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Protein

Aquaporin-1

Gene

AQP1

Organism
Homo sapiens (Human)
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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei56 – 561Substrate discrimination
Sitei180 – 1801Substrate discrimination
Sitei189 – 1891Hg(2+)-sensitive residue
Sitei195 – 1951Substrate discrimination

GO - Molecular functioni

  • ammonium transmembrane transporter activity Source: UniProtKB
  • carbon dioxide transmembrane transporter activity Source: UniProtKB
  • glycerol channel activity Source: GO_Central
  • glycerol transmembrane transporter activity Source: UniProtKB
  • intracellular cGMP activated cation channel activity Source: UniProtKB
  • nitric oxide transmembrane transporter activity Source: UniProtKB
  • potassium channel activity Source: UniProtKB
  • potassium ion transmembrane transporter activity Source: UniProtKB
  • transmembrane transporter activity Source: UniProtKB
  • water channel activity Source: UniProtKB
  • water transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  • ammonium transmembrane transport Source: GOC
  • ammonium transport Source: UniProtKB
  • bicarbonate transport Source: Reactome
  • camera-type eye morphogenesis Source: Ensembl
  • carbon dioxide transmembrane transport Source: UniProtKB
  • carbon dioxide transport Source: UniProtKB
  • cation transmembrane transport Source: GOC
  • cellular homeostasis Source: UniProtKB
  • cellular hyperosmotic response Source: UniProtKB
  • cellular response to cAMP Source: UniProtKB
  • cellular response to copper ion Source: UniProtKB
  • cellular response to dexamethasone stimulus Source: UniProtKB
  • cellular response to hydrogen peroxide Source: UniProtKB
  • cellular response to hypoxia Source: UniProtKB
  • cellular response to inorganic substance Source: UniProtKB
  • cellular response to mechanical stimulus Source: UniProtKB
  • cellular response to mercury ion Source: UniProtKB
  • cellular response to nitric oxide Source: UniProtKB
  • cellular response to retinoic acid Source: UniProtKB
  • cellular response to salt stress Source: UniProtKB
  • cellular response to stress Source: UniProtKB
  • cellular response to UV Source: UniProtKB
  • cellular water homeostasis Source: GO_Central
  • cell volume homeostasis Source: UniProtKB
  • cerebrospinal fluid secretion Source: UniProtKB
  • cGMP biosynthetic process Source: UniProtKB
  • corticotropin secretion Source: Ensembl
  • establishment or maintenance of actin cytoskeleton polarity Source: UniProtKB
  • glomerular filtration Source: Ensembl
  • glycerol transport Source: UniProtKB
  • hyperosmotic salinity response Source: Ensembl
  • lateral ventricle development Source: UniProtKB
  • lipid digestion Source: Ensembl
  • maintenance of symbiont-containing vacuole by host Source: UniProtKB
  • metanephric descending thin limb development Source: Ensembl
  • metanephric glomerulus vasculature development Source: Ensembl
  • metanephric proximal convoluted tubule segment 2 development Source: Ensembl
  • metanephric proximal straight tubule development Source: Ensembl
  • multicellular organismal water homeostasis Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  • nitric oxide transport Source: UniProtKB
  • odontogenesis Source: UniProtKB
  • pancreatic juice secretion Source: UniProtKB
  • positive regulation of angiogenesis Source: UniProtKB
  • positive regulation of epithelial cell migration Source: Ensembl
  • positive regulation of fibroblast proliferation Source: UniProtKB
  • positive regulation of lamellipodium assembly Source: Ensembl
  • positive regulation of saliva secretion Source: UniProtKB
  • potassium ion transmembrane transport Source: GOC
  • potassium ion transport Source: UniProtKB
  • renal water absorption Source: Ensembl
  • renal water homeostasis Source: Reactome
  • renal water transport Source: UniProtKB
  • response to drug Source: UniProtKB
  • response to estrogen Source: Ensembl
  • secretory granule organization Source: Ensembl
  • sensory perception of pain Source: Ensembl
  • small molecule metabolic process Source: Reactome
  • transepithelial water transport Source: UniProtKB
  • transmembrane transport Source: Reactome
  • water transport Source: UniProtKB
  • wound healing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Blood group antigen

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiREACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
REACT_23826. Passive transport by Aquaporins.
REACT_24023. Vasopressin regulates renal water homeostasis via Aquaporins.

Protein family/group databases

TCDBi1.A.8.8.1. the major intrinsic protein (mip) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Aquaporin-1
Short name:
AQP-1
Alternative name(s):
Aquaporin-CHIP
Urine water channel
Water channel protein for red blood cells and kidney proximal tubule
Gene namesi
Name:AQP1
Synonyms:CHIP28
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:633. AQP1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 76Cytoplasmic1 Publication
Transmembranei8 – 3629Helical; Name=Helix 1Add
BLAST
Topological domaini37 – 4812Extracellular1 PublicationAdd
BLAST
Transmembranei49 – 6618Helical; Name=Helix 2Add
BLAST
Topological domaini67 – 704Cytoplasmic1 Publication
Intramembranei71 – 766
Intramembranei77 – 848Helical; Name=Helix B
Topological domaini85 – 9410Cytoplasmic1 Publication
Transmembranei95 – 11521Helical; Name=Helix 3Add
BLAST
Topological domaini116 – 13621Extracellular1 PublicationAdd
BLAST
Transmembranei137 – 15519Helical; Name=Helix 4Add
BLAST
Topological domaini156 – 16611Cytoplasmic1 PublicationAdd
BLAST
Transmembranei167 – 18317Helical; Name=Helix 5Add
BLAST
Topological domaini184 – 1863Extracellular1 Publication
Intramembranei187 – 1926
Intramembranei193 – 2008Helical; Name=Helix E
Topological domaini201 – 2077Extracellular1 Publication
Transmembranei208 – 22821Helical; Name=Helix 6Add
BLAST
Topological domaini229 – 26941Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • apical part of cell Source: UniProtKB
  • apical plasma membrane Source: UniProtKB
  • axon terminus Source: Ensembl
  • basal plasma membrane Source: UniProtKB
  • basolateral plasma membrane Source: UniProtKB
  • brush border Source: UniProtKB
  • brush border membrane Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • nuclear membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • sarcolemma Source: UniProtKB
  • symbiont-containing vacuole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

MIMi110450. phenotype.
PharmGKBiPA24918.

Chemistry

DrugBankiDB00819. Acetazolamide.

Polymorphism and mutation databases

BioMutaiAQP1.
DMDMi267412.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 269268Aquaporin-1PRO_0000063920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...)
Glycosylationi205 – 2051N-linked (GlcNAc...)Sequence Analysis
Modified residuei262 – 2621PhosphoserineBy similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP29972.
PRIDEiP29972.

PTM databases

PhosphoSiteiP29972.

Expressioni

Tissue specificityi

Detected in erythrocytes (at protein level). Expressed in a number of tissues including erythrocytes, renal tubules, retinal pigment epithelium, heart, lung, skeletal muscle, kidney and pancreas. Weakly expressed in brain, placenta and liver.1 Publication

Gene expression databases

BgeeiP29972.
CleanExiHS_AQP1.
ExpressionAtlasiP29972. baseline and differential.
GenevisibleiP29972. HS.

Organism-specific databases

HPAiCAB001707.
HPA019206.

Interactioni

Subunit structurei

Homotetramer. Interacts with EPHB2; involved in endolymph production in the inner ear (By similarity). Identified in a complex with STOM.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC136Q96JN2-23EBI-745213,EBI-10171416
CCDC36Q8IYA83EBI-745213,EBI-8638439
CCDC57Q2TAC23EBI-745213,EBI-2808286
CEP44Q9C0F13EBI-745213,EBI-744115
CRTAC1Q9NQ793EBI-745213,EBI-10205543
CSRNP1Q96S653EBI-745213,EBI-4311573
FOSQ6FG413EBI-745213,EBI-10198738
FSD2A1L4K13EBI-745213,EBI-5661036
IKZF2Q9UKS73EBI-745213,EBI-3893057
IKZF3Q9UKT93EBI-745213,EBI-747204
KCTD9Q7L2733EBI-745213,EBI-4397613
KIAA1958Q8N8K93EBI-745213,EBI-10181113
KRT31Q153233EBI-745213,EBI-948001
KRT33BQ145253EBI-745213,EBI-1049638
KRT40Q6A1623EBI-745213,EBI-10171697
KRTAP10-7P604093EBI-745213,EBI-10172290
KRTAP4-2Q9BYR53EBI-745213,EBI-10172511
KRTAP9-2Q9BYQ43EBI-745213,EBI-1044640
MDFIQ997504EBI-745213,EBI-724076
MID2Q9UJV3-23EBI-745213,EBI-10172526
MTUS2Q5JR593EBI-745213,EBI-742948
NOTCH2NLQ7Z3S93EBI-745213,EBI-945833
RGS17Q9UGC63EBI-745213,EBI-3918154
RGS20O760813EBI-745213,EBI-1052678
RGS20O76081-63EBI-745213,EBI-10178530
RIMBP3Q9UFD93EBI-745213,EBI-10182375
SIAH1Q8IUQ43EBI-745213,EBI-747107
SPRY2O435973EBI-745213,EBI-742487
TCF4P158843EBI-745213,EBI-533224
TNK2Q079123EBI-745213,EBI-603457
TRAF1Q130773EBI-745213,EBI-359224
TRAF2Q129333EBI-745213,EBI-355744
TRIM23P364063EBI-745213,EBI-740098
TRIP6Q156544EBI-745213,EBI-742327

Protein-protein interaction databases

BioGridi106854. 41 interactions.
DIPiDIP-29607N.
IntActiP29972. 40 interactions.
MINTiMINT-1439356.
STRINGi9606.ENSP00000311165.

Structurei

Secondary structure

1
269
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 3227Combined sources
Beta strandi35 – 373Combined sources
Beta strandi39 – 435Combined sources
Helixi49 – 6719Combined sources
Turni68 – 703Combined sources
Helixi77 – 859Combined sources
Helixi93 – 11523Combined sources
Turni135 – 1384Combined sources
Helixi139 – 1424Combined sources
Turni143 – 1464Combined sources
Helixi147 – 1559Combined sources
Helixi168 – 1747Combined sources
Helixi176 – 1827Combined sources
Turni183 – 1864Combined sources
Helixi193 – 1975Combined sources
Beta strandi200 – 2034Combined sources
Turni207 – 2104Combined sources
Helixi211 – 2144Combined sources
Helixi217 – 22812Combined sources
Turni229 – 2313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FQYX-ray3.80A1-269[»]
1H6IX-ray3.54A1-269[»]
1IH5X-ray3.70A1-269[»]
4CSKX-ray3.28A1-269[»]
ProteinModelPortaliP29972.
SMRiP29972. Positions 3-235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29972.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi76 – 783NPA 1
Motifi192 – 1943NPA 2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi159 – 1624Poly-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

eggNOGiCOG0580.
GeneTreeiENSGT00760000119223.
HOGENOMiHOG000288286.
HOVERGENiHBG000312.
InParanoidiP29972.
KOiK09864.
OMAiFNNHWIF.
OrthoDBiEOG7N8ZWD.
PhylomeDBiP29972.
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]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P29972-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASEFKKKLF WRAVVAEFLA TTLFVFISIG SALGFKYPVG NNQTAVQDNV
60 70 80 90 100
KVSLAFGLSI ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS IFRALMYIIA
110 120 130 140 150
QCVGAIVATA ILSGITSSLT GNSLGRNDLA DGVNSGQGLG IEIIGTLQLV
160 170 180 190 200
LCVLATTDRR RRDLGGSAPL AIGLSVALGH LLAIDYTGCG INPARSFGSA
210 220 230 240 250
VITHNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDLTD RVKVWTSGQV
260
EEYDLDADDI NSRVEMKPK
Length:269
Mass (Da):28,526
Last modified:January 23, 2007 - v3
Checksum:iBA204D82FB26352E
GO
Isoform 2 (identifier: P29972-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: MASEFKKKLF...KYPVGNNQTA → MPGARPLPLV...LGRVGPGSRQ
     46-128: Missing.

Note: No experimental confirmation available.
Show »
Length:186
Mass (Da):19,956
Checksum:i5C132B4A21FCC8BC
GO
Isoform 3 (identifier: P29972-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-128: MASEFKKKLF...LTGNSLGRND → MFWTFGYEAV...LGRVGPGSRQ

Note: Gene prediction based on EST data.
Show »
Length:218
Mass (Da):23,425
Checksum:i409D14C5A0F352CE
GO
Isoform 4 (identifier: P29972-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MASEFKKKLFWRA → MQSGMGWNVLDFW
     14-128: Missing.

Note: Gene prediction based on EST data.
Show »
Length:154
Mass (Da):16,677
Checksum:i764FA0B49CB3B1FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451A → T in AAH22486 (PubMed:15489334).Curated

Polymorphismi

AQP1 is responsible for the Colton blood group system. Approximately 92% of Caucasians are Co(A+B-) (Ala-46), approximately 8% are Co(A+B+), and only 0.2% are Co(A-B+) (Val-46). Co(A-B-) which is very rare, is due to a complete absence of AQP1.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381P → L in Co(A-B-) antigen; non functional AQP1; red cells show low osmotic water permeability. 1 Publication
VAR_013279
Natural varianti45 – 451A → V in Co(A-B+) antigen. 2 Publications
Corresponds to variant rs28362692 [ dbSNP | Ensembl ].
VAR_004400
Natural varianti165 – 1651G → D.1 Publication
Corresponds to variant rs28362731 [ dbSNP | Ensembl ].
VAR_022318

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 128128MASEF…LGRND → MFWTFGYEAVSPAGPSHLFA SLLLGVLLTITFMPGARPLP LVLVPQNTLAWMQLDAKAPA HPRPLQLLGRVGPGSRQ in isoform 3. CuratedVSP_046679Add
BLAST
Alternative sequencei1 – 4545MASEF…NNQTA → MPGARPLPLVLVPQNTLAWM QLDAKAPAHPRPLQLLGRVG PGSRQ in isoform 2. 1 PublicationVSP_046109Add
BLAST
Alternative sequencei1 – 1313MASEF…LFWRA → MQSGMGWNVLDFW in isoform 4. CuratedVSP_046680Add
BLAST
Alternative sequencei14 – 128115Missing in isoform 4. CuratedVSP_046681Add
BLAST
Alternative sequencei46 – 12883Missing in isoform 2. 1 PublicationVSP_046110Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77829 mRNA. Translation: AAA58425.1.
U41517 mRNA. Translation: AAC50648.1.
U41518 mRNA. Translation: AAC50649.1.
S73482 mRNA. Translation: AAB31193.1.
AK309608 mRNA. No translation available.
AY953319 Genomic DNA. Translation: AAX24129.1.
AC004691 Genomic DNA. Translation: AAC16481.1.
AC005155 Genomic DNA. Translation: AAC23788.1.
AB451275 mRNA. Translation: BAG70089.1.
AB451402 mRNA. Translation: BAG70216.1.
CH471073 Genomic DNA. Translation: EAW93971.1.
BC022486 mRNA. Translation: AAH22486.1.
AF480415 Genomic DNA. Translation: AAL87136.1.
CCDSiCCDS5431.1. [P29972-1]
CCDS55096.1. [P29972-4]
CCDS55097.1. [P29972-3]
CCDS55098.1. [P29972-2]
PIRiA41616.
I52366.
RefSeqiNP_001171989.1. NM_001185060.1. [P29972-2]
NP_001171990.1. NM_001185061.1. [P29972-3]
NP_001171991.1. NM_001185062.1. [P29972-4]
NP_932766.1. NM_198098.2. [P29972-1]
UniGeneiHs.76152.

Genome annotation databases

EnsembliENST00000311813; ENSP00000311165; ENSG00000240583.
ENST00000409611; ENSP00000387178; ENSG00000240583. [P29972-3]
ENST00000409899; ENSP00000386712; ENSG00000240583. [P29972-4]
ENST00000441328; ENSP00000405698; ENSG00000240583. [P29972-2]
GeneIDi358.
KEGGihsa:358.
UCSCiuc003tbv.2. human. [P29972-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

dbRBC/BGMUT

Blood group antigen gene mutation database

SeattleSNPs
Protein Spotlight

Liquid states - Issue 36 of July 2003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M77829 mRNA. Translation: AAA58425.1.
U41517 mRNA. Translation: AAC50648.1.
U41518 mRNA. Translation: AAC50649.1.
S73482 mRNA. Translation: AAB31193.1.
AK309608 mRNA. No translation available.
AY953319 Genomic DNA. Translation: AAX24129.1.
AC004691 Genomic DNA. Translation: AAC16481.1.
AC005155 Genomic DNA. Translation: AAC23788.1.
AB451275 mRNA. Translation: BAG70089.1.
AB451402 mRNA. Translation: BAG70216.1.
CH471073 Genomic DNA. Translation: EAW93971.1.
BC022486 mRNA. Translation: AAH22486.1.
AF480415 Genomic DNA. Translation: AAL87136.1.
CCDSiCCDS5431.1. [P29972-1]
CCDS55096.1. [P29972-4]
CCDS55097.1. [P29972-3]
CCDS55098.1. [P29972-2]
PIRiA41616.
I52366.
RefSeqiNP_001171989.1. NM_001185060.1. [P29972-2]
NP_001171990.1. NM_001185061.1. [P29972-3]
NP_001171991.1. NM_001185062.1. [P29972-4]
NP_932766.1. NM_198098.2. [P29972-1]
UniGeneiHs.76152.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FQYX-ray3.80A1-269[»]
1H6IX-ray3.54A1-269[»]
1IH5X-ray3.70A1-269[»]
4CSKX-ray3.28A1-269[»]
ProteinModelPortaliP29972.
SMRiP29972. Positions 3-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106854. 41 interactions.
DIPiDIP-29607N.
IntActiP29972. 40 interactions.
MINTiMINT-1439356.
STRINGi9606.ENSP00000311165.

Chemistry

DrugBankiDB00819. Acetazolamide.
GuidetoPHARMACOLOGYi688.

Protein family/group databases

TCDBi1.A.8.8.1. the major intrinsic protein (mip) family.

PTM databases

PhosphoSiteiP29972.

Polymorphism and mutation databases

BioMutaiAQP1.
DMDMi267412.

Proteomic databases

PaxDbiP29972.
PRIDEiP29972.

Protocols and materials databases

DNASUi358.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000311813; ENSP00000311165; ENSG00000240583.
ENST00000409611; ENSP00000387178; ENSG00000240583. [P29972-3]
ENST00000409899; ENSP00000386712; ENSG00000240583. [P29972-4]
ENST00000441328; ENSP00000405698; ENSG00000240583. [P29972-2]
GeneIDi358.
KEGGihsa:358.
UCSCiuc003tbv.2. human. [P29972-1]

Organism-specific databases

CTDi358.
GeneCardsiGC07P030894.
HGNCiHGNC:633. AQP1.
HPAiCAB001707.
HPA019206.
MIMi107776. gene.
110450. phenotype.
neXtProtiNX_P29972.
PharmGKBiPA24918.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0580.
GeneTreeiENSGT00760000119223.
HOGENOMiHOG000288286.
HOVERGENiHBG000312.
InParanoidiP29972.
KOiK09864.
OMAiFNNHWIF.
OrthoDBiEOG7N8ZWD.
PhylomeDBiP29972.
TreeFamiTF312940.

Enzyme and pathway databases

ReactomeiREACT_121329. Erythrocytes take up carbon dioxide and release oxygen.
REACT_121380. Erythrocytes take up oxygen and release carbon dioxide.
REACT_23826. Passive transport by Aquaporins.
REACT_24023. Vasopressin regulates renal water homeostasis via Aquaporins.

Miscellaneous databases

ChiTaRSiAQP1. human.
EvolutionaryTraceiP29972.
GeneWikiiAquaporin_1.
GenomeRNAii358.
NextBioi1497.
PROiP29972.
SOURCEiSearch...

Gene expression databases

BgeeiP29972.
CleanExiHS_AQP1.
ExpressionAtlasiP29972. baseline and differential.
GenevisibleiP29972. HS.

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. "Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family."
    Preston G.M., Agre P.
    Proc. Natl. Acad. Sci. U.S.A. 88:11110-11114(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  2. "The human aquaporin-CHIP gene. Structure, organization, and chromosomal localization."
    Moon C., Preston G.M., Griffin C.A., Jabs E.W., Agre P.
    J. Biol. Chem. 268:15772-15778(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Characterization of the 3' UTR sequence encoded by the AQP-1 gene in human retinal pigment epithelium."
    Ruiz A.C., Bok D.
    Biochim. Biophys. Acta 1282:174-178(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Retinal pigment epithelium.
  4. "The water channel gene in human uterus."
    Li X., Yu H., Koide S.S.
    Biochem. Mol. Biol. Int. 32:371-377(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Uterus.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Mesangial cell.
  6. SeattleSNPs variation discovery resource
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-45 AND ASP-165.
  7. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  11. "Human chondrocytes in situ express aquaporin water channels: changes in AQP1 abundance in pathologies of articular cartilage."
    Trujillo E., Gonzalez T., Martin-Vasallo P., Marples D., Mobasheri A.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-269.
    Tissue: Articular cartilage.
  12. "Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins."
    Smith B.L., Agre P.
    J. Biol. Chem. 266:6407-6415(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-36.
  13. "Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein."
    Preston G.M., Carroll T.P., Guggino W.B., Agre P.
    Science 256:385-387(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel."
    Preston G.M., Jung J.S., Guggino W.B., Agre P.
    J. Biol. Chem. 268:17-20(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: TARGET OF MERCURY INHIBITION.
  15. "Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis."
    Preston G.M., Jung J.S., Guggino W.B., Agre P.
    J. Biol. Chem. 269:1668-1673(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY.
  16. "Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains."
    Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R.
    Biochim. Biophys. Acta 1828:956-966(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION IN A COMPLEX WITH STOM, SUBUNIT.
  17. "The three-dimensional structure of human erythrocyte aquaporin CHIP."
    Walz T., Smith B.L., Agre P., Engel A.
    EMBO J. 13:2985-2993(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (1.6 ANGSTROMS).
  18. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6 ANGSTROMS).
  19. "Structural determinants of water permeation through aquaporin-1."
    Murata K., Mitsuoka K., Hirai T., Walz T., Agre P., Heymann J.B., Engel A., Fujiyoshi Y.
    Nature 407:599-605(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.8 ANGSTROMS).
  20. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS).
  21. "Visualization of a water-selective pore by electron crystallography in vitreous ice."
    Ren G., Reddy V.S., Cheng A., Melnyk P., Mitra A.K.
    Proc. Natl. Acad. Sci. U.S.A. 98:1398-1403(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.7 ANGSTROMS).
  22. "Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens."
    Smith B.L., Preston G.M., Spring F., Anstee D.J., Agre P.
    J. Clin. Invest. 94:1043-1049(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT BLOOD GROUP COLTON VAL-45.
  23. "Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels."
    Preston G.M., Smith B.L., Zeidel M.L., Moulds J.J., Agre P.
    Science 265:1585-1587(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-38.

Entry informationi

Entry nameiAQP1_HUMAN
AccessioniPrimary (citable) accession number: P29972
Secondary accession number(s): B5BU39
, E7EM69, E9PC21, F5GY19, Q8TBI5, Q8TDC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 177 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Pharmacologically inhibited by submillimolar concentrations of mercury.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Blood group antigen proteins
    Nomenclature of blood group antigens and list of entries
  2. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  8. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.