Q8CHN8
PR
Gene name |
Masp1 (Crarf, Masp3) |
Protein name |
Mannan-binding lectin serine protease 1 |
Names |
Complement factor MASP-3, Complement-activating component of Ra-reactive factor, Mannose-binding lectin-associated serine protease 1, MASP-1, Mannose-binding protein-associated serine protease, Ra-reactive factor serine protease p100, RaRF, Serine protease 5 |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:64023 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
8 structures for Q8CHN8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3POB | X-ray | 180 A | A | 188-301 | PDB |
| 3POE | X-ray | 150 A | A | 188-301 | PDB |
| 3POF | X-ray | 150 A | A/B | 188-301 | PDB |
| 3POG | X-ray | 275 A | A/B/C | 188-301 | PDB |
| 3POI | X-ray | 170 A | A/B | 188-301 | PDB |
| 3POJ | X-ray | 145 A | A/B | 188-301 | PDB |
| 5CKQ | X-ray | 370 A | A | 25-301 | PDB |
| AF-Q8CHN8-F1 | Predicted | AlphaFoldDB |
1 variants for Q8CHN8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs8154756 | 232 | Q>H | No | EVA |
No associated diseases with Q8CHN8
10 regional properties for Q8CHN8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Sushi/SCR/CCP domain | 304 - 369 | IPR000436-1 |
| domain | Sushi/SCR/CCP domain | 370 - 439 | IPR000436-2 |
| domain | EGF-like domain | 171 - 186 | IPR000742 |
| domain | CUB domain | 16 - 143 | IPR000859-1 |
| domain | CUB domain | 190 - 302 | IPR000859-2 |
| domain | Serine proteases, trypsin domain | 453 - 701 | IPR001254 |
| domain | EGF-like calcium-binding domain | 144 - 187 | IPR001881 |
| conserved_site | EGF-like calcium-binding, conserved site | 144 - 171 | IPR018097 |
| active_site | Serine proteases, trypsin family, histidine active site | 491 - 496 | IPR018114 |
| active_site | Serine proteases, trypsin family, serine active site | 645 - 656 | IPR033116 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| extracellular space | That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid. |
| serine-type endopeptidase complex | A protein complex which is capable of serine-type endopeptidase activity. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| calcium ion binding | Binding to a calcium ion (Ca2+). |
| calcium-dependent protein binding | Binding to a protein or protein complex in the presence of calcium. |
| peptidase activity | Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
| serine-type endopeptidase activity | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| cell surface pattern recognition receptor signaling pathway | The series of molecular signals initiated by a ligand binding to a cell surface pattern recognition receptor (PRR). PRRs bind pathogen-associated molecular pattern (PAMPs), structures conserved among microbial species. |
| complement activation | Any process involved in the activation of any of the steps of the complement cascade, which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes; the initial steps of complement activation involve one of three pathways, the classical pathway, the alternative pathway, and the lectin pathway, all of which lead to the terminal complement pathway. |
| complement activation, lectin pathway | Any process involved in the activation of any of the steps of the lectin pathway of the complement cascade which allows for the direct killing of microbes and the regulation of other immune processes. |
| positive regulation of opsonization | Any process that activates or increases the frequency, rate or extent of opsonization. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
8 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P05049 | snk | Serine protease snake | Drosophila melanogaster (Fruit fly) | PR |
| Q6UWB4 | PRSS55 | Serine protease 55 | Homo sapiens (Human) | PR |
| P35030 | PRSS3 | Trypsin-3 | Homo sapiens (Human) | PR |
| Q9UI38 | PRSS50 | Probable threonine protease PRSS50 | Homo sapiens (Human) | PR |
| E5RG02 | PRSS46P | Putative serine protease 46 | Homo sapiens (Human) | PR |
| P0CW18 | PRSS56 | Serine protease 56 | Homo sapiens (Human) | PR |
| P98064 | Masp1 | Mannan-binding lectin serine protease 1 | Mus musculus (Mouse) | PR |
| Q6IE63 | Prss46 | Serine protease 46 | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRFLSFRRLL | LYHVLCLTLT | EVSAHTVELN | EMFGQIQSPG | YPDSYPSDSE | VTWNITVPEG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FRVQLYFMHF | NLESSYLCEY | DYVKVETEDQ | VLATFCGRET | TDTEQTPGQE | VVLSPGSFMS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VTFRSDFSNE | ERFTGFDAHY | MAVDVDECKE | REDEELSCDH | YCHNYIGGYY | CSCRFGYILH |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TDNRTCRVEC | SGNLFTQRTG | TITSPDYPNP | YPKSSECSYT | IDLEEGFMVT | LQFEDIFDIE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DHPEVPCPYD | YIKIKAGSKV | WGPFCGEKSP | EPISTQSHSI | QILFRSDNSG | ENRGWRLSYR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AAGNECPKLQ | PPVYGKIEPS | QAVYSFKDQV | LISCDTGYKV | LKDNEVMDTF | QIECLKDGAW |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SNKIPTCKIV | DCGVPAVLKH | GLVTFSTRNN | LTTYKSEIRY | SCQQPYYKML | HNTTGVYTCS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AHGTWTNEVL | KRSLPTCLPV | CGLPKFSRKH | ISRIFNGRPA | QKGTTPWIAM | LSQLNGQPFC |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GGSLLGSNWV | LTAAHCLHHP | LDPEEPILHN | SHLLSPSDFK | IIMGKHWRRR | SDEDEQHLHV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KHIMLHPLYN | PSTFENDLGL | VELSESPRLN | DFVMPVCLPE | HPSTEGTMVI | VSGWGKQFLQ |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RLPENLMEIE | IPIVNYHTCQ | EAYTPLGKKV | TQDMICAGEK | EGGKDACAGD | SGGPMVTKDA |
| 670 | 680 | 690 | 700 | ||
| ERDQWYLVGV | VSWGEDCGKK | DRYGVYSYIY | PNKDWIQRVT | GVRN |