AQPM_METTM
ID AQPM_METTM Reviewed; 246 AA.
AC Q9C4Z5; D9PV98;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 4.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Aquaporin AqpM;
GN Name=aqpM; OrderedLocusNames=MTBMA_c05510;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=16233136; DOI=10.1263/jbb.92.488;
RA Ding X., Kitagawa Y.;
RT "Rapid amplification of a water channel-like gene and its flanking
RT sequences from the Methanothermobacter marburgensis genome using a single
RT primer PCR strategy.";
RL J. Biosci. Bioeng. 92:488-491(2001).
RN [2]
RP SEQUENCE REVISION TO 51; 217 AND 223.
RA Kozono D., Ding X., Iwasaki I., Meng X., Kamagata Y., Agre P., Kitagawa Y.;
RL Submitted (JUL-2004) to UniProtKB.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
RN [4]
RP CHARACTERIZATION.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=12519768; DOI=10.1074/jbc.m212418200;
RA Kozono D., Ding X., Iwasaki I., Meng X., Kamagata Y., Agre P., Kitagawa Y.;
RT "Functional expression and characterization of an archaeal aquaporin. AqpM
RT from Methanothermobacter marburgensis.";
RL J. Biol. Chem. 278:10649-10656(2003).
CC -!- FUNCTION: Channel that permits osmotically driven movement of water in
CC both directions. It mediates rapid entry or exit of water in response
CC to abrupt changes in osmolarity. Exhibits also a transient but
CC reproducible increase in the initial glycerol flux.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC membrane-spanning domains and a pore-forming loop with the signature
CC motif Asn-Pro-Ala (NPA).
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AB055880; BAB32660.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL58146.1; -; Genomic_DNA.
DR RefSeq; WP_013295370.1; NC_014408.1.
DR PDB; 2EVU; X-ray; 2.30 A; A=1-246.
DR PDB; 2F2B; X-ray; 1.68 A; A=1-246.
DR PDBsum; 2EVU; -.
DR PDBsum; 2F2B; -.
DR AlphaFoldDB; Q9C4Z5; -.
DR SMR; Q9C4Z5; -.
DR STRING; 79929.MTBMA_c05510; -.
DR TCDB; 1.A.8.13.2; the major intrinsic protein (mip) family.
DR EnsemblBacteria; ADL58146; ADL58146; MTBMA_c05510.
DR GeneID; 9704259; -.
DR KEGG; mmg:MTBMA_c05510; -.
DR PATRIC; fig|79929.8.peg.535; -.
DR HOGENOM; CLU_020019_3_1_2; -.
DR OMA; IFKALMY; -.
DR OrthoDB; 45822at2157; -.
DR EvolutionaryTrace; Q9C4Z5; -.
DR Proteomes; UP000000345; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR45724; PTHR45724; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..246
FT /note="Aquaporin AqpM"
FT /id="PRO_0000064006"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..55
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..145
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 82..84
FT /note="NPA 1"
FT MOTIF 199..201
FT /note="NPA 2"
FT CONFLICT 217
FT /note="N -> D (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="P -> S (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 4..33
FT /evidence="ECO:0007829|PDB:2F2B"
FT TURN 46..51
FT /evidence="ECO:0007829|PDB:2F2B"
FT HELIX 52..73
FT /evidence="ECO:0007829|PDB:2F2B"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:2F2B"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:2F2B"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:2F2B"
FT HELIX 100..122
FT /evidence="ECO:0007829|PDB:2F2B"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:2F2B"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:2F2B"
FT HELIX 143..164
FT /evidence="ECO:0007829|PDB:2F2B"
FT HELIX 175..194
FT /evidence="ECO:0007829|PDB:2F2B"
FT HELIX 200..214
FT /evidence="ECO:0007829|PDB:2F2B"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:2F2B"
FT HELIX 224..243
FT /evidence="ECO:0007829|PDB:2F2B"
SQ SEQUENCE 246 AA; 25357 MW; B6A31126A66257D6 CRC64;
MVSLTKRCIA EFIGTFILVF FGAGSAAVTL MIASGGTSPN PFNIGIGLLG GLGDWVAIGL
AFGFAIAASI YALGNISGCH INPAVTIGLW SVKKFPGREV VPYIIAQLLG AAFGSFIFLQ
CAGIGAATVG GLGATAPFPG ISYWQAMLAE VVGTFLLMIT IMGIAVDERA PKGFAGIIIG
LTVAGIITTL GNISGSSLNP ARTFGPYLND MIFAGTNLWN YYPIYVIGPI VGAVLAALTY
QYLTSE
