| Tag | Content |
|---|
| CPLM ID | CPLM-014596 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein AMBP |
Protein Synonyms/Alias | Alpha-1-microglobulin; Inter-alpha-trypsin inhibitor light chain; ITI-LC; Bikunin; HI-30; Trypstatin |
Gene Name | Ambp |
Gene Synonyms/Alias | Itil |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 325 | GCKGNGNKFYSEKEC | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Inter-alpha-trypsin inhibitor inhibits trypsin, plasmin, and lysosomal granulocytic elastase. Inhibits calcium oxalate crystallization (By similarity). |
Sequence Annotation | DOMAIN 230 280 BPTI/Kunitz inhibitor 1.
DOMAIN 286 336 BPTI/Kunitz inhibitor 2.
BINDING 52 52 Multimeric 3-hydroxykynurenine
BINDING 110 110 Multimeric 3-hydroxykynurenine
BINDING 136 136 Multimeric 3-hydroxykynurenine
BINDING 148 148 Multimeric 3-hydroxykynurenine
MOD_RES 197 197 Phosphothreonine (By similarity).
CARBOHYD 114 114 N-linked (GlcNAc...) (Potential).
CARBOHYD 233 233 N-linked (GlcNAc...) (Potential).
DISULFID 90 187 By similarity.
DISULFID 230 280 By similarity.
DISULFID 239 263 By similarity.
DISULFID 255 276 By similarity.
DISULFID 286 336 By similarity.
DISULFID 295 319 By similarity.
DISULFID 311 332 By similarity. |
Keyword | Chromophore; Cleavage on pair of basic residues; Complete proteome; Direct protein sequencing; Disulfide bond; Glycoprotein; Phosphoprotein; Protease inhibitor; Reference proteome; Repeat; Secreted; Serine protease inhibitor; Signal. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 349 AA |
Protein Sequence | MQGLGALFLL LTACLTLKAD NVPTLPDIQV QENFNEARIY GKWFNLAVGS TCPWLRRIKN 60
KMSVSTLVLQ EGATEAEISV TSTQWRKGVC EEISGVYQKT DIDGKFLYHK SKWNATLESY 120
VVHTNYDEYA IFLTKKFSHR HGPTITAKLY GREPQLRDSL LQEFREVALS VGIPENSIVF 180
MADRGECVPG DREVESTSFA RARRAVLPQE NEGSGSEPLI TGTLKKEDSC QLNYSEGPCL 240
GMQQKYYYNG ASMACETFQY GGCLGNGNNF ASEKECLQTC RTIAACNLPI VQGPCRAFAE 300
LWAFDAAQGK CIQFIYGGCK GNGNKFYSEK ECKEYCGVPG DGYEELTRS 349 |
Gene Ontology | GO:0009986; C:cell surface; IDA:RGD. GO:0005615; C:extracellular space; IDA:RGD. GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD. GO:0005886; C:plasma membrane; ISS:UniProtKB. GO:0020037; F:heme binding; ISS:UniProtKB. GO:0019862; F:IgA binding; ISS:UniProtKB. GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:RGD. GO:0036094; F:small molecule binding; IEA:InterPro. GO:0030163; P:protein catabolic process; IDA:RGD. GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |