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 Q83KI8

Entry ID Method Resolution Chain Position Source
AF-Q83KI8-F1 Predicted AlphaFoldDB

No variants for Q83KI8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q83KI8

No associated diseases with Q83KI8

4 regional properties for Q83KI8

Type Name Position InterPro Accession
domain CBS domain 302 - 366 IPR000644-1
domain CBS domain 371 - 429 IPR000644-2
domain Transporter-associated domain 439 - 518 IPR005170
domain Ion transporter-like, CBS domain 301 - 419 IPR044751

Functions

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

2 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.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

1 GO annotations of molecular function

Name Definition
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MEWIADPSIW AGLITLIVIE LVLGIDNLVF IAILAEKLPP KQRDRARVTG LLLAMLMRLL
70 80 90 100 110 120
LLASISWLVT LTQPLFSFRS FTFSARDLIM LFGGFFLLFK ATMELNERLE GKDSNNPTQR
130 140 150 160 170 180
KGAKFWGVVT QIVVLDAIFS LDSVITAVGM VDHLLVMMAA VVIAISLMLM ASKPLTQFVN
190 200 210 220 230 240
SHPTIVILCL SFLLMIGFSL VAEGFGFVIP KGYLYAAIGF SVMIEALNQL AIFNRRRFLS
250 260 270 280 290 300
ANQTLRQRTT EAVMRLLSGQ KEDAELDAKT ASMLVDHGNQ QIFNPQERRM IERVLNLNQR
310 320 330 340 350 360
TVSSIMTSRH DIEHIDLNAP EEEIRQLLER NQHTRLVVTD GDDAEDLLGV VHVIDLLQQS
370 380 390 400 410 420
LRGEPLNLRV LIRQPLVFPE TLPLLPALEQ FRNARTHFAF VVDEFGSVEG IVTLSDVTET
430 440 450 460 470 480
IAGNLPNEVE EIDARHDIQK NADGSWTANG HMPLEDLVQY VPLPLDEKRE YHTIAGLLME
490 500 510 520
YLQRIPKPGE EVQVGDYLLK TLQVESHRVQ KVQIIPLRKD GEMEYEV