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

4 structures for P12799

Entry ID Method Resolution Chain Position Source
1DEQ X-ray 350 A C/F/P/S 25-432 PDB
1JY2 X-ray 140 A P/S 25-72 PDB
1JY3 X-ray 160 A P/S 25-72 PDB
AF-P12799-F1 Predicted AlphaFoldDB

No variants for P12799

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P12799

No associated diseases with P12799

2 regional properties for P12799

Type Name Position InterPro Accession
domain Activity-regulated cytoskeleton-associated protein, C-terminal domain 278 - 359 IPR040814
domain Activity-regulated cytoskeleton-associated protein, N-terminal domain 46 - 154 IPR045557

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
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.
fibrinogen complex A highly soluble, elongated protein complex found in blood plasma and involved in clot formation. It is converted into fibrin monomer by the action of thrombin. In the mouse, fibrinogen is a hexamer, 46 nm long and 9 nm maximal diameter, containing two sets of nonidentical chains (alpha, beta, and gamma) linked together by disulfide bonds.

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
signaling receptor binding Binding to one or more specific sites on a receptor molecule, a macromolecule that undergoes combination with a hormone, neurotransmitter, drug or intracellular messenger to initiate a change in cell function.

4 GO annotations of biological process

Name Definition
blood coagulation, fibrin clot formation A protein activation cascade that contributes to blood coagulation and consists of the cascade of enzymatic reactions initiated by physical damage to the wall of a blood vessel, leading to the formation of a formation of a fibrin clot at the site of the injury. The process also includes numerous positive and negative regulatory events.
cell-matrix adhesion The binding of a cell to the extracellular matrix via adhesion molecules.
platelet aggregation The adhesion of one platelet to one or more other platelets via adhesion molecules.
protein polymerization The process of creating protein polymers, compounds composed of a large number of component monomers; polymeric proteins may be made up of different or identical monomers. Polymerization occurs by the addition of extra monomers to an existing poly- or oligomeric protein.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q86XS5 ANGPTL5 Angiopoietin-related protein 5 Homo sapiens (Human) PR
P06399 Fga Fibrinogen alpha chain Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MSWSSHPPSV IFYILSLLSS ACLAYVATRD NCCILDERFG SYCPTTCGIA DFLNNYQTSV
70 80 90 100 110 120
DKDLRTLEGI LYQVENKTSE ARELVKAIQI SYNPDQPSKP NNIESATKNS KSMMEEIMKY
130 140 150 160 170 180
ETLISTHEST IRFLQEVYNS NSQKIVNLRD KVVQLEANCQ EPCQDTVKIH DVTGRDCQDV
190 200 210 220 230 240
ANKGAKESGL YFIRPLKAKQ FLVYCEIDGS GNGWTVFQKR LDGSLDFKKN WIQYKEGFGH
250 260 270 280 290 300
LSPTGTGNTE FWLGNEKIHL ISTQSSIPYV LRIQLEDWNG RTSTADYASF KVTGENDKYR
310 320 330 340 350 360
LTYAYFIGGD AGDAFDGYDF GDDSSDKFFT SHNGMQFSTW DSDNDKYDGN CAEQVGIGWW
370 380 390 400 410 420
MNKCHAGHLN GVYYQGGTYS KTSTPNGYDN GIIWATWKSR WYSMKKTTMK IIPLNRLAIG
430 440
EGQQHQLGGA KQVGVEHHVE IEYD