LOCUS       NP_001624                352 aa            linear   PRI 27-APR-2025
DEFINITION  protein AMBP preproprotein [Homo sapiens].
ACCESSION   NP_001624
VERSION     NP_001624.1
DBSOURCE    REFSEQ: accession NM_001633.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 352)
  AUTHORS   Jin,L., Niu,C. and Ni,Y.
  TITLE     Correlation between peripheral blood alpha1-MG, DNMT1 expression,
            and the severity of diabetic nephropathy renal pathological damage
  JOURNAL   Medicine (Baltimore) 102 (42), e35409 (2023)
   PUBMED   37861555
  REMARK    GeneRIF: Correlation between peripheral blood alpha1-MG, DNMT1
            expression, and the severity of diabetic nephropathy renal
            pathological damage.
REFERENCE   2  (residues 1 to 352)
  AUTHORS   Xu,Y., Carr,P.D., Guss,J.M. and Ollis,D.L.
  TITLE     The crystal structure of bikunin from the inter-alpha-inhibitor
            complex: a serine protease inhibitor with two Kunitz domains
  JOURNAL   J Mol Biol 276 (5), 955-966 (1998)
   PUBMED   9566199
REFERENCE   3  (residues 1 to 352)
  AUTHORS   Vetr,H. and Gebhard,W.
  TITLE     Structure of the human alpha 1-microglobulin-bikunin gene
  JOURNAL   Biol Chem Hoppe Seyler 371 (12), 1185-1196 (1990)
   PUBMED   1708673
REFERENCE   4  (residues 1 to 352)
  AUTHORS   Diarra-Mehrpour,M., Bourguignon,J., Sesboue,R., Salier,J.P.,
            Leveillard,T. and Martin,J.P.
  TITLE     Structural analysis of the human inter-alpha-trypsin inhibitor
            light-chain gene
  JOURNAL   Eur J Biochem 191 (1), 131-139 (1990)
   PUBMED   1696200
REFERENCE   5  (residues 1 to 352)
  AUTHORS   Schreitmuller,T., Hochstrasser,K., Reisinger,P.W., Wachter,E. and
            Gebhard,W.
  TITLE     cDNA cloning of human inter-alpha-trypsin inhibitor discloses three
            different proteins
  JOURNAL   Biol Chem Hoppe Seyler 368 (8), 963-970 (1987)
   PUBMED   3663330
REFERENCE   6  (residues 1 to 352)
  AUTHORS   Kaumeyer,J.F., Polazzi,J.O. and Kotick,M.P.
  TITLE     The mRNA for a proteinase inhibitor related to the HI-30 domain of
            inter-alpha-trypsin inhibitor also encodes alpha-1-microglobulin
            (protein HC)
  JOURNAL   Nucleic Acids Res 14 (20), 7839-7850 (1986)
   PUBMED   2430261
REFERENCE   7  (residues 1 to 352)
  AUTHORS   Traboni,C. and Cortese,R.
  TITLE     Sequence of a full length cDNA coding for human protein HC (alpha 1
            microglobulin)
  JOURNAL   Nucleic Acids Res 14 (15), 6340 (1986)
   PUBMED   2428011
REFERENCE   8  (residues 1 to 352)
  AUTHORS   Lopez Otin,C., Grubb,A.O. and Mendez,E.
  TITLE     The complete amino acid sequence of human complex-forming
            glycoprotein heterogeneous in charge (protein HC) from one
            individual
  JOURNAL   Arch Biochem Biophys 228 (2), 544-554 (1984)
   PUBMED   6198962
REFERENCE   9  (residues 1 to 352)
  AUTHORS   Takagi,T., Takagi,K. and Kawai,T.
  TITLE     Complete amino acid sequence of human alpha 1-microglobulin
  JOURNAL   Biochem Biophys Res Commun 98 (4), 997-1001 (1981)
   PUBMED   6164372
REFERENCE   10 (residues 1 to 352)
  AUTHORS   Ekstrom,B. and Berggard,I.
  TITLE     Human alpha1-microglobulin. Purification procedure, chemical and
            physiochemical properties
  JOURNAL   J Biol Chem 252 (22), 8048-8057 (1977)
   PUBMED   72071
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from BC041593.1.
            
            Summary: This gene encodes a complex glycoprotein secreted in
            plasma. The precursor is proteolytically processed into distinct
            functioning proteins: alpha-1-microglobulin, which belongs to the
            superfamily of lipocalin transport proteins and may play a role in
            the regulation of inflammatory processes, and bikunin, which is a
            urinary trypsin inhibitor belonging to the superfamily of
            Kunitz-type protease inhibitors and plays an important role in many
            physiological and pathological processes. This gene is located on
            chromosome 9 in a cluster of lipocalin genes. [provided by RefSeq,
            Jul 2008].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC041593.1, SRR5189652.12257.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA2145122, SAMEA2155590
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000265132.8/ ENSP00000265132.3
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..352
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="9"
                     /map="9q32"
     Protein         1..352
                     /product="protein AMBP preproprotein"
                     /note="protein HC; complex-forming glycoprotein
                     heterogeneous in charge; uronic-acid-rich protein;
                     trypstatin; bikunin; inter-alpha-trypsin inhibitor light
                     chain; protein AMBP; uristatin; growth-inhibiting protein
                     19"
                     /calculated_mol_wt=37115
     sig_peptide     1..19
                     /inference="COORDINATES: ab initio prediction:SignalP:6.0"
                     /calculated_mol_wt=1902
     mat_peptide     20..203
                     /product="Alpha-1-microglobulin. /id=PRO_0000017886"
                     /note="propagated from UniProtKB/Swiss-Prot (P02760.1)"
                     /calculated_mol_wt=20847
     Site            24
                     /site_type="glycosylation"
                     /note="O-linked (GalNAc...) threonine.
                     /evidence=ECO:0000269|PubMed:1694784. /id=CAR_000172;
                     propagated from UniProtKB/Swiss-Prot (P02760.1)"
     Region          28..190
                     /region_name="lipocalin_A1M-like"
                     /note="lipocalin domain of alpha1-microglobulin and
                     similar proteins; cd19418"
                     /db_xref="CDD:381193"
     Site            36
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:1694784; propagated from
                     UniProtKB/Swiss-Prot (P02760.1)"
     Site            order(40,44,68,70,79,81,83,94,96,98,107,109,118,120,122,
                     131,133,135,147,149,151)
                     /site_type="other"
                     /note="ligand binding cavity [chemical binding]"
                     /db_xref="CDD:381193"
     Site            115
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:1694784,
                     ECO:0000269|PubMed:22171320; propagated from
                     UniProtKB/Swiss-Prot (P02760.1)"
     Site            199
                     /site_type="cleavage"
                     /note="Cleavage, in the presence of oxyhemoglobin or MPO.
                     /evidence=ECO:0000269|PubMed:11877257; propagated from
                     UniProtKB/Swiss-Prot (P02760.1)"
     mat_peptide     206..352
                     /product="Inter-alpha-trypsin inhibitor light chain.
                     /id=PRO_0000017887"
                     /note="propagated from UniProtKB/Swiss-Prot (P02760.1)"
                     /calculated_mol_wt=15974
     Region          206..226
                     /region_name="Glycopeptide (secretory piece)"
                     /note="propagated from UniProtKB/Swiss-Prot (P02760.1)"
     Site            215
                     /site_type="glycosylation"
                     /note="O-linked (Xyl...) (chondroitin sulfate) serine.
                     /evidence=ECO:0000269|PubMed:1898736,
                     ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:32337544,
                     ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717,
                     ECO:0000269|PubMed:6171497, ECO:0000269|PubMed:7682553;
                     propagated from UniProtKB/Swiss-Prot (P02760.1)"
     Region          229..282
                     /region_name="Kunitz_bikunin_1-like"
                     /note="first Kunitz domain of bikunin and similar
                     proteins; cd22596"
                     /db_xref="CDD:438639"
     Site            order(237..241,243..245,260,264)
                     /site_type="other"
                     /note="putative serine protease binding site [polypeptide
                     binding]"
                     /db_xref="CDD:438639"
     Site            241..242
                     /site_type="inhibition"
                     /note="Inhibitory (P1) (chymotrypsin, elastase).
                     /evidence=ECO:0000250; propagated from
                     UniProtKB/Swiss-Prot (P02760.1)"
     Site            250
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) (complex) asparagine.
                     /evidence=ECO:0000269|PubMed:22171320,
                     ECO:0000269|PubMed:6171497; propagated from
                     UniProtKB/Swiss-Prot (P02760.1)"
     mat_peptide     284..344
                     /product="Trypstatin. /evidence=ECO:0000250.
                     /id=PRO_0000318926"
                     /note="propagated from UniProtKB/Swiss-Prot (P02760.1)"
                     /calculated_mol_wt=6620
     Region          284..338
                     /region_name="Kunitz_bikunin_2-like"
                     /note="second Kunitz domain of bikunin and similar
                     proteins; cd22597"
                     /db_xref="CDD:438640"
     Site            order(295..300,318..321)
                     /site_type="other"
                     /note="serine protease binding site [polypeptide binding]"
                     /db_xref="CDD:438640"
     Site            297..298
                     /site_type="inhibition"
                     /note="Inhibitory (P1) (trypsin). /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (P02760.1)"
     CDS             1..352
                     /gene="AMBP"
                     /gene_synonym="A1M; EDC1; HCP; HI30; IATIL; ITI; ITIL;
                     ITILC; UTI"
                     /coded_by="NM_001633.4:92..1150"
                     /db_xref="CCDS:CCDS6800.1"
                     /db_xref="GeneID:259"
                     /db_xref="HGNC:HGNC:453"
                     /db_xref="MIM:176870"
ORIGIN      
        1 mrslgallll lsaclavsag pvptppdniq vqenfnisri ygkwynlaig stcpwlkkim
       61 drmtvstlvl gegateaeis mtstrwrkgv ceetsgayek tdtdgkflyh kskwnitmes
      121 yvvhtnydey aifltkkfsr hhgptitakl ygrapqlret llqdfrvvaq gvgipedsif
      181 tmadrgecvp geqepepili prvrravlpq eeegsgggql vtevtkkeds cqlgysagpc
      241 mgmtsryfyn gtsmacetfq yggcmgngnn fvtekeclqt crtvaacnlp ivrgpcrafi
      301 qlwafdavkg kcvlfpyggc qgngnkfyse kecreycgvp gdgdeellrf sn
//
