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 P9WFP2

Entry ID Method Resolution Chain Position Source
AF-P9WFP2-F1 Predicted AlphaFoldDB

No variants for P9WFP2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P9WFP2

No associated diseases with P9WFP2

5 regional properties for P9WFP2

Type Name Position InterPro Accession
domain CBS domain 221 - 285 IPR000644-1
domain CBS domain 286 - 346 IPR000644-2
domain CNNM, transmembrane domain 2 - 205 IPR002550
domain Transporter-associated domain 354 - 444 IPR005170
domain Ion transporter-like, CBS domain 219 - 337 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
MNLTDTVATI LAILALTAGT GVFVAAEFSL TALDRSTVEA NARGGTSRDR FIQRAHHRLS
70 80 90 100 110 120
FQLSGAQLGI SITTLATGYL TEPLVAELPH PGLVAVGMSD RVADGLITFF ALVIVTSLSM
130 140 150 160 170 180
VFGELVPKYL AVARPLRTAR SVVAGQVLFS LLLTPAIRLT NGAANWIVRR LGIEPAEELR
190 200 210 220 230 240
SARTPQELVS LVRSSARSGA LDDATAWLMR RSLQFGALTA EELMTPRSKI VALQTDDTIA
250 260 270 280 290 300
DLVAAAAASG FSRFPVVEGD LDATVGIVHV KQVFEVPPGD RAHTLLTTVA EPVAVVPSTL
310 320 330 340 350 360
DGDAVMAQVR ASALQTAMVV DEYGGTAGMV TLEDLIEEIV GDVRDEHDDA TPDVVAAGNG
370 380 390 400 410 420
WRVSGLLRID EVASATGYRA PDGPYETISG LVLRELGHIP VAGETVELTA LDQDGLPDDS
430 440 450
MRWLATVIQM DGRRIDLLEL IKMGGHADPG SGRGR