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 Q6P734

Entry ID Method Resolution Chain Position Source
AF-Q6P734-F1 Predicted AlphaFoldDB

1 variants for Q6P734

Variant ID(s) Position Change Description Diseaes Association Provenance
rs198579228 163 S>L No EVA

No associated diseases with Q6P734

2 regional properties for Q6P734

Type Name Position InterPro Accession
conserved_site Serpin, conserved site 475 - 485 IPR023795
domain Serpin domain 150 - 502 IPR023796

Functions

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

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
complement binding Binding to a component or product of the complement cascade.
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.

7 GO annotations of biological process

Name Definition
aging A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700).
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.
complement activation, classical pathway Any process involved in the activation of any of the steps of the classical pathway of the complement cascade which allows for the direct killing of microbes, the disposal of immune complexes, and the regulation of other immune processes.
fibrinolysis A process that solubilizes fibrin in the bloodstream of a multicellular organism, chiefly by the proteolytic action of plasmin.
innate immune response Innate immune responses are defense responses mediated by germline encoded components that directly recognize components of potential pathogens.
negative regulation of complement activation, lectin pathway Any process that stops, prevents, or reduces the rate of complement activation by the lectin pathway.
negative regulation of endopeptidase activity Any process that decreases the frequency, rate or extent of endopeptidase activity, the endohydrolysis of peptide bonds within proteins.

37 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9N2I2 SERPINA5 Plasma serine protease inhibitor Bos taurus (Bovine) PR
P41361 SERPINC1 Antithrombin-III 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
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
Q86WD7 SERPINA9 Serpin A9 Homo sapiens (Human) PR
P01008 SERPINC1 Antithrombin-III 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
P08697 SERPINF2 Alpha-2-antiplasmin Homo sapiens (Human) PR
P05155 SERPING1 Plasma protease C1 inhibitor Homo sapiens (Human) PR
Q5SV42 Serpinb1c Leukocyte elastase inhibitor C Mus musculus (Mouse) PR
Q07235 Serpine2 Glia-derived nexin 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
Q9JK88 Serpini2 Serpin I2 Mus musculus (Mouse) PR
P12388 Serpinb2 Plasminogen activator inhibitor 2, macrophage Mus musculus (Mouse) PR
P32261 Serpinc1 Antithrombin-III Mus musculus (Mouse) PR
Q9D154 Serpinb1a Leukocyte elastase inhibitor A Mus musculus (Mouse) PR
Q8BYY9 Serpina3b Serine protease inhibitor A3B Mus musculus (Mouse) PR
Q80X76 Serpina3f Serine protease inhibitor A3F Mus musculus (Mouse) PR
Q62975 Serpina10 Protein Z-dependent protease inhibitor Rattus norvegicus (Rat) PR
P29524 Serpinb2 Plasminogen activator inhibitor 2 type A Rattus norvegicus (Rat) PR
P05545 Serpina3k Serine protease inhibitor A3K Rattus norvegicus (Rat) PR
P07092 Serpine2 Glia-derived nexin Rattus norvegicus (Rat) PR
P05544 Serpina3l Serine protease inhibitor A3L Rattus norvegicus (Rat) PR
P09005 Serine protease inhibitor 2.1 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
MASKLTPLTL LLLLLAGDRA FSDSEVTSHS SQDPLVVQEG SRDSVPERDG SRSPIEHTGQ
70 80 90 100 110 120
SSTWPTTSGS TKISNDTMDQ VANESFIQHV QPAAQLPEDS PSQSPVNSSS PPSTASAPPT
130 140 150 160 170 180
QAPTEPLCPE PLAWCSDSDR DSSEATLSEA LTDFSVKLYH AFSATKKAET NMAFSPFSIA
190 200 210 220 230 240
SLLTQVLLGA GDSTKSNLED ILSYPKDFAC VHQTLKAFSS KGVTSVSQIF HSPDLAIRDT
250 260 270 280 290 300
YVNASLSLYG SSPRVLGPDG DANLKLINTW VAENTNHKIN ELLDSLPSDT RLVLLNAVYL
310 320 330 340 350 360
SAKWKKTFEQ KKMMASFLYK NSMIKVPMLS SKKYPLALFN DQTLKAKVGQ LQLSHNLSFV
370 380 390 400 410 420
IMVPQSPTHQ LEDMEKALNP TVFKAILKKL ELSKFQPTYV MMPRIKVKSS QDMLSIMEKL
430 440 450 460 470 480
EFFDFTYDLN LCGLTEDPDL QVSSMKHETV LELTETGVEA AAASTISVAR NLLIFEVQQP
490 500
FLFLLWDQRH KFPVFMGRVY DPRA