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 Q10484

Entry ID Method Resolution Chain Position Source
AF-Q10484-F1 Predicted AlphaFoldDB

3 variants for Q10484

Variant ID(s) Position Change Description Diseaes Association Provenance
I_4479456_C_A 76 G>V No Jeffares_SNPs
I_4478955_G_A 216 P>L No Jeffares_SNPs
I_4478933_A_C 223 N>K No Jeffares_SNPs

No associated diseases with Q10484

1 regional properties for Q10484

Type Name Position InterPro Accession
domain Major sperm protein (MSP) domain 1 - 121 IPR000535

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum membrane ; Single-pass type IV membrane protein
  • Localizes at the cortical endoplasmic reticulum-plasma membrane contact sites
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
cortical endoplasmic reticulum A cortical network of highly dynamic tubules that are juxtaposed to the plasma membrane and undergo ring closure and tubule-branching movements.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of endoplasmic reticulum membrane The component of the endoplasmic reticulum 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.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

2 GO annotations of molecular function

Name Definition
FFAT motif binding Binding to a FFAT motif, a short motif containing diphenylalanine in an acidic tract that targets proteins to the cytosolic surface of the ER and to the nuclear membrane by binding directly to members of the VAP (VAMP-associated protein) protein family.
protein-membrane adaptor activity The binding activity of a molecule that brings together a protein or a protein complex with a membrane, or bringing together two membranes, either via membrane lipid binding or by interacting with a membrane protein, to establish or maintain the localization of the protein, protein complex or organelle.

5 GO annotations of biological process

Name Definition
endoplasmic reticulum membrane organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an endoplasmic reticulum membrane.
endoplasmic reticulum-plasma membrane tethering The attachment of an endoplasmic reticulum membrane to the plasma membrane via molecular tethers.
maintenance of ER location Any process in which the endoplasmic reticulum is maintained in a specific location within a cell and prevented from moving elsewhere.
phospholipid biosynthetic process The chemical reactions and pathways resulting in the formation of a phospholipid, a lipid containing phosphoric acid as a mono- or diester.
reticulophagy The selective autohagy process in which parts of the endoplasmic reticulum are loaded into autophagosomes, delivered to the vacuole, and degraded in response to changing cellular conditions.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MALECDSTIV FPRPLTRLVK CDLELRNTAP YPIGFKVKTT APKQYCVRPN GGRIEANSAV
70 80 90 100 110 120
SVEVILQPLD HEPAPGTKCR DKFLVQSTEL KPELQGMDIA DIWTQVSKAN ISERKIRCVY
130 140 150 160 170 180
SEGPSTANAH ANAHHQPAQT TTTSIPTSAT DNYTTVNGNV NQSYSKGIDG TALPSTHANP
190 200 210 220 230 240
VAAPSTATTQ HTQLPKTSAV SHQKPHEAPS TAVKAPTATV AENEPYPKPQ SVPTTTSPNN
250 260 270 280 290 300
ENNALRSTAN VINNTRQSTA TSPSMFAGNS GNQIGLARVS SSFGRPTSGA KVVPQIHNTV
310
TVQTAFLLAI ICFLIGLLF