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P29972 (AQP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:AQP1
Synonyms:CHIP28
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length269 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13

Subunit structure

Homotetramer. Interacts with EPHB2; involved in endolymph production in the inner ear By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

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.

Domain

Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).

Polymorphism

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.

Miscellaneous

Pharmacologically inhibited by submillimolar concentrations of mercury.

Sequence similarities

Belongs to the MIP/aquaporin (TC 1.A.8) family. [View classification]

Ontologies

Keywords
   Biological processTransport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Transmembrane
Transmembrane helix
   Molecular functionBlood group antigen
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Uncategorized?

Inferred from direct assay. Source: UniProtKB

   Biological_processammonium transport

Inferred from direct assay PubMed 16574458PubMed 19273840. Source: UniProtKB

bicarbonate transport

Traceable author statement. Source: Reactome

cGMP biosynthetic process

Inferred from direct assay PubMed 14561230. Source: UniProtKB

carbon dioxide transmembrane transport

Inferred from direct assay PubMed 17012249. Source: UniProtKB

carbon dioxide transport

Inferred from direct assay PubMed 12745312PubMed 16574458PubMed 19273840. Source: UniProtKB

cell volume homeostasis

Inferred from mutant phenotype PubMed 11922632. Source: UniProtKB

cellular homeostasis

Inferred from direct assay PubMed 19268465. Source: UniProtKB

cellular hyperosmotic response

Inferred from mutant phenotype PubMed 11922632. Source: UniProtKB

cellular response to UV

Inferred from direct assay PubMed 19424603. Source: UniProtKB

cellular response to cAMP

Inferred from direct assay PubMed 18538351. Source: UniProtKB

cellular response to copper ion

Inferred from direct assay PubMed 7491270PubMed 8584435. Source: UniProtKB

cellular response to dexamethasone stimulus

Inferred from direct assay PubMed 16711029. Source: UniProtKB

cellular response to hydrogen peroxide

Inferred from direct assay PubMed 19424603. Source: UniProtKB

cellular response to hypoxia

Inferred from direct assay PubMed 18275976. Source: UniProtKB

cellular response to inorganic substance

Inferred from direct assay PubMed 14561230. Source: UniProtKB

cellular response to mechanical stimulus

Inferred from direct assay PubMed 19268465. Source: UniProtKB

cellular response to mercury ion

Inferred from direct assay PubMed 12172703PubMed 12745312PubMed 7491270PubMed 8584435PubMed 9321919. Source: UniProtKB

cellular response to nitric oxide

Inferred from direct assay PubMed 14561230. Source: UniProtKB

cellular response to retinoic acid

Inferred from direct assay PubMed 12051745PubMed 19424603. Source: UniProtKB

cellular response to salt stress

Inferred from direct assay PubMed 18509662. Source: UniProtKB

cellular response to stress

Inferred from direct assay PubMed 19268465. Source: UniProtKB

cerebrospinal fluid secretion

Inferred from expression pattern PubMed 16814974. Source: UniProtKB

establishment or maintenance of actin cytoskeleton polarity

Inferred from mutant phenotype PubMed 19584911. Source: UniProtKB

glycerol transport

Inferred from direct assay PubMed 7491270PubMed 8584435. Source: UniProtKB

lateral ventricle development

Inferred from expression pattern PubMed 16133142. Source: UniProtKB

maintenance of symbiont-containing vacuole by host

Inferred from mutant phenotype PubMed 18665841. Source: UniProtKB

multicellular organismal water homeostasis

Inferred from expression pattern PubMed 17645239. Source: UniProtKB

negative regulation of apoptotic process

Inferred from direct assay PubMed 16565507. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 21215257. Source: UniProtKB

nitric oxide transport

Inferred from direct assay PubMed 16682607. Source: UniProtKB

odontogenesis

Inferred from expression pattern PubMed 12522663. Source: UniProtKB

pancreatic juice secretion

Inferred from expression pattern PubMed 12801959. Source: UniProtKB

positive regulation of angiogenesis

Inferred from mutant phenotype PubMed 18275976. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from direct assay PubMed 16565507. Source: UniProtKB

positive regulation of saliva secretion

Inferred from mutant phenotype PubMed 15727941PubMed 9096382. Source: UniProtKB

potassium ion transmembrane transport

Inferred from mutant phenotype PubMed 11914159. Source: GOC

potassium ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

renal water transport

Inferred from direct assay PubMed 9096382. Source: UniProtKB

response to drug

Inferred from direct assay PubMed 12172703. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

transepithelial water transport

Inferred from direct assay PubMed 12766090. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

water transport

Inferred from direct assay PubMed 11914159PubMed 12172703PubMed 12766090PubMed 14561230Ref.22PubMed 8576117PubMed 8584435PubMed 9321919. Source: UniProtKB

   Cellular_componentapical part of cell

Inferred from direct assay PubMed 14675051. Source: UniProtKB

apical plasma membrane

Inferred from direct assay PubMed 12766090PubMed 12801959PubMed 16133142PubMed 17890385PubMed 18617525PubMed 9013443PubMed 9096382. Source: UniProtKB

basal plasma membrane

Inferred from direct assay PubMed 17409744. Source: UniProtKB

basolateral plasma membrane

Inferred from direct assay PubMed 12766090PubMed 12801959PubMed 16133142PubMed 16814974PubMed 18617525PubMed 9013443PubMed 9096382. Source: UniProtKB

brush border

Inferred from direct assay PubMed 16133142PubMed 16814974. Source: UniProtKB

brush border membrane

Inferred from direct assay PubMed 9013443. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 16814974PubMed 17645239PubMed 18509662PubMed 19545896. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 15326289PubMed 19056867. Source: UniProt

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

nuclear membrane

Inferred from direct assay PubMed 17645239. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 17645239. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 12002613PubMed 12051745PubMed 14521551PubMed 17012249PubMed 17645239PubMed 18392839PubMed 18509662PubMed 19545896PubMed 19584911PubMed 7491270PubMed 9321919. Source: UniProtKB

sarcolemma

Inferred from direct assay PubMed 17409744. Source: UniProtKB

symbiont-containing vacuole

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncarbon dioxide transmembrane transporter activity

Inferred from direct assay PubMed 17012249. Source: UniProtKB

glycerol transmembrane transporter activity

Inferred from direct assay PubMed 7491270PubMed 8584435. Source: UniProtKB

intracellular cGMP activated cation channel activity

Inferred from direct assay PubMed 14561230. Source: UniProtKB

nitric oxide transmembrane transporter activity

Inferred from direct assay PubMed 16682607. Source: UniProtKB

potassium channel activity

Inferred from mutant phenotype PubMed 11914159. Source: UniProtKB

potassium ion transmembrane transporter activity

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane transporter activity

Inferred from direct assay PubMed 17012249. Source: UniProtKB

water channel activity

Inferred from direct assay PubMed 12801959. Source: UniProtKB

water transmembrane transporter activity

Inferred from direct assay PubMed 11914159PubMed 12172703PubMed 12766090PubMed 14561230Ref.22PubMed 8576117PubMed 8584435PubMed 9096382PubMed 9321919. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MDFIQ997504EBI-745213,EBI-724076

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P29972-1)

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.
Isoform 2 (identifier: P29972-2)

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.
Isoform 3 (identifier: P29972-3)

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.
Isoform 4 (identifier: P29972-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 269268Aquaporin-1
PRO_0000063920

Regions

Topological domain2 – 76Cytoplasmic Ref.15
Transmembrane8 – 3629Helical; Name=Helix 1
Topological domain37 – 4812Extracellular Ref.15
Transmembrane49 – 6618Helical; Name=Helix 2
Topological domain67 – 704Cytoplasmic Ref.15
Intramembrane71 – 766
Intramembrane77 – 848Helical; Name=Helix B
Topological domain85 – 9410Cytoplasmic Ref.15
Transmembrane95 – 11521Helical; Name=Helix 3
Topological domain116 – 13621Extracellular Ref.15
Transmembrane137 – 15519Helical; Name=Helix 4
Topological domain156 – 16611Cytoplasmic Ref.15
Transmembrane167 – 18317Helical; Name=Helix 5
Topological domain184 – 1863Extracellular Ref.15
Intramembrane187 – 1926
Intramembrane193 – 2008Helical; Name=Helix E
Topological domain201 – 2077Extracellular Ref.15
Transmembrane208 – 22821Helical; Name=Helix 6
Topological domain229 – 26941Cytoplasmic Ref.15
Motif76 – 783NPA 1
Motif192 – 1943NPA 2
Compositional bias159 – 1624Poly-Arg

Sites

Site561Substrate discrimination
Site1801Substrate discrimination
Site1891Hg(2+)-sensitive residue
Site1951Substrate discrimination

Amino acid modifications

Modified residue2621Phosphoserine By similarity
Glycosylation421N-linked (GlcNAc...)
Glycosylation2051N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 128128MASEF…LGRND → MFWTFGYEAVSPAGPSHLFA SLLLGVLLTITFMPGARPLP LVLVPQNTLAWMQLDAKAPA HPRPLQLLGRVGPGSRQ in isoform 3.
VSP_046679
Alternative sequence1 – 4545MASEF…NNQTA → MPGARPLPLVLVPQNTLAWM QLDAKAPAHPRPLQLLGRVG PGSRQ in isoform 2.
VSP_046109
Alternative sequence1 – 1313MASEF…LFWRA → MQSGMGWNVLDFW in isoform 4.
VSP_046680
Alternative sequence14 – 128115Missing in isoform 4.
VSP_046681
Alternative sequence46 – 12883Missing in isoform 2.
VSP_046110
Natural variant381P → L in Co(A-B-) antigen; non functional AQP1; red cells show low osmotic water permeability. Ref.22
VAR_013279
Natural variant451A → V in Co(A-B+) antigen. Ref.6 Ref.21
Corresponds to variant rs28362692 [ dbSNP | Ensembl ].
VAR_004400
Natural variant1651G → D. Ref.6
Corresponds to variant rs28362731 [ dbSNP | Ensembl ].
VAR_022318

Experimental info

Sequence conflict451A → T in AAH22486. Ref.10

Secondary structure

......................... 269
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: BA204D82FB26352E

FASTA26928,526
        10         20         30         40         50         60 
MASEFKKKLF WRAVVAEFLA TTLFVFISIG SALGFKYPVG NNQTAVQDNV KVSLAFGLSI 

        70         80         90        100        110        120 
ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS IFRALMYIIA QCVGAIVATA ILSGITSSLT 

       130        140        150        160        170        180 
GNSLGRNDLA DGVNSGQGLG IEIIGTLQLV LCVLATTDRR RRDLGGSAPL AIGLSVALGH 

       190        200        210        220        230        240 
LLAIDYTGCG INPARSFGSA VITHNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDLTD 

       250        260 
RVKVWTSGQV EEYDLDADDI NSRVEMKPK 

« Hide

Isoform 2 [UniParc].

Checksum: 5C132B4A21FCC8BC
Show »

FASTA18619,956
Isoform 3 [UniParc].

Checksum: 409D14C5A0F352CE
Show »

FASTA21823,425
Isoform 4 [UniParc].

Checksum: 764FA0B49CB3B1FE
Show »

FASTA15416,677

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"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).
[17]"The three-dimensional structure of aquaporin-1."
Walz T., Hirai T., Murata K., Heymann J.B., Mitsuoka K., Fujiyoshi Y., Smith B.L., Agre P., Engel A.
Nature 387:624-627(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6 ANGSTROMS).
[18]"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).
[19]"A refined structure of human aquaporin-1."
de Groot B.L., Engel A., Grubmueller H.
FEBS Lett. 504:206-211(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS).
[20]"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).
[21]"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.
[22]"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.
+Additional computationally mapped references.

Web resources

dbRBC/BGMUT

Blood group antigen gene mutation database

SeattleSNPs
Protein Spotlight

Liquid states - Issue 36 of July 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA41616.
I52366.
RefSeqNP_001171989.1. NM_001185060.1.
NP_001171990.1. NM_001185061.1.
NP_001171991.1. NM_001185062.1.
NP_932766.1. NM_198098.2.
UniGeneHs.76152.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FQYX-ray3.80A1-269[»]
1H6IX-ray3.54A1-269[»]
1IH5X-ray3.70A1-269[»]
ProteinModelPortalP29972.
SMRP29972. Positions 9-233.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106854. 7 interactions.
DIPDIP-29607N.
IntActP29972. 8 interactions.
MINTMINT-1439356.
STRING9606.ENSP00000311165.

Chemistry

DrugBankDB00819. Acetazolamide.
GuidetoPHARMACOLOGY688.

Protein family/group databases

TCDB1.A.8.8.1. the major intrinsic protein (mip) family.

PTM databases

PhosphoSiteP29972.

Polymorphism databases

DMDM267412.

Proteomic databases

PaxDbP29972.
PRIDEP29972.

Protocols and materials databases

DNASU358.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311813; ENSP00000311165; ENSG00000240583. [P29972-1]
ENST00000409611; ENSP00000387178; ENSG00000240583. [P29972-3]
ENST00000409899; ENSP00000386712; ENSG00000240583. [P29972-4]
ENST00000441328; ENSP00000405698; ENSG00000240583. [P29972-2]
GeneID358.
KEGGhsa:358.
UCSCuc003tbv.2. human. [P29972-1]

Organism-specific databases

CTD358.
GeneCardsGC07P030894.
HGNCHGNC:633. AQP1.
HPACAB001707.
HPA019206.
MIM107776. gene.
110450. phenotype.
neXtProtNX_P29972.
PharmGKBPA24918.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0580.
HOGENOMHOG000288286.
HOVERGENHBG000312.
InParanoidP29972.
KOK09864.
OMASALGFHY.
OrthoDBEOG7N8ZWD.
PhylomeDBP29972.
TreeFamTF312940.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP29972.
BgeeP29972.
CleanExHS_AQP1.
GenevestigatorP29972.

Family and domain databases

Gene3D1.20.1080.10. 1 hit.
InterProIPR023271. Aquaporin-like.
IPR023274. Aquaporin_1.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]
PANTHERPTHR19139. PTHR19139. 1 hit.
PfamPF00230. MIP. 1 hit.
[Graphical view]
PRINTSPR02013. AQUAPORIN1.
PR00783. MINTRINSICP.
SUPFAMSSF81338. SSF81338. 1 hit.
TIGRFAMsTIGR00861. MIP. 1 hit.
PROSITEPS00221. MIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP29972.
GeneWikiAquaporin_1.
GenomeRNAi358.
NextBio1497.
PROP29972.
SOURCESearch...

Entry information

Entry nameAQP1_HUMAN
AccessionPrimary (citable) accession number: P29972
Secondary accession number(s): B5BU39 expand/collapse secondary AC list , E7EM69, E9PC21, F5GY19, Q8TBI5, Q8TDC1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

Blood group antigen proteins

Nomenclature of blood group antigens and list of entries