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1.A.8.13.2
Hg2+-inhibitable aquaporin, AqpM (transports both water and glycerol as well as CO2) (Kozono et al., 2003; Araya-Secchi et al., 2011). Its 3-d structure has been determined to 1.7 Å. In AqpM, isoleucine replaces a key histidine residue found in the lumen of water channels, which becomes a glycine residue in aquaglyceroporins. As a result of this and other side-chain substituents in the walls of the channel, the channel is intermediate in size and exhibits differentially tuned electrostatics when compared with the other subfamilies (Lee et al. 2005).

Accession Number:Q9C4Z5
Protein Name:AqpM
Length:246
Molecular Weight:25348.00
Species:Methanobacterium thermoautotrophicum (strain Marburg / DSM 2133) [79929]
Number of TMSs:6
Location1 / Topology2 / Orientation3: Cell membrane1 / Multi-pass membrane protein2
Substrate water, glycerol, carbon dioxide

Cross database links:

Pfam: PF00230   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0005886 C:plasma membrane
GO:0005215 F:transporter activity
GO:0055085 P:transmembrane transport

References (2)

[1] “Rapid amplification of a water channel-like gene and its flanking sequences from the Methanothermobacter marburgensis genome using a single primer PCR strategy.”  Ding X.et.al.   16233136
[2] “Functional expression and characterization of an archaeal aquaporin. AqpM from Methanothermobacter marburgensis.”  Kozono D.et.al.   12519768
Structure:
2EVU   2F2B     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence 
1:	MVSLTKRCIA EFIGTFILVF FGAGSAAVTL MIASGGTSPN PFNIGIGLLG GLGDWVAIGL 
61:	AFGFAIAASI YALGNISGCH INPAVTIGLW SVKKFPGREV VPYIIAQLLG AAFGSFIFLQ 
121:	CAGIGAATVG GLGATAPFPG ISYWQAMLAE VVGTFLLMIT IMGIAVDERA PKGFAGIIIG 
181:	LTVAGIITTL GNISGSSLNP ARTFGPYLND MIFAGTDLWN YYSIYVIGPI VGAVLAALTY 
241:	QYLTSE