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Protein

Aquaporin Z

Gene

aqpZ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei20 – 201Involved in tetramerization or stability of the tetramer
Sitei43 – 431Selectivity filter
Sitei174 – 1741Selectivity filter
Sitei183 – 1831Selectivity filter
Sitei189 – 1891Selectivity filter

GO - Molecular functioni

  • glycerol channel activity Source: GO_Central
  • identical protein binding Source: EcoCyc
  • water channel activity Source: EcoCyc

GO - Biological processi

  • cellular water homeostasis Source: EcoCyc
  • ion transmembrane transport Source: GO_Central
  • response to osmotic stress Source: EcoCyc
  • water transport Source: CACAO
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

BioCyciEcoCyc:AQPZ-MONOMER.
ECOL316407:JW0859-MONOMER.
MetaCyc:AQPZ-MONOMER.

Protein family/group databases

TCDBi1.A.8.3.1. the major intrinsic protein (mip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Aquaporin Z
Alternative name(s):
Bacterial nodulin-like intrinsic protein
Gene namesi
Name:aqpZ
Synonyms:bniP
Ordered Locus Names:b0875, JW0859
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13270. aqpZ.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence analysis
Transmembranei9 – 2921Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini30 – 334PeriplasmicSequence analysis
Transmembranei34 – 5421Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini55 – 8127CytoplasmicSequence analysisAdd
BLAST
Transmembranei82 – 10221Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini103 – 13028PeriplasmicSequence analysisAdd
BLAST
Transmembranei131 – 15121Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini152 – 1554CytoplasmicSequence analysis
Transmembranei156 – 17621Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini177 – 20125PeriplasmicSequence analysisAdd
BLAST
Transmembranei202 – 22221Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini223 – 2319CytoplasmicSequence analysis

GO - Cellular componenti

  • integral component of membrane Source: EcoliWiki
  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91C → S: No effect. 1 Publication
Mutagenesisi20 – 201C → S: Loss of oligomerization; no alteration of water permeability. 1 Publication
Mutagenesisi183 – 1831T → C: No effect. 1 Publication
Mutagenesisi189 – 1891R → V or S: Loss of function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 231231Aquaporin ZPRO_0000063989Add
BLAST

Proteomic databases

PaxDbiP60844.

Expressioni

Inductioni

By extracellular hypoosmotic conditions, especially during the mid-logarithmic phase of growth.

Interactioni

Subunit structurei

Homotetramer.3 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4260000. 107 interactions.
DIPiDIP-35499N.
STRINGi511145.b0875.

Structurei

Secondary structure

231
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 2525Combined sources
Turni26 – 283Combined sources
Turni30 – 323Combined sources
Helixi35 – 5824Combined sources
Helixi64 – 729Combined sources
Helixi78 – 803Combined sources
Helixi81 – 10323Combined sources
Helixi111 – 1144Combined sources
Helixi115 – 1173Combined sources
Helixi122 – 1243Combined sources
Beta strandi125 – 1273Combined sources
Helixi131 – 15222Combined sources
Helixi162 – 18120Combined sources
Helixi187 – 19711Combined sources
Helixi200 – 2034Combined sources
Helixi205 – 22622Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RC2X-ray2.50A/B1-231[»]
2ABMX-ray3.20A/B/C/D/E/F/G/H1-231[»]
2O9DX-ray2.30A/B1-231[»]
2O9EX-ray2.20A1-231[»]
2O9FX-ray2.55A/B1-231[»]
2O9GX-ray1.90A1-231[»]
3NK5X-ray2.40A/B1-231[»]
3NKAX-ray2.50A/B1-231[»]
3NKCX-ray3.10A/B1-231[»]
ProteinModelPortaliP60844.
SMRiP60844. Positions 1-231.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60844.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi63 – 653NPA 1
Motifi186 – 1883NPA 2

Domaini

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 similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105D8C. Bacteria.
COG0580. LUCA.
HOGENOMiHOG000288286.
InParanoidiP60844.
KOiK06188.
OMAiMPIIGGI.
PhylomeDBiP60844.

Family and domain databases

CDDicd00333. MIP. 1 hit.
Gene3Di1.20.1080.10. 1 hit.
HAMAPiMF_01146. Aquaporin_Z. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR023743. Aquaporin_Z.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERiPTHR19139. PTHR19139. 1 hit.
PfamiPF00230. MIP. 1 hit.
[Graphical view]
PRINTSiPR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P60844-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRKLAAECF GTFWLVFGGC GSAVLAAGFP ELGIGFAGVA LAFGLTVLTM
60 70 80 90 100
AFAVGHISGG HFNPAVTIGL WAGGRFPAKE VVGYVIAQVV GGIVAAALLY
110 120 130 140 150
LIASGKTGFD AAASGFASNG YGEHSPGGYS MLSALVVELV LSAGFLLVIH
160 170 180 190 200
GATDKFAPAG FAPIAIGLAL TLIHLISIPV TNTSVNPARS TAVAIFQGGW
210 220 230
ALEQLWFFWV VPIVGGIIGG LIYRTLLEKR D
Length:231
Mass (Da):23,703
Last modified:April 13, 2004 - v1
Checksum:i3BDE1A932D45CF14
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141W → C in BAA08441 (Ref. 2) Curated
Sequence conflicti26 – 261A → P in BAA08441 (Ref. 2) Curated
Sequence conflicti99 – 991L → V in AAC43518 (PubMed:7493926).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38664 Genomic DNA. Translation: AAC43518.1.
D49469 Genomic DNA. Translation: BAA08441.1.
U00096 Genomic DNA. Translation: AAC73962.1.
AP009048 Genomic DNA. Translation: BAA35589.1.
PIRiC64826.
RefSeqiNP_415396.1. NC_000913.3.
WP_001298299.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73962; AAC73962; b0875.
BAA35589; BAA35589; BAA35589.
GeneIDi945497.
KEGGiecj:JW0859.
eco:b0875.
PATRICi32116957. VBIEscCol129921_0904.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U38664 Genomic DNA. Translation: AAC43518.1.
D49469 Genomic DNA. Translation: BAA08441.1.
U00096 Genomic DNA. Translation: AAC73962.1.
AP009048 Genomic DNA. Translation: BAA35589.1.
PIRiC64826.
RefSeqiNP_415396.1. NC_000913.3.
WP_001298299.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RC2X-ray2.50A/B1-231[»]
2ABMX-ray3.20A/B/C/D/E/F/G/H1-231[»]
2O9DX-ray2.30A/B1-231[»]
2O9EX-ray2.20A1-231[»]
2O9FX-ray2.55A/B1-231[»]
2O9GX-ray1.90A1-231[»]
3NK5X-ray2.40A/B1-231[»]
3NKAX-ray2.50A/B1-231[»]
3NKCX-ray3.10A/B1-231[»]
ProteinModelPortaliP60844.
SMRiP60844. Positions 1-231.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260000. 107 interactions.
DIPiDIP-35499N.
STRINGi511145.b0875.

Protein family/group databases

TCDBi1.A.8.3.1. the major intrinsic protein (mip) family.

Proteomic databases

PaxDbiP60844.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73962; AAC73962; b0875.
BAA35589; BAA35589; BAA35589.
GeneIDi945497.
KEGGiecj:JW0859.
eco:b0875.
PATRICi32116957. VBIEscCol129921_0904.

Organism-specific databases

EchoBASEiEB1283.
EcoGeneiEG13270. aqpZ.

Phylogenomic databases

eggNOGiENOG4105D8C. Bacteria.
COG0580. LUCA.
HOGENOMiHOG000288286.
InParanoidiP60844.
KOiK06188.
OMAiMPIIGGI.
PhylomeDBiP60844.

Enzyme and pathway databases

BioCyciEcoCyc:AQPZ-MONOMER.
ECOL316407:JW0859-MONOMER.
MetaCyc:AQPZ-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP60844.
PROiP60844.

Family and domain databases

CDDicd00333. MIP. 1 hit.
Gene3Di1.20.1080.10. 1 hit.
HAMAPiMF_01146. Aquaporin_Z. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR023743. Aquaporin_Z.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERiPTHR19139. PTHR19139. 1 hit.
PfamiPF00230. MIP. 1 hit.
[Graphical view]
PRINTSiPR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAQPZ_ECOLI
AccessioniPrimary (citable) accession number: P60844
Secondary accession number(s): P48838, P75827, Q47159
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: September 7, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

It is a remarkably rigid tetramer that does not dissociate even when solubilized in SDS.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.