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 P76352

Entry ID Method Resolution Chain Position Source
AF-P76352-F1 Predicted AlphaFoldDB

No variants for P76352

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P76352

No associated diseases with P76352

No regional properties for P76352

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P76352

Functions

Description
EC Number
Subcellular Localization
  • Cell inner membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
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.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

5 GO annotations of molecular function

Name Definition
antiporter activity Enables the active transport of a solute across a membrane by a mechanism whereby two or more species are transported in opposite directions in a tightly coupled process not directly linked to a form of energy other than chemiosmotic energy. The reaction is: solute A(out) + solute B(in) = solute A(in) + solute B(out).
dipeptide transmembrane transporter activity Enables the transfer of a dipeptide from one side of a membrane to the other. A dipeptide is a combination of two amino acids linked together by a peptide (-CO-NH-) bond.
FAD transmembrane transporter activity Enables the directed movement of flavin-adenine dinucleotide (FAD) from one side of a membrane to the other. FAD forms the coenzyme of the prosthetic group of various flavoprotein oxidoreductase enzymes, in which it functions as an electron acceptor by being reversibly converted to its reduced form.
FMN transmembrane transporter activity Enables the directed movement of flavine mononucleotide (FMN) from one side of a membrane to the other.
xenobiotic transmembrane transporter activity Enables the directed movement of a xenobiotic from one side of a membrane to the other. A xenobiotic is a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.

3 GO annotations of biological process

Name Definition
dipeptide transmembrane transport The directed movement of a dipeptide across a membrane by means of some agent such as a transporter or pore. A dipeptide is a combination of two amino acids linked together by a peptide (-CO-NH-) bond.
FAD transmembrane transport The process in which flavin-adenine dinucleotide (FAD) is transported across a membrane. FAD forms the coenzyme of the prosthetic group of various flavoprotein oxidoreductase enzymes, in which it functions as an electron acceptor by being reversibly converted to its reduced form.
protein transport The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MLRHILTAKN LLSNPIFKFP NCLPFLSTVC CICRQFVGEN LCSFADSPSL FEMWFHFLQL
70 80 90 100 110 120
RSALNISSAL RQVVHGTRWH AKRKSYKVLF WREITPLAVP IFMENACVLL MGVLSTFLVS
130 140 150 160 170 180
WLGKDAMAGV GLADSFNMVI MAFFAAIDLG TTVVVAFSLG KRDRRRARVA TRQSLVIMTL
190 200 210 220 230 240
FAVLLATLIH HFGEQIIDFV AGDATTEVKA LALTYLELTV LSYPAAAITL IGSGALRGAG
250 260 270 280 290 300
NTKIPLLING SLNILNIIIS GILIYGLFSW PGLGFVGAGL GLTISRYIGA VAILWVLAIG
310 320 330 340 350 360
FNPALRISLK SYFKPLNFSI IWEVMGIGIP ASVESVLFTS GRLLTQMFVA GMGTSVIAGN
370 380 390 400 410 420
FIAFSIAALI NLPGSALGSA STIITGRRLG VGQIAQAEIQ LRHVFWLSTL GLTAIAWLTA
430 440 450 460 470 480
PFAGVMASFY TQDPQVKHVV VILIWLNALF MPIWSASWVL PAGFKGARDA RYAMWVSMLS
490 500 510 520 530 540
MWGCRVVVGY VLGIMLGWGV VGVWMGMFAD WAVRAVLFYW RMVTGRWLWK YPRPEPQKCE
KKPVVSE