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 Q8IS16

Entry ID Method Resolution Chain Position Source
AF-Q8IS16-F1 Predicted AlphaFoldDB

No variants for Q8IS16

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8IS16

No associated diseases with Q8IS16

1 regional properties for Q8IS16

Type Name Position InterPro Accession
domain Aminotransferase class V domain 160 - 280 IPR000192

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane
  • The Sca1 complex is recruited to the plasma membrane in a chemoattractant- and F-actin-dependent manner and is enriched at the leading edge of chemotaxing cells (PubMed:20493808)
  • Membrane localization of the Sca1 complex is regulated by scaA phosphorylation by PKB and PKB-related PKBR1 (PubMed:20493808)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
Ras guanyl-nucleotide exchange factor complex A protein complex which is capable of Ras guanyl-nucleotide exchange factor activity.

2 GO annotations of molecular function

Name Definition
guanyl-nucleotide exchange factor activity Stimulates the exchange of GDP to GTP on a signaling GTPase, changing its conformation to its active form. Guanine nucleotide exchange factors (GEFs) act by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP), which is more abundant in the cell under normal cellular physiological conditions.
protein kinase activator activity Binds to and increases the activity of a protein kinase, an enzyme which phosphorylates a protein.

6 GO annotations of biological process

Name Definition
activation of GTPase activity Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP.
aggregation involved in sorocarp development The process whose specific outcome is the progression of the aggregate over time, from its formation to the point when a slug is formed. Aggregate development begins in response to starvation and continues by the chemoattractant-mediated movement of cells toward each other. The aggregate is a multicellular structure that gives rise to the slug.
chemotaxis to cAMP The directed movement of a motile cell or organism in response to the presence of 3',5'-cAMP.
positive regulation of GTPase activity Any process that activates or increases the activity of a GTPase.
positive regulation of Ras protein signal transduction Any process that activates or increases the frequency, rate or extent of Ras protein signal transduction.
Ras protein signal transduction The series of molecular signals within the cell that are mediated by a member of the Ras superfamily of proteins switching to a GTP-bound active state.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSNTNINVQS STPKKSLGSS QYSLAGSSSS NLNNINNNNN NNNNNNNNST GQENSIDDSG
70 80 90 100 110 120
SSSFVNFPAS EWLSKAMHKH PDILELRERT RPITQVKSYS RNKRSSKTEA SHSINDTMLL
130 140 150 160 170 180
KLIMQYFHEE NLTTSLKKIQ EETKVQFTPN EVDKDSLENL LRIGIKDTNW FGPLEDIEDA
190 200 210 220 230 240
DPEVETYHSY ISEDSLNENG LEGEGNLIED RYDESQISRN PDGTIKAATF NRLLLWLIGN
250 260 270 280 290 300
FNGPDVNEFK KIFFLTYPSF TTAEAILNKF TQIYQLFDNI ESAQVICFIR FWIEQHPTDF
310 320 330 340 350 360
NEKLLAILNN FIEHQVAASH AKQLRAVINL KIENYKEARK EIKDPPEPKV PKNIFSPTLT
370 380 390 400 410 420
FDDIDEEEIA RQLCCIDFAL YELIKPSEFL IKGWTKPQYR NKAVNLLNMM RRFNDFTKWI
430 440 450 460 470 480
AASILNEQNS KGRSKLLGRF LKISEHLRAN NNFHSLMAIY GGINNTHVFR TKAIRKDLSR
490 500 510 520 530 540
QQQETYAELE KLFASENSFR NYRIAYKDAK PPCIPFLGIH LRDLAFVDES NPDRINNLLN
550 560 570 580 590 600
LNKRRVIWRV IVNTMRYQPI PYYFLKVHQI SLFLTELKTE SEQPQLTLDL SSHDTVLPSS
PSSK