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Protein

Aquaporin Z

Gene

aqpZ

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei20Involved in tetramerization or stability of the tetramer1
Sitei43Selectivity filter1
Sitei174Selectivity filter1
Sitei183Selectivity filter1
Sitei189Selectivity filter1

GO - Molecular functioni

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

GO - Biological processi

  • cellular water homeostasis Source: EcoCyc
  • response to osmotic stress Source: EcoCyc
  • water transport Source: EcoCyc

Keywordsi

Biological processTransport

Enzyme and pathway databases

BioCyciEcoCyc:AQPZ-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13270 aqpZ

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 8CytoplasmicSequence analysis8
Transmembranei9 – 29Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini30 – 33PeriplasmicSequence analysis4
Transmembranei34 – 54Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini55 – 81CytoplasmicSequence analysisAdd BLAST27
Transmembranei82 – 102Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini103 – 130PeriplasmicSequence analysisAdd BLAST28
Transmembranei131 – 151Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini152 – 155CytoplasmicSequence analysis4
Transmembranei156 – 176Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini177 – 201PeriplasmicSequence analysisAdd BLAST25
Transmembranei202 – 222Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini223 – 231CytoplasmicSequence analysis9

GO - Cellular componenti

  • integral component of membrane Source: EcoliWiki
  • integral component of plasma membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9C → S: No effect. 1 Publication1
Mutagenesisi20C → S: Loss of oligomerization; no alteration of water permeability. 1 Publication1
Mutagenesisi183T → C: No effect. 1 Publication1
Mutagenesisi189R → V or S: Loss of function. 1 Publication1

Chemistry databases

DrugBankiDB03152 B-2-Octylglucoside
DB07923 octyl alpha-L-altropyranoside
DB07924 octyl beta-D-galactopyranoside

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000639891 – 231Aquaporin ZAdd BLAST231

Proteomic databases

PaxDbiP60844
PRIDEiP60844

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Homotetramer.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-957663,EBI-957663

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4260000, 107 interactors
DIPiDIP-35499N
STRINGi316385.ECDH10B_0945

Structurei

Secondary structure

1231
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1 – 25Combined sources25
Turni26 – 28Combined sources3
Turni30 – 32Combined sources3
Helixi35 – 58Combined sources24
Helixi64 – 72Combined sources9
Helixi78 – 80Combined sources3
Helixi81 – 103Combined sources23
Helixi111 – 114Combined sources4
Helixi115 – 117Combined sources3
Helixi122 – 124Combined sources3
Beta strandi125 – 127Combined sources3
Helixi131 – 152Combined sources22
Helixi162 – 181Combined sources20
Helixi187 – 197Combined sources11
Helixi200 – 203Combined sources4
Helixi205 – 226Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60844

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi63 – 65NPA 13
Motifi186 – 188NPA 23

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
OMAiELFGTFW
PhylomeDBiP60844

Family and domain databases

CDDicd00333 MIP, 1 hit
Gene3Di1.20.1080.10, 1 hit
HAMAPiMF_01146 Aquaporin_Z, 1 hit
InterProiView protein in InterPro
IPR023271 Aquaporin-like
IPR034294 Aquaporin_transptr
IPR023743 Aquaporin_Z
IPR000425 MIP
IPR022357 MIP_CS
PANTHERiPTHR19139 PTHR19139, 1 hit
PfamiView protein in Pfam
PF00230 MIP, 1 hit
PRINTSiPR00783 MINTRINSICP
SUPFAMiSSF81338 SSF81338, 1 hit
TIGRFAMsiTIGR00861 MIP, 1 hit
PROSITEiView protein in PROSITE
PS00221 MIP, 1 hit

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)DescriptionActionsGraphical viewLength
Sequence conflicti14W → C in BAA08441 (Ref. 2) Curated1
Sequence conflicti26A → P in BAA08441 (Ref. 2) Curated1
Sequence conflicti99L → V in AAC43518 (PubMed:7493926).Curated1

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
PATRICifig|1411691.4.peg.1402

Similar proteinsi

Entry informationi

Entry nameiAQPZ_ECOLI
AccessioniPrimary (citable) accession number: P60844
Secondary accession number(s): P48838, P75827, Q47159
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: March 28, 2018
This is version 131 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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