Q5R5J1

PR
Gene name
PCK1
Protein name
Phosphoenolpyruvate carboxykinase, cytosolic [GTP]
Names
PEPCK-C, Serine-protein kinase PCK1
Species
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
KEGG Pathway
pon:100173760
EC number
4.1.1.32: Carboxy-lyases
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-46 (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 Q5R5J1

Entry ID Method Resolution Chain Position Source
AF-Q5R5J1-F1 Predicted AlphaFoldDB

No variants for Q5R5J1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5R5J1

No associated diseases with Q5R5J1

3 regional properties for Q5R5J1

Type Name Position InterPro Accession
conserved_site Phosphoenolpyruvate carboxykinase, GTP-utilising, conserved site 284 - 292 IPR018091
domain Phosphoenolpyruvate carboxykinase, C-terminal P-loop domain 260 - 618 IPR035077
domain Phosphoenolpyruvate carboxykinase, GTP-utilising, N-terminal 29 - 256 IPR035078

Functions

Description
EC Number 4.1.1.32 Carboxy-lyases
Subcellular Localization
  • Cytoplasm, cytosol
  • Endoplasmic reticulum
  • Phosphorylation at Ser-90 promotes translocation to the endoplasmic reticulum
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 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.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).

4 GO annotations of molecular function

Name Definition
GTP binding Binding to GTP, guanosine triphosphate.
metal ion binding Binding to a metal ion.
phosphoenolpyruvate carboxykinase (GTP) activity Catalysis of the reaction: GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO2.
protein serine kinase activity (using GTP as donor) Catalysis of the reactions: GTP + L-seryl- = GDP + H(+) + O-phospho-L-seryl-

7 GO annotations of biological process

Name Definition
cellular response to glucose stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a glucose stimulus.
cellular response to insulin stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
gluconeogenesis The formation of glucose from noncarbohydrate precursors, such as pyruvate, amino acids and glycerol.
oxaloacetate metabolic process The chemical reactions and pathways involving oxaloacetate, the anion of oxobutanedioic acid, an important intermediate in metabolism, especially as a component of the TCA cycle.
peptidyl-serine phosphorylation The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine.
positive regulation of memory T cell differentiation Any process that activates or increases the frequency, rate or extent of memory T cell differentiation.
regulation of lipid biosynthetic process Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of lipids.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MPPQLQNGLN LSAKVVQGSL DSLPQAVRKF LENNAELCQP DHIHICDGSE EENGRLLGQM
70 80 90 100 110 120
EEEGILRRLK KYDNCWLALT DPRDVARIGS KTVIVTQEQR DTVPIPKTGL SQLGRWMSEE
130 140 150 160 170 180
DFEKALNARF PGCMKGRTMY VIPFSMGPLG SPLSKIGIEL TDSPYVVASM RIMTRMGTPV
190 200 210 220 230 240
LEALGDGEFV KCLHSVGCPL PLQKPLVNNW PCNPELTLIA HLPDRREIIS FGSGYGGNSL
250 260 270 280 290 300
LGKKCFALRM ASRLAKEEGW LAEHMLILGI TNPEGEKKYL AAAFPSACGK TNLAMMNPSL
310 320 330 340 350 360
PGWKVECVGD DIAWMKFDAQ GHLRAINPEN GFFGVAPGTS VKTNPNAIKT IQKNTIFTNV
370 380 390 400 410 420
AETSDGGVYW EGIDEPLASG VTITSWKNKE WSPEDGEPCA HPNSRFCTPA SQCPIIDAAW
430 440 450 460 470 480
ESPEGVPIEG IIFGGRRPAG VPLVYEALSW QHGVFVGAAM RSEATAAAEH KGKIIMHDPF
490 500 510 520 530 540
AMRPFFGYNF GKYLAHWLSM AQHPAAKLPK IFHVNWFRKD KEGKFLWPGF GENSRVLEWM
550 560 570 580 590 600
FNRIDGKAGA KLTPIGYIPK EDALNLKGLG HINVMELFSI SKEFWEKEVE DIEKYLEDQV
610 620
NADLPCEIER EILALKQRIS QM