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 O09043

Entry ID Method Resolution Chain Position Source
AF-O09043-F1 Predicted AlphaFoldDB

22 variants for O09043

Variant ID(s) Position Change Description Diseaes Association Provenance
rs260907547 4 L>P No EVA
rs239105084 36 R>S No EVA
rs3388907015 42 N>K No EVA
rs260190239 47 L>V No EVA
rs3388867010 57 G>D No EVA
rs3388866979 61 S>A No EVA
rs3388907072 81 T>M No EVA
rs3388907002 96 N>Y No EVA
rs3388904530 99 V>A No EVA
rs16785952 127 P>T No EVA
rs16785953 134 I>V No EVA
rs16785954 151 T>N No EVA
rs3388897016 153 G>V No EVA
rs16785967 222 G>V No EVA
rs16785968 243 T>I No EVA
rs3388906511 309 F>L No EVA
rs16793446 324 H>R No EVA
rs3388907042 355 A>V No EVA
rs217999864 375 P>S No EVA
rs3388904526 382 R>C No EVA
rs31476421 400 S>A No EVA
rs3388899211 403 R>W No EVA

No associated diseases with O09043

3 regional properties for O09043

Type Name Position InterPro Accession
active_site Aspartic peptidase, active site 88 - 99 IPR001969-1
active_site Aspartic peptidase, active site 275 - 286 IPR001969-2
domain Peptidase family A1 domain 72 - 394 IPR033121

Functions

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

3 GO annotations of cellular component

Name Definition
alveolar lamellar body A specialized secretory organelle found in type II pneumocytes and involved in the synthesis, secretion, and reutilization of pulmonary surfactant.
extracellular space That part of a multicellular organism outside the cells proper, usually taken to be outside the plasma membranes, and occupied by fluid.
lysosome A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions.

3 GO annotations of molecular function

Name Definition
aspartic-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which a water molecule bound by the side chains of aspartic residues at the active center acts as a nucleophile.
endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain.
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.

3 GO annotations of biological process

Name Definition
membrane protein proteolysis The proteolytic cleavage of a transmembrane protein leading to the release of its intracellular or ecto-domains.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
surfactant homeostasis Any process involved in the maintenance of a steady-state level of the surface-active lipoprotein mixture which coats the alveoli.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q29078 Pregnancy-associated glycoprotein 1 Sus scrofa (Pig) PR
P08424 Ren1 Renin Rattus norvegicus (Rat) PR
Q9XEC4 APA3 Aspartic proteinase A3 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MSPLLLLLLC LLLGNLEPEE AKLIRVPLQR IHLGHRILNP LNGWEQLAEL SRTSTSGGNP
70 80 90 100 110 120
SFVPLSKFMN TQYFGTIGLG TPPQNFTVVF DTGSSNLWVP STRCHFFSLA CWFHHRFNPK
130 140 150 160 170 180
ASSSFRPNGT KFAIQYGTGR LSGILSQDNL TIGGIHDAFV TFGEALWEPS LIFALAHFDG
190 200 210 220 230 240
ILGLGFPTLA VGGVQPPLDA MVEQGLLEKP VFSFYLNRDS EGSDGGELVL GGSDPAHYVP
250 260 270 280 290 300
PLTFIPVTIP AYWQVHMESV KVGTGLSLCA QGCSAILDTG TSLITGPSEE IRALNKAIGG
310 320 330 340 350 360
YPFLNGQYFI QCSKTPTLPP VSFHLGGVWF NLTGQDYVIK ILQSDVGLCL LGFQALDIPK
370 380 390 400 410
PAGPLWILGD VFLGPYVAVF DRGDKNVGPR VGLARAQSRS TDRAERRTTQ AQFFKRRPG