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Putative glycerol:H+ symporter of 546 aas and 12 TMSs, GUP1.  In yeast, Gup1 is associated with a high number and diversity of biological functions, namely polarity establishment, secretory/endocytic pathway functionality, vacuole morphology, wall and membrane composition, structure and maintenance, cell death, morphogenesis and differentiation (Lucas et al. 2016). The protein HHAT (Hedgehog O-acyltransferase) modifies Hh morphogens prior to their secretion, while HHATL (Hh O-acyltransferase-like) negatively regulates the pathway. HHAT and HHATL are homologous to Saccharomyces cerevisiae Gup2 and Gup1, respectively (Lucas et al. 2016).

GUP1 of Saccharomyces cerevisiae

Protein-cysteine N-palmitoyltransferase HHAT-like protein (Glycerol uptake/transporter homologue) (Hedgehog acyltransferase-like protein)

HHATL protein of Mus musculus

Protein-cysteine N-palmitoyltransferase HHAT (EC 2.3.1.-) (Hedgehog acyltransferase) (Skinny hedgehog protein)
Hhat of Mus musculus

The alanyl teichoic acid synthesis protein, DltB of 395 aas and 12 TMSs. It may transport activated alanine across the membrane (Perego et al., 1995).  Crystal structures of DltB, a membrane-bound O-acyl transferase, MBOAT, responsible for the D-alanylation of cell-wall teichoic acid in Gram-positive bacteri, both alone and in complex with the D-alanyl donor protein DltC (an acyl carrier protein) have been solved (Ma et al. 2018). DltB contains a ring of 11 peripheral transmembrane helices, which shield a highly conserved extracellular structural funnel extending into the middle of the lipid bilayer. The conserved catalytic histidine residue is located at the bottom of this funnel and is connected to the intracellular DltC (acyl carrier protein) through a narrow tunnel. Mutation of either the catalytic histidine or the DltC-binding site of DltB abolishes D-alanylation of lipoteichoic acid and sensitizes Bacillus subtilis to cell-wall stress, which suggests cross-membrane catalysis involving the tunnel. Structure-guided sequence comparisons among DltB and vertebrate MBOATs reveals a conserved structural core and suggests that MBOATs from different organisms have similar catalytic mechanisms (Ma et al. 2018).

DltB of Bacillus subtilis (P39580)

DltC of Bacillus subtiois (P39579)

MBOAT family protein of 494 aas and 10 - 12 TMSs.

MBOAT family protein of Leptospira santarosai

Uncharacterized MBOAT family protein of 461 aas and 12 TMSs.

UP of Lunatimonas lonarensis

Uncharacterized MBOAT family protein of 483 aas and 11 TMSs.

UP of Entamoeba histolytica

MBOAT7, also called BB1, LENG4, OCT7, of 472 aas and possibly 12 TMSs as 3 sets of 4 putative TMSs, where in each set, the last two TMSs are closs together.  Caddeo et al. 2019 reported that the protein is anchored to the endo membrane via a 6 TMS domain. The predicted catalytic dyad of the protein, composed of the conserved asparagine in position 321 (Asn-321) and the preserved histidine in position 356 (His-356), has a lumenal localization. This is compatible with the role of MBOAT7 in remodeling the acyl chain composition of endomembranes.

MBOAT7 of Homo sapiens