Q5R5A3
Gene name |
SERPINC1 (AT3) |
Protein name |
Antithrombin-III |
Names |
ATIII, Serpin C1 |
Species |
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) |
KEGG Pathway |
pon:100173818 |
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
1 structures for Q5R5A3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5R5A3-F1 | Predicted | AlphaFoldDB |
No variants for Q5R5A3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5R5A3 | |||||
No associated diseases with Q5R5A3
1 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| heparin binding | Binding to heparin, a member of a group of glycosaminoglycans found mainly as an intracellular component of mast cells and which consist predominantly of alternating alpha-(1->4)-linked D-galactose and N-acetyl-D-glucosamine-6-sulfate residues. |
| serine-type endopeptidase inhibitor activity | Binds to and stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| blood coagulation | The sequential process in which the multiple coagulation factors of the blood interact, ultimately resulting in the formation of an insoluble fibrin clot; it may be divided into three stages: stage 1, the formation of intrinsic and extrinsic prothrombin converting principle; stage 2, the formation of thrombin; stage 3, the formation of stable fibrin polymers. |
| regulation of blood coagulation, intrinsic pathway | Any process that modulates the frequency, rate or extent of blood coagulation, intrinsic pathway. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MYSNVIGTIT | SGKRKVYLLS | LLLIGFWDCV | TCHGSPVDIC | IAKPRDIPMN | PMCIYRSPEK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KATEDEGSEQ | KIPEATNRRV | WELSKANSRF | ATTFYQHLAD | SKNDNDNIFL | SPLSISTAFA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MTKLGACNDT | LQQLMEVFKF | DTISEKTSDQ | IHFFFAKLNC | RLYRKANKSS | KLVSANRLFG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DKSLTFNETY | QDISELVYGA | KLQPLDFKEN | AEQSRAAINK | WVSNKTEGRI | TDVIPPEAIN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ELTVLVLVNT | IYFKGLWKSK | FSPENTRKEL | FYKADGESCS | ASMMYQEGKF | RYRRVAEGTQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VLELPFKGDD | ITMVLILPKP | EKSLAKVEKE | LTPEVLQEWL | DELEEMMLVV | HMPRFRIEDG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FSLKEQLQDM | GLVDLFSPEK | SKLPGIVAEG | RDDLYVSDAF | HKAFLEVNEE | GSEAAASTAV |
| 430 | 440 | 450 | 460 | ||
| VIAGRSLNPN | RVTFKANRPF | LVFIREVPLN | TIIFMGRVAN | PCVK |