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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)DescriptionActionsGraphical viewLength
Sitei58Substrate discrimination1
Sitei182Substrate discrimination1
Sitei191Hg(2+)-sensitive residue1
Sitei197Substrate discrimination1

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)DescriptionActionsGraphical viewLength
Topological domaini2 – 9Cytoplasmic8
Transmembranei10 – 34Helical; Name=Helix 1Add BLAST25
Topological domaini35 – 50ExtracellularAdd BLAST16
Transmembranei51 – 68Helical; Name=Helix 2Add BLAST18
Topological domaini69 – 73Cytoplasmic5
Intramembranei74 – 785
Intramembranei79 – 88Helical; Name=Helix B10
Topological domaini89 – 92Cytoplasmic4
Transmembranei93 – 117Helical; Name=Helix 3Add BLAST25
Topological domaini118 – 142ExtracellularAdd BLAST25
Transmembranei143 – 158Helical; Name=Helix 4Add BLAST16
Topological domaini159 – 169CytoplasmicAdd BLAST11
Transmembranei170 – 187Helical; Name=Helix 5Add BLAST18
Topological domaini188 – 189Extracellular2
Intramembranei190 – 1934
Intramembranei194 – 204Helical; Name=Helix EAdd BLAST11
Topological domaini205 – 215ExtracellularAdd BLAST11
Transmembranei216 – 230Helical; Name=Helix 6Add BLAST15
Topological domaini231 – 271CytoplasmicAdd BLAST41

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000639182 – 271Aquaporin-1Add BLAST270

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi42N-linked (GlcNAc...)Sequence analysis1
Modified residuei249PhosphoserineBy similarity1
Modified residuei255PhosphotyrosineBy similarity1
Modified residuei264PhosphoserineBy similarity1

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP47865.
PRIDEiP47865.

Expressioni

Gene expression databases

BgeeiENSBTAG00000000745.

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

1271
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 33Combined sources28
Helixi34 – 36Combined sources3
Helixi51 – 73Combined sources23
Helixi79 – 87Combined sources9
Helixi93 – 117Combined sources25
Turni118 – 120Combined sources3
Helixi139 – 141Combined sources3
Helixi142 – 158Combined sources17
Helixi170 – 189Combined sources20
Helixi195 – 204Combined sources10
Turni209 – 212Combined sources4
Helixi213 – 230Combined sources18
Turni231 – 233Combined sources3
Helixi240 – 244Combined sources5
Helixi245 – 247Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP47865.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi78 – 80NPA 13
Motifi194 – 196NPA 23

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi161 – 164Poly-Arg4

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.
OMAiFQDHWIF.
OrthoDBiEOG091G166T.
TreeFamiTF312940.

Family and domain databases

CDDicd00333. MIP. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1J4NX-ray2.20A1-271[»]
ProteinModelPortaliP47865.
SMRiP47865.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000000993.

Proteomic databases

PaxDbiP47865.
PRIDEiP47865.

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.
OMAiFQDHWIF.
OrthoDBiEOG091G166T.
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.

Gene expression databases

BgeeiENSBTAG00000000745.

Family and domain databases

CDDicd00333. MIP. 1 hit.
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...

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: November 30, 2016
This is version 132 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.