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 A6QNK1

Entry ID Method Resolution Chain Position Source
AF-A6QNK1-F1 Predicted AlphaFoldDB

No variants for A6QNK1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A6QNK1

No associated diseases with A6QNK1

No regional properties for A6QNK1

Type Name Position InterPro Accession
No domain, repeats, and functional sites for A6QNK1

Functions

Description
EC Number 2.8.2.11 Sulfotransferases
Subcellular Localization
  • Golgi apparatus membrane ; Single-pass type II membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
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.

3 GO annotations of molecular function

Name Definition
galactose 3-O-sulfotransferase activity Catalysis of the reaction: N-acetyllactosamine + 3'-phosphoadenosine 5'-phosphosulfate = 3-sulfo-N-acetyllactosamine + adenosine 3',5'-bisphosphate. N-acetyllactosamine residues are found in a number of different carbohydrate types. N-acetyllactosamine can also be written as Gal-beta-(1,4)-GlcNAc.
galactosylceramide sulfotransferase activity Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + a galactosylceramide = adenosine 3',5'-bisphosphate + a galactosylceramidesulfate.
sulfotransferase activity Catalysis of the transfer of a sulfate group from 3'-phosphoadenosine 5'-phosphosulfate to the hydroxyl group of an acceptor, producing the sulfated derivative and 3'-phosphoadenosine 5'-phosphate.

5 GO annotations of biological process

Name Definition
galactosylceramide biosynthetic process The chemical reactions and pathways resulting in the formation of galactosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of galactose by a ceramide group.
galactosylceramide metabolic process The chemical reactions and pathways involving galactosylceramides, any compound formed by the replacement of the glycosidic hydroxyl group of a cyclic form of galactose by a ceramide group.
glycerolipid metabolic process The chemical reactions and pathways involving glycerolipids, any lipid with a glycerol backbone. Diacylglycerol and phosphatidate are key lipid intermediates of glycerolipid biosynthesis.
myelination The process in which myelin sheaths are formed and maintained around neurons. Oligodendrocytes in the brain and spinal cord and Schwann cells in the peripheral nervous system wrap axons with compact layers of their plasma membrane. Adjacent myelin segments are separated by a non-myelinated stretch of axon called a node of Ranvier.
sphingolipid metabolic process The chemical reactions and pathways involving sphingolipids, any of a class of lipids containing the long-chain amine diol sphingosine or a closely related base (a sphingoid).

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q99999 GAL3ST1 Galactosylceramide sulfotransferase Homo sapiens (Human) PR
Q9JHE4 Gal3st1 Galactosylceramide sulfotransferase Mus musculus (Mouse) PR
10 20 30 40 50 60
MPLPQKKRWE SMAKGLVLGA LFTSFLLLLY SYAVPPLYTG LASTTPEGAA PCSPAPREPE
70 80 90 100 110 120
APTSANGSAG GCQPRRDIVF MKTHKTASST LLNILFRFGQ KHGLKFAFPN GRNDFDYPAF
130 140 150 160 170 180
FARSLVQDYR PGACFNIICN HMRFHYDEVR GLVAPNATFI TVLRDPARLF ESSFHYFGSV
190 200 210 220 230 240
VPFTWKLSGR DKLAEFLQDP DRYYDARGYN AHYLRNLLFF DLGYDSDLDP SSPQVQEHIL
250 260 270 280 290 300
EVERHFHLVL LQEYFDESLV LLKDLLCWEL EDVLYFKLNA RRASAVPRLS GELYRRATAW
310 320 330 340 350 360
NVLDARLYRH FNASFWRKVE AFGRERMARE VAALRRANER MRRICIDGGR AVDAAAIEDS
370 380 390 400 410 420
AMQPWQPLGA KSILGYNLKK SIGQRHAQLC RRMLTPEIQY LMDLGANLWI TKLWKFIRDF
LRW