P32261

PR
Gene name
Serpinc1 (At3)
Protein name
Antithrombin-III
Names
ATIII, Serpin C1
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:11905
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

27-104 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for P32261

Entry ID Method Resolution Chain Position Source
AF-P32261-F1 Predicted AlphaFoldDB

41 variants for P32261

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388511151 18 L>H No EVA
rs238171425 28 G>A No EVA
rs3388511804 30 A>T No EVA
rs3413058601 41 C>S No EVA
rs3388511386 48 I>L No EVA
rs3388509852 50 V>M No EVA
rs3388511771 51 N>T No EVA
rs3388511218 52 P>H No EVA
rs3388510778 75 E>D No EVA
rs3388509817 79 R>L No EVA
rs3388508585 86 K>N No EVA
rs3388508396 89 S>L No EVA
rs13460842 91 F>L No EVA
rs3388511421 122 M>K No EVA
rs3388508366 128 C>Y No EVA
rs3388510787 129 N>K No EVA
rs3388509436 135 L>Q No EVA
rs3388506998 136 M>R No EVA
rs3388509447 142 D>V No EVA
rs3413145644 150 D>Y No EVA
rs3388507012 154 F>L No EVA
rs227108953 172 D>N No EVA
rs3388512922 174 V>I No EVA
rs3388511345 214 Q>R No EVA
rs3388508165 259 K>* No EVA
rs3388512965 261 K>N No EVA
rs3388510418 269 K>M No EVA
rs261982908 271 P>S No EVA
rs3388508572 305 L>M No EVA
rs233796502 347 T>I No EVA
rs3388509786 361 G>D No EVA
rs3388511370 368 L>M No EVA
rs13460840 371 M>T No EVA
rs49991990 376 L>I No EVA
rs3388506037 383 Q>K No EVA
rs3388509778 413 S>C No EVA
rs3388509850 413 S>N No EVA
rs3388508347 417 A>V No EVA
rs3388507074 419 T>I No EVA
rs3388509871 450 L>P No EVA
rs3388511742 455 F>I No EVA

No associated diseases with P32261

3 regional properties for P32261

Type Name Position InterPro Accession
conserved_site Serpin, conserved site 435 - 445 IPR023795
domain Serpin domain 87 - 462 IPR023796
domain Antithrombin-III, serpin domain 71 - 464 IPR033829

Functions

Description
EC Number
Subcellular Localization
  • Secreted, extracellular space
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
collagen-containing extracellular matrix An extracellular matrix consisting mainly of proteins (especially collagen) and glycosaminoglycans (mostly as proteoglycans) that provides not only essential physical scaffolding for the cellular constituents but can also initiate crucial biochemical and biomechanical cues required for tissue morphogenesis, differentiation and homeostasis. The components are secreted by cells in the vicinity and form a sheet underlying or overlying cells such as endothelial and epithelial cells.
extracellular space That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.

4 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.
identical protein binding Binding to an identical protein or proteins.
protease binding Binding to a protease or a peptidase.
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.

4 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.
negative regulation of endopeptidase activity Any process that decreases the frequency, rate or extent of endopeptidase activity, the endohydrolysis of peptide bonds within proteins.
regulation of blood coagulation, intrinsic pathway Any process that modulates the frequency, rate or extent of blood coagulation, intrinsic pathway.
response to nutrient Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a nutrient stimulus.

35 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9N2I2 SERPINA5 Plasma serine protease inhibitor Bos taurus (Bovine) PR
A6QPQ2 SERPINA3-8 Serpin A3-8 Bos taurus (Bovine) PR
A2I7N1 SERPINA3-5 Serpin A3-5 Bos taurus (Bovine) PR
Q1JPB0 SERPINB1 Leukocyte elastase inhibitor Bos taurus (Bovine) PR
P13909 SERPINE1 Plasminogen activator inhibitor 1 Bos taurus (Bovine) PR
Q9TTE1 SERPINA3-1 Serpin A3-1 Bos taurus (Bovine) PR
P41361 SERPINC1 Antithrombin-III Bos taurus (Bovine) PR
O73790 SERPINB10 Heterochromatin-associated protein MENT Gallus gallus (Chicken) PR
P05121 SERPINE1 Plasminogen activator inhibitor 1 Homo sapiens (Human) PR
Q9UK55 SERPINA10 Protein Z-dependent protease inhibitor Homo sapiens (Human) PR
P05155 SERPING1 Plasma protease C1 inhibitor Homo sapiens (Human) PR
P08697 SERPINF2 Alpha-2-antiplasmin Homo sapiens (Human) PR
Q86WD7 SERPINA9 Serpin A9 Homo sapiens (Human) PR
P07093 SERPINE2 Glia-derived nexin Homo sapiens (Human) PR
Q96P15 SERPINB11 Serpin B11 Homo sapiens (Human) PR
P01011 SERPINA3 Alpha-1-antichymotrypsin Homo sapiens (Human) PR
P01008 SERPINC1 Antithrombin-III Homo sapiens (Human) PR
P12388 Serpinb2 Plasminogen activator inhibitor 2, macrophage Mus musculus (Mouse) PR
Q07235 Serpine2 Glia-derived nexin Mus musculus (Mouse) PR
Q5SV42 Serpinb1c Leukocyte elastase inhibitor C Mus musculus (Mouse) PR
Q80X76 Serpina3f Serine protease inhibitor A3F Mus musculus (Mouse) PR
Q8BYY9 Serpina3b Serine protease inhibitor A3B Mus musculus (Mouse) PR
Q9D154 Serpinb1a Leukocyte elastase inhibitor A Mus musculus (Mouse) PR
Q9JK88 Serpini2 Serpin I2 Mus musculus (Mouse) PR
Q8CDC0 Serpinb13 Serpin B13 Mus musculus (Mouse) PR
P22777 Serpine1 Plasminogen activator inhibitor 1 Mus musculus (Mouse) PR
Q5I2A0 Serpina3g Serine protease inhibitor A3G Mus musculus (Mouse) PR
P29524 Serpinb2 Plasminogen activator inhibitor 2 type A Rattus norvegicus (Rat) PR
Q6P734 Serping1 Plasma protease C1 inhibitor Rattus norvegicus (Rat) PR
P05545 Serpina3k Serine protease inhibitor A3K Rattus norvegicus (Rat) PR
P07092 Serpine2 Glia-derived nexin Rattus norvegicus (Rat) PR
Q62975 Serpina10 Protein Z-dependent protease inhibitor Rattus norvegicus (Rat) PR
O48706 At2g26390 Serpin-Z3 Arabidopsis thaliana (Mouse-ear cress) PR
Q9M1T7 At3g45220 Serpin-Z4 Arabidopsis thaliana (Mouse-ear cress) PR
Q9ZQR6 At2g14540 Serpin-Z2 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MYSPGAGSGA AGERKLCLLS LLLIGALGCA ICHGNPVDDI CIAKPRDIPV NPLCIYRSPG
70 80 90 100 110 120
KKATEEDGSE QKVPEATNRR VWELSKANSR FATNFYQHLA DSKNDNDNIF LSPLSISTAF
130 140 150 160 170 180
AMTKLGACND TLKQLMEVFK FDTISEKTSD QIHFFFAKLN CRLYRKANKS SDLVSANRLF
190 200 210 220 230 240
GDKSLTFNES YQDVSEVVYG AKLQPLDFKE NPEQSRVTIN NWVANKTEGR IKDVIPQGAI
250 260 270 280 290 300
NELTALVLVN TIYFKGLWKS KFSPENTRKE PFYKVDGQSC PVPMMYQEGK FKYRRVAEGT
310 320 330 340 350 360
QVLELPFKGD DITMVLILPK PEKSLAKVEQ ELTPELLQEW LDELSETMLV VHMPRFRTED
370 380 390 400 410 420
GFSLKEQLQD MGLIDLFSPE KSQLPGIVAG GRDDLYVSDA FHKAFLEVNE EGSEAAASTS
430 440 450 460
VVITGRSLNP NRVTFKANRP FLVLIREVAL NTIIFMGRVA NPCVN