AMBP_PLEPL
ID AMBP_PLEPL Reviewed; 355 AA.
AC P36992;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein AMBP;
DE Contains:
DE RecName: Full=Alpha-1-microglobulin;
DE Contains:
DE RecName: Full=Inter-alpha-trypsin inhibitor light chain;
DE Short=ITI-LC;
DE AltName: Full=Bikunin;
DE AltName: Full=HI-30;
DE Flags: Precursor; Fragment;
OS Pleuronectes platessa (European plaice).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae;
OC Pleuronectes.
OX NCBI_TaxID=8262;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7521726; DOI=10.1016/0305-0491(94)90077-9;
RA Leaver M.J., Wright J., George S.G.;
RT "Conservation of the tandem arrangement of alpha 1-microglobulin/bikunin
RT mRNA: cloning of a cDNA from plaice (Pleuronectes platessa).";
RL Comp. Biochem. Physiol. 108B:275-281(1994).
CC -!- SUBUNIT: I-alpha-I plasma protease inhibitors are assembled from one or
CC two heavy chains (H1, H2 or H3) and one light chain, bikunin. Inter-
CC alpha-inhibitor (I-alpha-I) is composed of H1, H2 and bikunin, inter-
CC alpha-like inhibitor (I-alpha-LI) of H2 and bikunin, and pre-alpha-
CC inhibitor (P-alpha-I) of H3 and bikunin (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC -!- PTM: The precursor is proteolytically processed into two separately
CC functioning proteins. {ECO:0000250}.
CC -!- PTM: 3-hydroxykynurenine, an oxidized tryptophan metabolite that is
CC common in biological fluids, reacts with Cys-55, Lys-138, and Lys-150
CC to form heterogeneous polycyclic chromophores including
CC hydroxanthommatin. The reaction by alpha-1-microglobulin is
CC autocatalytic. The chromophore can react with accessible cysteines
CC forming non-reducible thioether cross-links with other molecules of
CC alpha-1-microglobulin or with other proteins (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the calycin
CC superfamily. Lipocalin family. {ECO:0000305}.
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DR EMBL; X63762; CAA45294.1; -; mRNA.
DR PIR; S22181; S22181.
DR AlphaFoldDB; P36992; -.
DR SMR; P36992; -.
DR MEROPS; I02.005; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; KU; 2.
DR Gene3D; 2.40.128.20; -; 1.
DR Gene3D; 4.10.410.10; -; 2.
DR InterPro; IPR002968; A1-microglobln.
DR InterPro; IPR029856; AMBP.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR PANTHER; PTHR46676; PTHR46676; 1.
DR Pfam; PF00014; Kunitz_BPTI; 2.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01215; A1MCGLOBULIN.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 2.
DR SUPFAM; SSF50814; SSF50814; 1.
DR SUPFAM; SSF57362; SSF57362; 2.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 2.
PE 2: Evidence at transcript level;
KW Chromophore; Cleavage on pair of basic residues; Disulfide bond;
KW Glycoprotein; Protease inhibitor; Repeat; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL <1..?
FT /evidence="ECO:0000255"
FT CHAIN ?..204
FT /note="Alpha-1-microglobulin"
FT /id="PRO_0000017900"
FT CHAIN 210..355
FT /note="Inter-alpha-trypsin inhibitor light chain"
FT /id="PRO_0000017901"
FT DOMAIN 236..286
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 292..342
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT BINDING 55
FT /ligand="3-hydroxy-L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:58125"
FT /ligand_note="multimeric 3-hydroxykynurenine chromophore"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="3-hydroxy-L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:58125"
FT /ligand_note="multimeric 3-hydroxykynurenine chromophore"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="3-hydroxy-L-kynurenine"
FT /ligand_id="ChEBI:CHEBI:58125"
FT /ligand_note="multimeric 3-hydroxykynurenine chromophore"
FT /note="covalent"
FT /evidence="ECO:0000250"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 92..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 236..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 245..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 261..282
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 292..342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 301..325
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 317..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT NON_TER 1
SQ SEQUENCE 355 AA; 39669 MW; 2A60270FC711CD86 CRC64;
RLKTTVVLVP LLLLGWTGTL QGLPVLPEPL YPTQENFDLT RFVGTWHDVA LTSSCPHMQR
NRADAAIGKL VLEKDTGNKL KVTRTRLRHG TCVEMSGEYE LTSTPGRIFY HIDRWDADVD
AYVVHTNYDE YAIIIMSKQK TSGENSTSLK LYSRTMSVRD TVLDDFKTLV RHQGMSDDTI
IIKQNKGDCI PGEQVEEAPS QPEPKRLRRQ VLPTLALSDE EGSGDMSALF NDSEACKAAP
ETGPCFGFIQ GFFYNSTSMR CELFTYGGCL GNQNNFVTVR ECLQRCRTEA VCRLPMAPEP
CTGQPTIWAF DFVTGSCMPY KDGICQANAN QFYSRAECQE YCGVIKDDGE LLTAS
