| Tag | Content |
|---|
| CPLM ID | CPLM-014483 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Alpha-1-macroglobulin |
Protein Synonyms/Alias | Alpha-1-M; Alpha-1-macroglobulin 165 kDa subunit; Alpha-1-macroglobulin 45 kDa subunit |
Gene Name | A1m |
Gene Synonyms/Alias | Pzp |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 114 | GPTHHFIKKKSMWIT | acetylation | [1] | | 137 | QTDKPIYKPGQTVKF | acetylation | [1] | | 207 | IYKVVVQKDSGKKIE | acetylation | [1] | | 220 | IEHSFEVKEYVLPKF | acetylation | [1] | | 226 | VKEYVLPKFEVQVKM | acetylation | [1] | | 318 | RQKGYDMKIEVEAKI | acetylation | [1] | | 915 | VQKDTVVKPVIVEPE | acetylation | [1] | | 1088 | AFNWLSMKQRENGCF | acetylation | [1] | | 1256 | SDLTTASKIVKWISK | acetylation | [1] | | 1259 | TTASKIVKWISKQQN | acetylation | [1] | | 1378 | TLPLNFDKAEHHRKF | 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 | Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase (By similarity). |
Sequence Annotation | REGION 686 746 Bait region (By similarity).
REGION 1360 1500 Receptor-binding domain.
CARBOHYD 55 55 N-linked (GlcNAc...) (Potential).
CARBOHYD 61 61 N-linked (GlcNAc...) (Potential).
CARBOHYD 157 157 N-linked (GlcNAc...) (Potential).
CARBOHYD 382 382 N-linked (GlcNAc...) (Potential).
CARBOHYD 412 412 N-linked (GlcNAc...) (Potential).
CARBOHYD 568 568 N-linked (GlcNAc...) (Potential).
CARBOHYD 883 883 N-linked (GlcNAc...) (Potential).
CARBOHYD 944 944 N-linked (GlcNAc...) (Potential).
CARBOHYD 1005 1005 N-linked (GlcNAc...) (Potential).
CARBOHYD 1390 1390 N-linked (GlcNAc...) (Potential).
CARBOHYD 1448 1448 N-linked (GlcNAc...) (Potential).
DISULFID 48 86 By similarity.
DISULFID 249 298 By similarity.
DISULFID 267 286 By similarity.
DISULFID 277 277 Interchain (with C-430) (By similarity).
DISULFID 430 430 Interchain (with C-277) (By similarity).
DISULFID 469 562 By similarity.
DISULFID 594 785 By similarity.
DISULFID 642 689 By similarity.
DISULFID 835 863 By similarity.
DISULFID 861 897 By similarity.
DISULFID 935 1344 By similarity.
DISULFID 1094 1142 By similarity.
CROSSLNK 986 989 Isoglutamyl cysteine thioester (Cys-Gln) |
Keyword | 3D-structure; Bait region; Complete proteome; Direct protein sequencing; Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome; Secreted; Serine protease inhibitor; Signal; Thioester bond. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1500 AA |
Protein Sequence | MRRNQLPIPV FLLLLLLLPR DATAATGKPR YVVLVPSELY AGVPEKVCVH LNHLNETVTL 60
NVTLEYGVQY SNLLIDQAVD KDSSYCSSFT ISRPLSPSAL IAVEIKGPTH HFIKKKSMWI 120
TKAESPVFVQ TDKPIYKPGQ TVKFRVVSVD ISFRPVNETF PVVYIENPKR NRIFQWQNVD 180
LPGGLHQLSF PLSVEPALGI YKVVVQKDSG KKIEHSFEVK EYVLPKFEVQ VKMPKTMAFL 240
EEELVVTACG LYTYGKPVPG LVTMKVCRKY TQSYSNCHGQ HSKSICEEFS KQADEKGCFR 300
QVVKTKVFQP RQKGYDMKIE VEAKIKEDGT GIELTGTGSC EIANTLSKLK FTKANTFYRP 360
GLPFFGQVLL VDEKGQPIPN KNLTVQVNSV RSQFTFTTDE HGLANILIDT TNFTFSFMGI 420
RVIYKQNNIC FDNWWVDEYH TQADHSAARI FSPSRSYIQL ELVLGTLACG QTQEIRIHFL 480
LNEDALKDAK DLTFYYLIKA RGSIFNSGSH VLPLEQGKVK GVVSFPIRVE PGMAPVAKLI 540
VYTILPNEEL IADVQKFDIE KCFANTVNLS FPSAQSLPAS DTHLTVKATP LSLCALTAVD 600
QSVLLLKPEA KLSPQSIYNL LPQKAEQGAY LGPLPYKGGE NCIKAEDITH NGIVYTPKQD 660
LNDNDAYSVF QSIGLKIFTN TRVHKPRYCP MYQAYPPLPY VGEPQALAMS AIPGAGYRSS 720
NIRTSSMMMM GASEVAQEVE VRETVRKYFP ETWIWDMVPL DLSGDGELPV KVPDTITEWK 780
ASAFCLSGTT GLGLSSTISH KVFQPFFLEL TLPYSVVRGE AFILKATVLN YMPHCIRIHV 840
SLEMSPDFLA VPVGSHEDSH CICGNERKTV SWAVTPKSLG EVNFTATAEA LQSPELCGNK 900
VAEVPALVQK DTVVKPVIVE PEGIEKEQTY NTLLCPQDAE LQENWTLDLP ANVVEGSARA 960
TQSVLGDILG SAMQNLQNLL QMPYGCGEQN MVLFVPNIYV LEYLNETQQL TEAIKSKAIS 1020
YLISGYQRQL NYQHSDGSYS TFGDRGMRHS QGNTWLTAFV LKAFAQAQSY IYIEKTHITN 1080
AFNWLSMKQR ENGCFQQSGS LLNNAMKGGV DDEVTLSAYI TIALLEMPLP VTHSVVRNAL 1140
FCLETAWASI SNSQESHVYT KALLAYAFAL AGNRAKRSEV LESLNKDAVN EEESVHWQRP 1200
KNVEENVREM RSFSYKPRAP SAEVEMTAYV LLAYLTSASS RPTRDLSSSD LTTASKIVKW 1260
ISKQQNSHGG FSSTQDTVVA LQALSKYGAA TFTKSNKEVS VTIESSGTVS GTLHVNNGNR 1320
LLLQEVRLAD LPGNYITKVS GSGCVYLQTS LKYNILPEAE GEAPFTLKVN TLPLNFDKAE 1380
HHRKFQIHIN VSYIGERPNS NMVIVDVKMV SGFIPVKPSV KKLQDQSNIQ RTEVNTNHVL 1440
IYIEKLTNQT MGFSFAVEQD IPVKNLKPAP VKVYDYYETD EFAIEEYSAP FSSDSEQGNA 1500 |
Gene Ontology | GO:0005615; C:extracellular space; IEA:InterPro. GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW. GO:0010951; P:negative regulation of endopeptidase activity; IEA:GOC. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |