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Protein

Aquaporin-1

Gene

AQP1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Forms a water-specific channel that provides the plasma membranes of red cells and kidney proximal tubules with high permeability to water, thereby permitting water to move in the direction of an osmotic gradient.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei58 – 581Substrate discrimination
Sitei182 – 1821Substrate discrimination
Sitei191 – 1911Hg(2+)-sensitive residue
Sitei197 – 1971Substrate discrimination

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiR-BTA-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-BTA-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-BTA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-BTA-432047. Passive transport by Aquaporins.

Names & Taxonomyi

Protein namesi
Recommended name:
Aquaporin-1
Short name:
AQP-1
Alternative name(s):
Aquaporin-CHIP
Water channel protein CHIP29
Water channel protein for red blood cells and kidney proximal tubule
Gene namesi
Name:AQP1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 4

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 98Cytoplasmic
Transmembranei10 – 3425Helical; Name=Helix 1Add
BLAST
Topological domaini35 – 5016ExtracellularAdd
BLAST
Transmembranei51 – 6818Helical; Name=Helix 2Add
BLAST
Topological domaini69 – 735Cytoplasmic
Intramembranei74 – 785
Intramembranei79 – 8810Helical; Name=Helix B
Topological domaini89 – 924Cytoplasmic
Transmembranei93 – 11725Helical; Name=Helix 3Add
BLAST
Topological domaini118 – 14225ExtracellularAdd
BLAST
Transmembranei143 – 15816Helical; Name=Helix 4Add
BLAST
Topological domaini159 – 16911CytoplasmicAdd
BLAST
Transmembranei170 – 18718Helical; Name=Helix 5Add
BLAST
Topological domaini188 – 1892Extracellular
Intramembranei190 – 1934
Intramembranei194 – 20411Helical; Name=Helix EAdd
BLAST
Topological domaini205 – 21511ExtracellularAdd
BLAST
Transmembranei216 – 23015Helical; Name=Helix 6Add
BLAST
Topological domaini231 – 27141CytoplasmicAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 271270Aquaporin-1PRO_0000063918Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence analysis
Modified residuei249 – 2491PhosphoserineBy similarity
Modified residuei255 – 2551PhosphotyrosineBy similarity
Modified residuei264 – 2641PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP47865.

Interactioni

Subunit structurei

Homotetramer. Interacts with EPHB2; involved in endolymph production in the inner ear. Identified in a complex with STOM (By similarity).By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000993.

Structurei

Secondary structure

1
271
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 3328Combined sources
Helixi34 – 363Combined sources
Helixi51 – 7323Combined sources
Helixi79 – 879Combined sources
Helixi93 – 11725Combined sources
Turni118 – 1203Combined sources
Helixi139 – 1413Combined sources
Helixi142 – 15817Combined sources
Helixi170 – 18920Combined sources
Helixi195 – 20410Combined sources
Turni209 – 2124Combined sources
Helixi213 – 23018Combined sources
Turni231 – 2333Combined sources
Helixi240 – 2445Combined sources
Helixi245 – 2473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J4NX-ray2.20A1-271[»]
ProteinModelPortaliP47865.
SMRiP47865. Positions 1-249.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP47865.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi78 – 803NPA 1
Motifi194 – 1963NPA 2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi161 – 1644Poly-Arg

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

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
GeneTreeiENSGT00760000119223.
HOGENOMiHOG000288286.
HOVERGENiHBG000312.
InParanoidiP47865.
KOiK09864.
OMAiIHARVEM.
OrthoDBiEOG7N8ZWD.
TreeFamiTF312940.

Family and domain databases

Gene3Di1.20.1080.10. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR023274. Aquaporin_1.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERiPTHR19139. PTHR19139. 1 hit.
PfamiPF00230. MIP. 1 hit.
[Graphical view]
PRINTSiPR02013. AQUAPORIN1.
PR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P47865-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASEFKKKLF WRAVVAEFLA MILFIFISIG SALGFHYPIK SNQTTGAVQD
60 70 80 90 100
NVKVSLAFGL SIATLAQSVG HISGAHLNPA VTLGLLLSCQ ISVLRAIMYI
110 120 130 140 150
IAQCVGAIVA TAILSGITSS LPDNSLGLNA LAPGVNSGQG LGIEIIGTLQ
160 170 180 190 200
LVLCVLATTD RRRRDLGGSG PLAIGFSVAL GHLLAIDYTG CGINPARSFG
210 220 230 240 250
SSVITHNFQD HWIFWVGPFI GAALAVLIYD FILAPRSSDL TDRVKVWTSG
260 270
QVEEYDLDAD DINSRVEMKP K
Length:271
Mass (Da):28,800
Last modified:January 23, 2007 - v3
Checksum:i3A1C9A2071CDA5E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74759 mRNA. Translation: AAB32365.1.
AF028005 mRNA. Translation: AAB84190.1.
BT025412 mRNA. Translation: ABF57368.1.
BC105525 mRNA. Translation: AAI05526.1.
PIRiJC2348.
RefSeqiNP_777127.1. NM_174702.3.
UniGeneiBt.1525.

Genome annotation databases

EnsembliENSBTAT00000000993; ENSBTAP00000000993; ENSBTAG00000000745.
GeneIDi282653.
KEGGibta:282653.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74759 mRNA. Translation: AAB32365.1.
AF028005 mRNA. Translation: AAB84190.1.
BT025412 mRNA. Translation: ABF57368.1.
BC105525 mRNA. Translation: AAI05526.1.
PIRiJC2348.
RefSeqiNP_777127.1. NM_174702.3.
UniGeneiBt.1525.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J4NX-ray2.20A1-271[»]
ProteinModelPortaliP47865.
SMRiP47865. Positions 1-249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000993.

Proteomic databases

PaxDbiP47865.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000000993; ENSBTAP00000000993; ENSBTAG00000000745.
GeneIDi282653.
KEGGibta:282653.

Organism-specific databases

CTDi358.

Phylogenomic databases

eggNOGiKOG0223. Eukaryota.
COG0580. LUCA.
GeneTreeiENSGT00760000119223.
HOGENOMiHOG000288286.
HOVERGENiHBG000312.
InParanoidiP47865.
KOiK09864.
OMAiIHARVEM.
OrthoDBiEOG7N8ZWD.
TreeFamiTF312940.

Enzyme and pathway databases

ReactomeiR-BTA-1237044. Erythrocytes take up carbon dioxide and release oxygen.
R-BTA-1247673. Erythrocytes take up oxygen and release carbon dioxide.
R-BTA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-BTA-432047. Passive transport by Aquaporins.

Miscellaneous databases

EvolutionaryTraceiP47865.

Family and domain databases

Gene3Di1.20.1080.10. 1 hit.
InterProiIPR023271. Aquaporin-like.
IPR023274. Aquaporin_1.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERiPTHR19139. PTHR19139. 1 hit.
PfamiPF00230. MIP. 1 hit.
[Graphical view]
PRINTSiPR02013. AQUAPORIN1.
PR00783. MINTRINSICP.
SUPFAMiSSF81338. SSF81338. 1 hit.
TIGRFAMsiTIGR00861. MIP. 1 hit.
PROSITEiPS00221. MIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a novel cDNA homologous to CHIP28 water channel from ocular ciliary epithelium."
    Patil R.V., Yang X., Saito I., Coca-Prados M., Wax M.B.
    Biochem. Biophys. Res. Commun. 204:861-866(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ocular ciliary epithelium.
  2. "Nucleotide sequence of an aquaporin cDNA from bovine bone marrow."
    Joshi S., Recinos A., Jap B.K.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Bone marrow.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. NIH - Mammalian Gene Collection (MGC) project
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Ascending colon.
  5. "Crystallization and preliminary X-ray crystallographic analysis of water channel AQP1."
    Sui H., Walian P.J., Tang G., Oh A., Jap B.K.
    Acta Crystallogr. D 56:1198-1200(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  6. "Structural basis of water-specific transport through the AQP1 water channel."
    Sui H., Han B.-G., Lee J.K., Walian P., Jap B.K.
    Nature 414:872-878(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Entry informationi

Entry nameiAQP1_BOVIN
AccessioniPrimary (citable) accession number: P47865
Secondary accession number(s): Q2HJE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Pharmacologically inhibited by submillimolar concentrations of mercury.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.