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

2 structures for A0R2I8

Entry ID Method Resolution Chain Position Source
2GRV X-ray 240 A A/B/C 28-627 PDB
AF-A0R2I8-F1 Predicted AlphaFoldDB

No variants for A0R2I8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A0R2I8

No associated diseases with A0R2I8

1 regional properties for A0R2I8

Type Name Position InterPro Accession
domain Solute-binding protein family 5 domain 111 - 478 IPR000914

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

3 GO annotations of biological process

Name Definition
glycolipid biosynthetic process The chemical reactions and pathways resulting in the formation of glycolipid, a class of 1,2-di-O-acylglycerols joined at oxygen 3 by a glycosidic linkage to a carbohydrate part (usually a mono-, di- or tri-saccharide).
phosphatidylinositol metabolic process The chemical reactions and pathways involving phosphatidylinositol, any glycophospholipid in which a sn-glycerol 3-phosphate residue is esterified to the 1-hydroxyl group of 1D-myo-inositol.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGVPTPARRA RLTFGALLAV PTLLLGGCTV SPPPAPQSTE TTETTPPPPP KAPTQIIMAI
70 80 90 100 110 120
DSIGPGFNPH LLSDQSPVNA AIASLVLPSS FRPVPDPTSP TGSRWELDTT LLESAEVTNE
130 140 150 160 170 180
NPFTVTYKIR PEAQWTDNAP IAADDYWYLW RQMVSQPGVV DPAGYDLITG VQSVEGGKQA
190 200 210 220 230 240
VVTFSQPYPA WRELFNDILP AHIVKDIPGG FGAGLARAMP VTGGQFRVET IDPQRDEILL
250 260 270 280 290 300
ARNDRFWSVP AKPDLVLFRR GGAPAALADS IRNGDTQVAQ VHGGAATFAQ LSAIPDVRTA
310 320 330 340 350 360
RIVTPRVMQL TLRAQQPKLA DPQVRKAILG LIDVDLLASV GAGDDNTVTL AQAQVRSPSD
370 380 390 400 410 420
PGYVPTAPPA MTRDDALELL RDAGYVSEPV PPPDNTADDP PPDNGRERIV KDGVPLTIVL
430 440 450 460 470 480
GVASNDPTSV AVANTAADQL RNVGIDASVL ALDPVALYGD ALVNNRVDAV VGWRQAGGDL
490 500 510 520 530 540
ATVLASRYGC RALEATPVAT AVPGPATTTS QAPTTTTTTT PPATTTPTPT APIPAPESGE
550 560 570 580 590 600
LVQAPSNITG ICDRSIQPRI DAALDGTDDI ADVIQAVEPR LWNMATVLPI LQDTTIVAAG
610 620
PSVQNVSLTG AVPVGIVGDA GDWTKTK