TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*9.B.37.1.1









Huntington-interacting Protein 14, HIP14, of 632 aas and 6 or more TMSS.  This protein has been suggested to be a Mg2+ transporter, but the evidence is equivocal (Schäffers et al. 2018).

Eukaryota
Metazoa
HIP14 of Homo sapiens (Q8IUH5)
*9.B.37.1.2









Huntington-interacting Protein 14, HIP14. Eukaryotic divalent cation transporter (Quamme, 2009)

Eukaryota
Metazoa
HIP14 of Drosophila melanogaster (Q9VUW9)
*9.B.37.2.1









Golgi Ca2+ and Mg2+ transporting palmitoyltransferase GodZ (ZDHHC3) (also palmitoylates protein substrates; Hines et al., 2010; Goytain et al., 2008).  Residues 50-233 in this protein show 27% identity to residues 372-539 in 9.B.37.1.1.

Eukaryota
Metazoa
ZDHHC3 (GodZ) of Homo sapiens (Q8R173)
*9.B.37.2.2









S-acyltransferase of 294 aas and 4 TMSs

Eukaryota
Viridiplantae
S-acyltransferase of Volvox carteri
*9.B.37.2.3









The ZDHHC9-GOLGA7 complex is a palmitoyltransferase specific for hRAS and nRAS (Swarthout et al. 2005). DHHC (Asp-His-His-Cys) palmitoyltransferases are eukaryotic integral membrane enzymes that catalyze protein palmitoylation, which is important in a range of physiological processes, including small guanosine triphosphatase (GTPase) signaling, cell adhesion, and neuronal receptor scaffolding.  Rana et al. 2018 presented crystal structures of two DHHC palmitoyltransferases and a covalent intermediate mimic. The active site resides at the membrane-cytosol interface allow the enzyme to catalyze thioester-exchange using fatty acyl-coenzyme A, explaining why membrane-proximal cysteines are candidates for palmitoylation. The acyl chain binds in a cavity formed by the transmembrane domain. Rana et al. 2018 proposed a mechanism for acyl chain-length selectivity in DHHC enzymes on the basis of cavity muRana et al. 2018 presented crystal structures of two DHHC palmitoyltransferases and a covalent intermediate mimic. The active site resides at the membrane-cytosol interface allow the enzyme to catalyze thioester-exchange using fatty acyl-coenzyme A, explaining why membrane-proximal cysteines are candidates for palmitoylation. The acyl chain binds in a cavity formed by the transmembrane domain. Rana et al. 2018 proposed a mechanism for acyl chain-length selectivity in DHHC enzymes on the basis of cavity muRana et al. 2018 proposed a mechanism for acyl chain-length selectivity in DHHC enzymes on the basis of cavity mutants with preferences for shorter and longer acyl chains.

 

Eukaryota
Metazoa
The ZDHHC9-GOLGA7 complex of Homo sapiens
*9.B.37.3.1









Golgi electrogenic, voltage-dependent, Mg2+-transporting palmitoyltransferase, Huntington-interacting protein, HIP14 (ZDHHC13) (Up-regulated with low [Mg2+]; Km =0.8 mM; regulated by autopalmitoylation) (Goytain et al., 2008).

Eukaryota
Metazoa
HIP14 of Homo sapiens (Q8IUH4)