| Tag | Content |
|---|
| CPLM ID | CPLM-011096 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Murinoglobulin-1 |
Protein Synonyms/Alias | Alpha-1 inhibitor 3 variant I; Alpha-X protein |
Gene Name | Mug1 |
Gene Synonyms/Alias | A1i3 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 347 | EVERTRNKFLFLKAD | glycation | [1] |
|
Reference | [1] Differential carbonylation of proteins as a function of in vivo oxidative stress. Madian AG, Myracle AD, Diaz-Maldonado N, Rochelle NS, Janle EM, Regnier FE. J Proteome Res. 2011 Sep 2;10(9):3959-72. [ PMID: 21800835] |
Functional Description | A proteinase activates the inhibitor by specific proteolysis in the bait region, which, by an unknown mechanism leads to reaction at the cysteinyl-glutamyl internal thiol ester site and to a conformational change, whereby the proteinase is trapped and/or covalently bound to the inhibitor. While in the tetrameric proteinase inhibitors steric inhibition is sufficiently strong, monomeric forms need a covalent linkage between the activated glutamyl residue of the original thiol ester and a terminal amino group of a lysine or another nucleophilic group on the proteinase, for inhibition to be effective. |
Sequence Annotation | REGION 686 745 Bait region (By similarity).
CARBOHYD 55 55 N-linked (GlcNAc...) (Potential).
CARBOHYD 247 247 N-linked (GlcNAc...) (Potential).
CARBOHYD 301 301 N-linked (GlcNAc...) (Potential).
CARBOHYD 321 321 N-linked (GlcNAc...) (Potential).
CARBOHYD 393 393 N-linked (GlcNAc...) (Potential).
CARBOHYD 508 508 N-linked (GlcNAc...) (Potential).
CARBOHYD 760 760 N-linked (GlcNAc...) (Potential).
CARBOHYD 787 787 N-linked (GlcNAc...) (Potential).
CARBOHYD 882 882 N-linked (GlcNAc...) (Potential).
CARBOHYD 1004 1004 N-linked (GlcNAc...) (Potential).
CARBOHYD 1153 1153 N-linked (GlcNAc...) (Potential).
CARBOHYD 1324 1324 N-linked (GlcNAc...) (Potential).
CARBOHYD 1437 1437 N-linked (GlcNAc...) (Potential).
DISULFID 48 86 By similarity.
DISULFID 251 283 By similarity.
DISULFID 269 295 By similarity.
DISULFID 468 563 By similarity.
DISULFID 595 784 By similarity.
DISULFID 643 689 By similarity.
DISULFID 860 896 By similarity.
DISULFID 934 1334 By similarity.
DISULFID 1092 1140 By similarity.
DISULFID 1365 1480 By similarity.
CROSSLNK 985 988 Isoglutamyl cysteine thioester (Cys-Gln) |
Keyword | Acute phase; Alternative splicing; Bait region; Complete proteome; Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome; Secreted; Serine protease inhibitor; Signal; Thioester bond. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1487 AA |
Protein Sequence | MKKNREAQLC LFSALLAFLP FASLLNGNSK YMVLVPSQLY TETPEKICLH LYHLNETVTV 60
TASLISQRGT RKLFDELVVD KDLFHCLSFT IPRLPSSEEE ESLDINIEGA KHKFSERRVV 120
LVKNKESVVF VQTDKPVYKP GQSVKFRVVS MDKNLHPLNE LFPLAYIEDP KMNRIMQWQD 180
IKTENGLKQL SFSLSAEPIQ GPYKIVILKQ SGVKEEHSFT VMEFVLPRFG VDVKVPNAIS 240
VYDEIINVTA CAIYTYGKPV PGHVKISLCH GNPSFSSETK SACKEEDSEL DNNGCSTQEV 300
NITEFQLKEN YLKMHQAFHV NATVTEEGTG SEFSGSGRIE VERTRNKFLF LKADSHFRHG 360
IPFFVKIRLV DIKGDPIPNE QVFIKAQEAG YTNATTTDQH GLAKFSIDTS SISGYSLNIK 420
VYHKEESSCI HSSCTAERHA EEHHTAYAVY SLSKSYIYLD TEAGVLPCNQ IHTVQAHFIL 480
KGQVLGVLPQ IVFHYLVMAQ GSILQTGNHT HQVEPGVSQV QGNFALEIPV EFSMVPVAKM 540
LIYTILPDGE VIADSVTFQV EKCLRNKVHL SFSPSQSLPA SQTHMRVTAS PQSLCGLRAV 600
DQSVLLLKPE AELSPSLIYD LPGMQDSNFI PSSYHPFEDE YDCLMYQPRD TEELTYSVPY 660
GREKDVYRYV RDMGLTAFTN LKIKHPTYCY EMNMVVLSAP AVESELSPRG GEFEMMPLGV 720
NKSPLPKEPP RKDPPPKDPV IETIRNYFPE TWIWDLVTVN SSGVTEVEMT VPDTITEWKA 780
GALCLSNDTG LGLSSVATLQ AFQPFFVELT MPYSVIRGEA FMLKATVMNY LPTSLPMAVQ 840
LEASPDFTAV PVGNDQDSYC LGANGRHTSS WLVTPKSLGN VNFSVSVEAQ QSPELCGSQV 900
ATVPETGRKD TVVKVLIVEP EGIKKEHTFS SLLCASDAEL SETLSLLLPP TVVKDSARAH 960
FSVMGDILSS AIKNTQNLIQ MPYGCGEQNM VLFAPNIYVL KYLNETQQLT EKIKSKALGY 1020
LRAGYQRELN YKHKDGSYSA FGDHNGQGQG NTWLTAFVLK SFAQARAFIF IDESHITDAF 1080
TWLSKQQKDS GCFRSSGSLF NNAMKGGVDD EITLSAYITM ALLESSLPDT DPVVSKALGC 1140
LEASWETIEQ GRNGSFVYTK TLMAYAFALA GNQEKRNEIL KSLDKEAIRE DNSIHWERPQ 1200
KPTKSEGYLY TPQASSAEVE MSAYVVLARL TAQPAPSPED LALSMGTIKW LTKQQNSHGG 1260
FSSTQDTVVA LDALSKYGAA TFSKSQKTPL VTIQSSGSFS QKFQVDNSNR LLLQQVSLPD 1320
IPGNYTVSVS GEGCVYAQTT LRYNMPLEKQ QPAFALKVQT VPLTCNNPKG QNSFQISLEI 1380
SYTGSRPASN MVIADVKMLS GFIPLKPTVK KLERLEHVSR TEVTTNNVLL YLDQVTNQTL 1440
SFSFIIQQDI PVKNLQPAIV KVYDYYETDE VAFAEYSSPC SSDKQNV 1487 |
Gene Ontology | GO:0005615; C:extracellular space; IEA:InterPro. GO:0030414; F:peptidase inhibitor activity; TAS:RGD. GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW. GO:0006953; P:acute-phase response; IEA:UniProtKB-KW. GO:0006954; P:inflammatory response; IEP:RGD. GO:0010951; P:negative regulation of endopeptidase activity; IEA:GOC. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |