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 O08984

Entry ID Method Resolution Chain Position Source
AF-O08984-F1 Predicted AlphaFoldDB

No variants for O08984

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O08984

No associated diseases with O08984

11 regional properties for O08984

Type Name Position InterPro Accession
domain C2 domain 402 - 524 IPR000008-1
domain C2 domain 560 - 693 IPR000008-2
domain Synaptotagmin 564 - 579 IPR001565-1
domain Synaptotagmin 579 - 592 IPR001565-2
domain Synaptotagmin 636 - 651 IPR001565-3
domain Synaptotagmin 656 - 666 IPR001565-4
domain Rab-binding domain 44 - 161 IPR010911
domain Zinc finger, FYVE-related 92 - 149 IPR017455
domain Rabphilin-3A, FYVE domain 92 - 172 IPR028698
domain FYVE-type zinc finger 49 - 161 IPR041282
domain Rabphilin/Doc2, first C2 domain 403 - 526 IPR047022

Functions

Description
EC Number 1.3.1.70 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
  • Nucleus inner membrane ; Multi-pass membrane protein
  • Nucleus
  • Cytoplasm
  • Endoplasmic reticulum membrane
  • Nucleus; nuclear rim
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

8 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
nuclear envelope The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).
nuclear inner membrane The inner, i.e. lumen-facing, lipid bilayer of the nuclear envelope.
nuclear membrane Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space.
nuclear pore A protein complex providing a discrete opening in the nuclear envelope of a eukaryotic cell, where the inner and outer nuclear membranes are joined.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

7 GO annotations of molecular function

Name Definition
chaperone binding Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.
chromo shadow domain binding Binding to a chromo shadow domain, a protein domain that is distantly related, and found in association with, the chromo domain.
delta14-sterol reductase activity Catalysis of the reaction: NADP+ + 4,4-dimethyl-5-alpha-cholesta-8,24-dien-3-beta-ol = NADPH + H+ + 4,4-dimethyl-5-alpha-cholesta-8,14,24-trien-3-beta-ol.
DNA binding Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid).
NADPH binding Binding to the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions.
nuclear localization sequence binding Binding to a nuclear localization sequence, a specific peptide sequence that acts as a signal to localize the protein within the nucleus.
oxidoreductase activity, acting on the CH-CH group of donors Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.

4 GO annotations of biological process

Name Definition
cholesterol biosynthetic process The chemical reactions and pathways resulting in the formation of cholesterol, cholest-5-en-3 beta-ol, the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.
mitotic cell cycle Progression through the phases of the mitotic cell cycle, the most common eukaryotic cell cycle, which canonically comprises four successive phases called G1, S, G2, and M and includes replication of the genome and the subsequent segregation of chromosomes into daughter cells. In some variant cell cycles nuclear replication or nuclear division may not be followed by cell division, or G1 and G2 phases may be absent.
neutrophil differentiation The process in which a myeloid precursor cell acquires the specialized features of a neutrophil.
sterol biosynthetic process The chemical reactions and pathways resulting in the formation of sterols, steroids with one or more hydroxyl groups and a hydrocarbon side-chain in the molecule.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P23913 LBR Delta(14)-sterol reductase LBR Gallus gallus (Chicken) PR
Q14739 LBR Delta(14)-sterol reductase LBR Homo sapiens (Human) PR
Q3U9G9 Lbr Delta(14)-sterol reductase LBR Mus musculus (Mouse) PR
10 20 30 40 50 60
MPGRKFADGE VVRGRWPGSS LYYEVEILSH DSTSQLYTVK YKDGTELELK ESDIKPLKSF
70 80 90 100 110 120
KQRKSGSTSS SPSRRRSSRS RSRSRSRSPG RAPKGSRRSV SASYQADAKE KEMRREILQV
130 140 150 160 170 180
KLTPLVLKPF ANSVSVYNGE PEHMEKSATP PKNKQERVIL STEDSYIATQ YSLRPRREEV
190 200 210 220 230 240
KPKHRVRGTN LVTRGPVPLG TFQVTTPQRR DLEFGGVPGA LLIMLGLPAC VFLLLLQCAQ
250 260 270 280 290 300
KDPGLLQFPP PLPALRELWE ARVCGVYLLW FFLQALFSLL PVGKVVEGTP LVDGRRLKYR
310 320 330 340 350 360
LNGLYAFILT SAAVGTAVFW DIELYYLYTH FLQFALAAIV FSVVLSVYLY ARSLKVPRDE
370 380 390 400 410 420
LSPASSGNAV YDFFIGRELN PRIGAFDLKF FCELRPGLIG WVVINLVMLL AEMKVQERSA
430 440 450 460 470 480
PSLAMTLVNS FQLLYVVDAL WFEEALLTTM DIIHDGFGFM LAFGDLVWVP FTYSLQAFYL
490 500 510 520 530 540
VNHPQDLSWP LTSVIIALKL CGYVIFRCAN SQKNAFRKNP TDPKLAHLKT IPTSTWKSLL
550 560 570 580 590 600
VSGWWGFVRH PNYLGDLIMA LAWSLPCGFN HILPYFYVIY FTALLIHREA RDEHQCRRKY
610
GLAWEKYCQR VPYRIFPYIY