Q9C4Z5 (AQPM_METTM) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 69.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Aquaporin AqpM | ||||
| Gene names |
| ||||
| Organism | Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 79929 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter |
Protein attributes
| Sequence length | 246 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Channel that permits osmotically driven movement of water in both directions. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. Exhibits also a transient but reproducible increase in the initial glycerol flux. |
| Subunit structure | Homotetramer. |
| Subcellular location | |
| Domain | Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). |
| Sequence similarities | Belongs to the MIP/aquaporin (TC 1.A.8) family. [View classification] |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transport |
| Cellular component | Cell membrane Membrane |
| Domain | Repeat Transmembrane Transmembrane helix |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | transmembrane transport Inferred from electronic annotation. Source: InterPro water transportInferred from electronic annotation. Source: InterPro |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | transporter activity Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 246 | 246 | Aquaporin AqpM | PRO_0000064006 | ||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||
| Topological domain | 1 – 11 | 11 | Cytoplasmic Potential | |||||||||||||||||||||||||||||||
| Transmembrane | 12 – 32 | 21 | Helical; Potential | |||||||||||||||||||||||||||||||
| Topological domain | 33 – 55 | 23 | Extracellular Potential | |||||||||||||||||||||||||||||||
| Transmembrane | 56 – 76 | 21 | Helical; Potential | |||||||||||||||||||||||||||||||
| Topological domain | 77 – 103 | 27 | Cytoplasmic Potential | |||||||||||||||||||||||||||||||
| Transmembrane | 104 – 124 | 21 | Helical; Potential | |||||||||||||||||||||||||||||||
| Topological domain | 125 – 145 | 21 | Extracellular Potential | |||||||||||||||||||||||||||||||
| Transmembrane | 146 – 166 | 21 | Helical; Potential | |||||||||||||||||||||||||||||||
| Topological domain | 167 – 172 | 6 | Cytoplasmic Potential | |||||||||||||||||||||||||||||||
| Transmembrane | 173 – 193 | 21 | Helical; Potential | |||||||||||||||||||||||||||||||
| Topological domain | 194 – 217 | 24 | Extracellular Potential | |||||||||||||||||||||||||||||||
| Transmembrane | 218 – 238 | 21 | Helical; Potential | |||||||||||||||||||||||||||||||
| Topological domain | 239 – 246 | 8 | Cytoplasmic Potential | |||||||||||||||||||||||||||||||
| Motif | 82 – 84 | 3 | NPA 1 | |||||||||||||||||||||||||||||||
| Motif | 199 – 201 | 3 | NPA 2 | |||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||
| Sequence conflict | 217 | 1 | N → D no nucleotide entry Ref.2 | |||||||||||||||||||||||||||||||
| Sequence conflict | 223 | 1 | P → S no nucleotide entry Ref.2 | |||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||
| Helix | 4 – 33 | 30 | ||||||||||||||||||||||||||||||||
| Beta strand | 45 – 47 | 3 | ||||||||||||||||||||||||||||||||
| Turn | 48 – 51 | 4 | ||||||||||||||||||||||||||||||||
| Helix | 52 – 77 | 26 | ||||||||||||||||||||||||||||||||
| Helix | 83 – 90 | 8 | ||||||||||||||||||||||||||||||||
| Turn | 91 – 93 | 3 | ||||||||||||||||||||||||||||||||
| Helix | 97 – 122 | 26 | ||||||||||||||||||||||||||||||||
| Helix | 125 – 128 | 4 | ||||||||||||||||||||||||||||||||
| Helix | 131 – 133 | 3 | ||||||||||||||||||||||||||||||||
| Helix | 143 – 164 | 22 | ||||||||||||||||||||||||||||||||
| Helix | 175 – 194 | 20 | ||||||||||||||||||||||||||||||||
| Helix | 200 – 212 | 13 | ||||||||||||||||||||||||||||||||
| Beta strand | 213 – 215 | 3 | ||||||||||||||||||||||||||||||||
| Turn | 219 – 223 | 5 | ||||||||||||||||||||||||||||||||
| Helix | 224 – 243 | 20 | ||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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., Kitagawa Y. J. Biosci. Bioeng. 92:488-491(2001) [PubMed: 16233136] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg. |
| [2] | Kozono D., Ding X., Iwasaki I., Meng X., Kamagata Y., Agre P., Kitagawa Y. Submitted (JUL-2004) to UniProtKB Cited for: SEQUENCE REVISION TO 51; 217 AND 223. |
| [3] | "Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism." Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K. J. Bacteriol. 192:5850-5851(2010) [PubMed: 20802048] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg. |
| [4] | "Functional expression and characterization of an archaeal aquaporin. AqpM from Methanothermobacter marburgensis." Kozono D., Ding X., Iwasaki I., Meng X., Kamagata Y., Agre P., Kitagawa Y. J. Biol. Chem. 278:10649-10656(2003) [PubMed: 12519768] [Abstract] Cited for: CHARACTERIZATION. Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AB055880 Genomic DNA. Translation: BAB32660.1. CP001710 Genomic DNA. Translation: ADL58146.1. | ||||||||||||||||||
| RefSeq | YP_003849459.1. NC_014408.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein family/group databases | |||||||||||||||||||
| TCDB | 1.A.8.13.2. major intrinsic protein (MIP) family. | ||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| GeneID | 9704259. | ||||||||||||||||||
| GenomeReviews | Gene locus MTBMA_c05510 in contig CP001710_GR. | ||||||||||||||||||
| KEGG | mmg:MTBMA_c05510. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CMR | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| OMA | YFPIYVI. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR012269. Aquaporin. IPR023271. Aquaporin-like. IPR000425. MIP. IPR022357. MIP_CS. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:1.20.1080.10. MIP. 1 hit. | ||||||||||||||||||
| KO | K02440. | ||||||||||||||||||
| PANTHER | PTHR19139. MIP. 1 hit. | ||||||||||||||||||
| Pfam | PF00230. MIP. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR00783. MINTRINSICP. | ||||||||||||||||||
| SUPFAM | SSF81338. MIP. 1 hit. | ||||||||||||||||||
| TIGRFAMs | TIGR00861. MIP. 1 hit. | ||||||||||||||||||
| PROSITE | PS00221. MIP. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | AQPM_METTM | ||||||||
| Accession | Primary (citable) accession number: Q9C4Z5 Secondary accession number(s): D9PV98 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with