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 Q6WV16

Entry ID Method Resolution Chain Position Source
AF-Q6WV16-F1 Predicted AlphaFoldDB

No variants for Q6WV16

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q6WV16

No associated diseases with Q6WV16

3 regional properties for Q6WV16

Type Name Position InterPro Accession
domain Ricin B, lectin domain 519 - 648 IPR000772
domain Glycosyltransferase 2-like 205 - 389 IPR001173
domain N-acetylgalactosaminyltransferase 205 - 502 IPR045885

Functions

Description
EC Number 2.4.1.41 Hexosyltransferases
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

5 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).
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
Golgi stack The set of thin, flattened membrane-bounded compartments, called cisternae, that form the central portion of the Golgi complex. The stack usually comprises cis, medial, and trans cisternae; the cis- and trans-Golgi networks are not considered part of the stack.
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
carbohydrate binding Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates.
metal ion binding Binding to a metal ion.
polypeptide N-acetylgalactosaminyltransferase activity Catalysis of the reaction: UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide. This reaction is the modification of serine or threonine residues in polypeptide chains by the transfer of a N-acetylgalactose from UDP-N-acetylgalactose to the hydroxyl group of the amino acid; it is the first step in O-glycan biosynthesis.

2 GO annotations of biological process

Name Definition
oligosaccharide biosynthetic process The chemical reactions and pathways resulting in the formation of oligosaccharides, molecules with between two and (about) 20 monosaccharide residues connected by glycosidic linkages.
protein O-linked glycosylation A protein glycosylation process in which a carbohydrate or carbohydrate derivative unit is added to a protein via the hydroxyl group of peptidyl-serine, peptidyl-threonine, peptidyl-hydroxylysine, or peptidyl-hydroxyproline, or via the phenol group of peptidyl-tyrosine, forming an O-glycan.

23 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q07537 GALNT1 Polypeptide N-acetylgalactosaminyltransferase 1 Bos taurus (Bovine) PR
Q9Y117 Pgant3 Polypeptide N-acetylgalactosaminyltransferase 3 Drosophila melanogaster (Fruit fly) PR
Q6WV17 Pgant5 Polypeptide N-acetylgalactosaminyltransferase 5 Drosophila melanogaster (Fruit fly) PR
Q9NY28 GALNT8 Probable polypeptide N-acetylgalactosaminyltransferase 8 Homo sapiens (Human) PR
Q7Z7M9 GALNT5 Polypeptide N-acetylgalactosaminyltransferase 5 Homo sapiens (Human) PR
Q10472 GALNT1 Polypeptide N-acetylgalactosaminyltransferase 1 Homo sapiens (Human) PR
Q8IXK2 GALNT12 Polypeptide N-acetylgalactosaminyltransferase 12 Homo sapiens (Human) PR
Q14435 GALNT3 Polypeptide N-acetylgalactosaminyltransferase 3 Homo sapiens (Human) PR
Q8IUC8 GALNT13 Polypeptide N-acetylgalactosaminyltransferase 13 Homo sapiens (Human) PR
Q86SR1 GALNT10 Polypeptide N-acetylgalactosaminyltransferase 10 Homo sapiens (Human) PR
Q49A17 GALNTL6 Polypeptide N-acetylgalactosaminyltransferase-like 6 Homo sapiens (Human) PR
O08912 Galnt1 Polypeptide N-acetylgalactosaminyltransferase 1 Mus musculus (Mouse) PR
P70419 Galnt3 Polypeptide N-acetylgalactosaminyltransferase 3 Mus musculus (Mouse) PR
Q921L8 Galnt11 Polypeptide N-acetylgalactosaminyltransferase 11 Mus musculus (Mouse) PR
Q8BGT9 Galnt12 Polypeptide N-acetylgalactosaminyltransferase 12 Mus musculus (Mouse) PR
Q8CF93 Galnt13 Polypeptide N-acetylgalactosaminyltransferase 13 Mus musculus (Mouse) PR
Q29121 GALNT1 Polypeptide N-acetylgalactosaminyltransferase 1 Sus scrofa (Pig) PR
O88422 Galnt5 Polypeptide N-acetylgalactosaminyltransferase 5 Rattus norvegicus (Rat) PR
Q10473 Galnt1 Polypeptide N-acetylgalactosaminyltransferase 1 Rattus norvegicus (Rat) PR
Q6UE39 Galnt13 Polypeptide N-acetylgalactosaminyltransferase 13 Rattus norvegicus (Rat) PR
Q925R7 Galnt10 Polypeptide N-acetylgalactosaminyltransferase 10 Rattus norvegicus (Rat) PR
Q7K755 gly-11 Putative polypeptide N-acetylgalactosaminyltransferase 11 Caenorhabditis elegans PR
P34678 gly-3 Polypeptide N-acetylgalactosaminyltransferase 3 Caenorhabditis elegans PR
10 20 30 40 50 60
MRRPNLKWIV KASLLLLISL TLFVLITSWI SSTPYTNKPV HHGVEPVPEK AGLSGDVKVK
70 80 90 100 110 120
VPAIKQPEPQ KPQEPDFEED PELQKIDEPE PVEEEVDNPH PADDEPQQQP QEELQMAAPA
130 140 150 160 170 180
DASVKKDWHD YTFMEKDAKR VGLGEGGKAS TLDDESQRDL EKRMSLENGF NALLSDSISV
190 200 210 220 230 240
NRSVPDIRHP LCRKKEYVAK LPTVSVIIIF YNEYLSVLMR SVHSLINRSP PELMKEIILV
250 260 270 280 290 300
DDHSDREYLG KELETYIAEH FKWVRVVRLP RRTGLIGARA AGARNATAEV LIFLDSHVEA
310 320 330 340 350 360
NYNWLPPLLE PIALNKRTAV CPFIDVIDHT NFHYRAQDEG ARGAFDWEFF YKRLPLLPED
370 380 390 400 410 420
LKHPADPFKS PIMAGGLFAI SREFFWELGG YDEGLDIWGG EQYELSFKIW MCGGEMYDAP
430 440 450 460 470 480
CSRIGHIYRG PRNHQPSPRK GDYLHKNYKR VAEVWMDEYK NYLYSHGDGL YESVDPGDLT
490 500 510 520 530 540
EQKAIRTKLN CKSFKWFMEE VAFDLMKTYP PVDPPSYAMG ALQNVGNQNL CLDTLGRKKH
550 560 570 580 590 600
NKMGMYACAD NIKTPQRTQF WELSWKRDLR LRRKKECLDV QIWDANAPVW LWDCHSQGGN
610 620 630 640 650 660
QYWYYDYRHK QLKHGTEGRR CLELLPFSQE VVANKCDTDN RFQQWNFGSF NKTALDNYSQ
DLVLSL