AQPM_ARCFU
ID AQPM_ARCFU Reviewed; 246 AA.
AC O28846;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Probable aquaporin AqpM;
GN Name=aqpM; OrderedLocusNames=AF_1426;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
CC -!- FUNCTION: Channel that permits osmotically driven movement of water in
CC both directions. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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; AE000782; AAB89820.1; -; Genomic_DNA.
DR PIR; A69428; A69428.
DR PDB; 3NE2; X-ray; 3.00 A; A/B/C/D/E/F/G/H=1-246.
DR PDBsum; 3NE2; -.
DR AlphaFoldDB; O28846; -.
DR SMR; O28846; -.
DR STRING; 224325.AF_1426; -.
DR TCDB; 1.A.8.13.1; the major intrinsic protein (mip) family.
DR EnsemblBacteria; AAB89820; AAB89820; AF_1426.
DR KEGG; afu:AF_1426; -.
DR eggNOG; arCOG04431; Archaea.
DR HOGENOM; CLU_020019_3_2_2; -.
DR OMA; IFKALMY; -.
DR PhylomeDB; O28846; -.
DR EvolutionaryTrace; O28846; -.
DR Proteomes; UP000002199; 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; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..246
FT /note="Probable aquaporin AqpM"
FT /id="PRO_0000064007"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..56
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..104
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..146
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..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 83..85
FT /note="NPA 1"
FT MOTIF 200..202
FT /note="NPA 2"
FT HELIX 5..34
FT /evidence="ECO:0007829|PDB:3NE2"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3NE2"
FT TURN 47..52
FT /evidence="ECO:0007829|PDB:3NE2"
FT HELIX 53..78
FT /evidence="ECO:0007829|PDB:3NE2"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:3NE2"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:3NE2"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3NE2"
FT HELIX 101..123
FT /evidence="ECO:0007829|PDB:3NE2"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:3NE2"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:3NE2"
FT HELIX 144..165
FT /evidence="ECO:0007829|PDB:3NE2"
FT HELIX 176..195
FT /evidence="ECO:0007829|PDB:3NE2"
FT HELIX 201..213
FT /evidence="ECO:0007829|PDB:3NE2"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:3NE2"
FT HELIX 224..243
FT /evidence="ECO:0007829|PDB:3NE2"
SQ SEQUENCE 246 AA; 25212 MW; 2CAE3D80B3BE97C3 CRC64;
MTMTLAKRFT AEVVGTFILV FFGPGAAVIT LMIANGADKP NEFNIGIGAL GGLGDWFAIG
MAFALAIAAV IYSLGRISGA HINPAVTIAL WSIGRFPGRE VVPYIVAQFI GAALGSLLFL
ACVGPAAATV GGLGATAPFP GIGYGQAILT EAIGTFLLML VIMGVAVDER APPGFAGLVI
GLTVGGIITT IGNITGSSLN PARTFGPYLG DSLMGINLWQ YFPIYVIGPI VGAVAAAWLY
NYLAKE
