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 P53121

Entry ID Method Resolution Chain Position Source
AF-P53121-F1 Predicted AlphaFoldDB

6 variants for P53121

Variant ID(s) Position Change Description Diseaes Association Provenance
s07-245769 17 I>V No SGRP
s07-246606 296 N>D No SGRP
s07-247671 651 A>P No SGRP
s07-247693 658 T>R No SGRP
s07-247754 678 F>L No SGRP
s07-247801 694 E>A No SGRP

No associated diseases with P53121

2 regional properties for P53121

Type Name Position InterPro Accession
domain TRP, C-terminal 172 - 602 IPR010308
domain ML-like domain 30 - 168 IPR032800

Functions

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

4 GO annotations of cellular component

Name Definition
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).
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.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

1 GO annotations of molecular function

Name Definition
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.

4 GO annotations of biological process

Name Definition
FAD transport The directed movement of flavin-adenine dinucleotide (FAD) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. 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.
fungal-type cell wall biogenesis A cellular process that results in the biosynthesis of constituent macromolecules, assembly, and arrangement of constituent parts of a fungal-type cell wall. The fungal-type cell wall contains beta-glucan and may contain chitin.
sphingolipid biosynthetic process The chemical reactions and pathways resulting in the formation of sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid).
transmembrane transport The process in which a solute is transported across a lipid bilayer, from one side of a membrane to the other.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q08967 FLC1 Flavin carrier protein 1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P39719 FLC2 Flavin carrier protein 2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
10 20 30 40 50 60
MRFLQVYKSS ALIGLIILLA SKVNLAEAKR KLVATSLVTC MENSQLSANS FDVVFNPDDR
70 80 90 100 110 120
SLHYDLDMST QIDSYIFADI DVYAYGFKII TKNVDLCSIN WKQFCPVHPG NIQIDSIEYI
130 140 150 160 170 180
SSEYVNEIPG IAYQVPDIDA YARVKITNNV SEYLACIQIY FSNGKTVSQI GVKWATAVVA
190 200 210 220 230 240
GIGLLLSAIL STFGNSTAAS HISANTMSLF LYFQSVVVVA MQHVHRVPPI AAAWAENLVW
250 260 270 280 290 300
SMGLIRISFM QRIFRWYVQS TGGTPSLYLT STSMSVLAQR SWQYLMELPL IKRATNVLYG
310 320 330 340 350 360
NANTLIFRGI KRLGYKMGIE NTSIVCTGFT FFVLCGYVLA GFIIVFKCCV ELATRLGWIQ
370 380 390 400 410 420
KARFWEFRKQ WRMILKGALL RYIYIGFVQL TILSFWEFTE RDSPAVIVIA CLFILLSCGL
430 440 450 460 470 480
MLWAAWRTVF FARRSVALYN NPAALLYGDE YVLHKYGFFY TMFNANHYWW NIVLLSYIFV
490 500 510 520 530 540
KSLLVGFAQA SGQTQVLFMF ILDLFYFVAI IYYKPYLDRP TNIMNILIAT VTVVNSFLFM
550 560 570 580 590 600
FFSDLFNQSY KVAAIMGWIF FIMNAAFSFI LLMMILAFAG MMLFSKNPDL RFKPAKDDRT
610 620 630 640 650 660
SFQRNTMKPE GTVNRSVANE LLALGNVAKD HDDNSDYESN DTGVNDELKQ AQDETTPTTV
670 680 690 700 710 720
TSSDDNKPTF SEKILSKFSR PKNENASTDA LRVEAPKQQT FPHNLTNLSR ENLSTLGSKP
730 740 750 760 770 780
YPGHTRSQSD AHNGLINSFE EEDTSSNTDP FHDSTEGDLL DTSSSDGGFR SQNYVRDDSI
790 800
NSLGNNKQPL RKPPGFFDEG FM