;
AltName: Full=BI-14;
AltName: Full=Bikunin;
AltName: Full=Cumulus extracellular matrix-stabilizing factor;
Short=ESF;
AltName: Full=HI-30;
Contains:
RecName: Full=Trypstatin;
Flags: Precursor;
Name=AMBP; Synonyms=ITIL;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8611630; DOI=10.1016/0167-4781(95)00235-9;
Lindqvist A., Aakerstroem B.;
"Bovine alpha 1-microglobulin/bikunin. Isolation and characterization
of liver cDNA and urinary alpha 1-microglobulin.";
Biochim. Biophys. Acta 1306:98-106(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Testis;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 206-219.
TISSUE=Fetal serum;
PubMed=1376324;
Chen L., Mao S.J.T., Larsen W.J.;
"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.";
J. Biol. Chem. 267:12380-12386(1992).
[4]
PROTEIN SEQUENCE OF 227-349.
PubMed=2408637;
Hochstrasser K., Wachter E., Albrecht G.J., Reisinger P.;
"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.";
Biol. Chem. Hoppe-Seyler 366:473-478(1985).
[5]
PROTEIN SEQUENCE OF 227-348.
PubMed=6199275;
Hochstrasser K., Wachter E.;
"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.";
Hoppe-Seyler's Z. Physiol. Chem. 364:1679-1687(1983).
[6]
REACTIVE SITES.
PubMed=6199276;
Hochstrasser K., Albrecht G.J., Schoenberger O.L., Wachter E.;
"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.";
Hoppe-Seyler's Z. Physiol. Chem. 364:1689-1696(1983).
-!- FUNCTION: Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin,
and lysosomal granulocytic elastase. Inhibits calcium oxalate
crystallization.
-!- FUNCTION: Trypstatin is a trypsin inhibitor. {ECO:0000250}.
-!- FUNCTION: 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.
-!- 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. Alpha-1-microglobulin interacts with FN1.
Trypstatin is a monomer and also occurs as a complex with tryptase
in mast cells (By similarity). {ECO:0000250}.
-!- 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.
-!- PTM: The precursor is proteolytically processed into separately
functioning proteins.
-!- PTM: 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). {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; U35642; AAB07599.1; -; mRNA.
EMBL; BC102637; AAI02638.1; -; mRNA.
PIR; S68149; TIBOBI.
RefSeq; NP_776414.1; NM_173989.3.
UniGene; Bt.39060; -.
ProteinModelPortal; P00978; -.
SMR; P00978; -.
STRING; 9913.ENSBTAP00000020817; -.
MEROPS; I02.006; -.
iPTMnet; P00978; -.
PaxDb; P00978; -.
PeptideAtlas; P00978; -.
PRIDE; P00978; -.
GeneID; 280996; -.
KEGG; bta:280996; -.
CTD; 259; -.
eggNOG; KOG4295; Eukaryota.
eggNOG; ENOG410XQNP; LUCA.
HOGENOM; HOG000001572; -.
HOVERGEN; HBG000225; -.
InParanoid; P00978; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
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; IPR036880; Kunitz_BPTI_sf.
InterPro; IPR022272; Lipocalin_CS.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
InterPro; IPR020901; Prtase_inh_Kunz-CS.
PANTHER; PTHR10083:SF18; PTHR10083:SF18; 1.
Pfam; PF00014; Kunitz_BPTI; 2.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR01215; A1MCGLOBULIN.
PRINTS; PR00759; BASICPTASE.
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 20 203 Alpha-1-microglobulin.
/FTId=PRO_0000017884.
CHAIN 206 352 Inter-alpha-trypsin inhibitor light
chain.
/FTId=PRO_0000017885.
CHAIN 284 344 Trypstatin. {ECO:0000250}.
/FTId=PRO_0000318925.
DOMAIN 231 281 BPTI/Kunitz inhibitor 1.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
DOMAIN 287 337 BPTI/Kunitz inhibitor 2.
{ECO:0000255|PROSITE-ProRule:PRU00031}.
BINDING 53 53 Multimeric 3-hydroxykynurenine
chromophore (covalent). {ECO:0000250}.
BINDING 111 111 Multimeric 3-hydroxykynurenine
chromophore (covalent). {ECO:0000250}.
BINDING 137 137 Multimeric 3-hydroxykynurenine
chromophore (covalent). {ECO:0000250}.
BINDING 149 149 Multimeric 3-hydroxykynurenine
chromophore (covalent). {ECO:0000250}.
SITE 241 242 Inhibitory (P1) (chymotrypsin, elastase).
SITE 297 298 Inhibitory (P1) (trypsin).
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 223 223 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 250 250 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:6199275}.
DISULFID 91 188 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 231 281 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 240 264 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 256 277 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 287 337 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 296 320 {ECO:0000255|PROSITE-ProRule:PRU00031}.
DISULFID 312 333 {ECO:0000255|PROSITE-ProRule:PRU00031}.
CONFLICT 71 71 I -> K (in Ref. 2; AAI02638).
{ECO:0000305}.
CONFLICT 103 103 A -> T (in Ref. 2; AAI02638).
{ECO:0000305}.
CONFLICT 200 200 L -> V (in Ref. 2; AAI02638).
{ECO:0000305}.
CONFLICT 209 209 T -> G (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 217 217 A -> D (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 268 268 G -> L (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
CONFLICT 274 274 E -> Q (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
CONFLICT 298 299 SY -> AF (in Ref. 4; AA sequence and 5;
AA sequence). {ECO:0000305}.
CONFLICT 305 305 F -> I (in Ref. 2; AAI02638).
{ECO:0000305}.
CONFLICT 330 330 E -> Q (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
CONFLICT 346 346 E -> R (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
SEQUENCE 352 AA; 39235 MW; ED31C5CA02E70B19 CRC64;
MRSLSGLLLL LTACLAVNAS SVPTLPDDIQ VQENFDLSRI YGKWFNVAVG STCPWLKRFK
EKMTMSTVVL IAGPTSKEIS VTNTHRRKGV CESISGTYEK TSADGKFLYH KAKWNITMES
YVVHTNYDEY AIFLTKKLSR RHGPTITVKL YGREPQLRES LLEEFREVAL GVGIPEDAIF
TMPDRGECVP GEQDPVPTPL SRARRAVLTQ EEEGSGAGQP VTNFSKKADS CQLDYSQGPC
LGLFKRYFYN GTSMACETFL YGGCMGNGNN FLSEKECLQT CRTVEACNLP IVQGPCRSYI
QLWAFDAVKG KCVRFSYGGC KGNGNKFYSE KECKEYCGIP GEADEELLRF SN


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