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   27-MAR-2024, entry version 122.
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   PaxDb; 79929-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   OrthoDB; 36050at2157; -.
DR   EvolutionaryTrace; Q9C4Z5; -.
DR   Proteomes; UP000000345; Chromosome.
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; Glycerol uptake facilitator protein; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR034294; Aquaporin_transptr.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   NCBIfam; TIGR00861; MIP; 1.
DR   PANTHER; PTHR19139:SF199; AQUAPORIN; 1.
DR   PANTHER; PTHR19139; AQUAPORIN TRANSPORTER; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; Aquaporin-like; 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
//