P29972 (AQP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	AQP1
Synonyms:	CHIP28

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	269 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Transport
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Transmembrane Transmembrane helix
Molecular function	Blood group antigen
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ammonium 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 cell volume homeostasis Inferred from mutant phenotype PubMed 11922632. 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 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 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 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 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 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 renal water transport Inferred from direct assay PubMed 9096382. Source: UniProtKB response to drug Inferred from direct assay PubMed 12172703. Source: UniProtKB transepithelial water transport Inferred from direct assay PubMed 12766090. Source: UniProtKB
Cellular_component	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 brush border membrane Inferred from direct assay PubMed 9013443. Source: UniProtKB cytoplasm Inferred from direct assay PubMed 16814974PubMed 17645239PubMed 18509662PubMed 19545896. Source: UniProtKB integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc nuclear membrane Inferred from direct assay PubMed 17645239. Source: UniProtKB sarcolemma Inferred from direct assay PubMed 17409744. Source: UniProtKB symbiont-containing vacuole Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	ammonia transmembrane transporter activity Inferred from direct assay PubMed 19273840. Source: UniProtKB carbon 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 water channel activity Inferred from direct assay PubMed 12801959. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MDFI	Q99750	4	EBI-745213,EBI-724076

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.12

Chain

2 – 269

268

Aquaporin-1

PRO_0000063920

Regions

Topological domain

2 – 7

6

Cytoplasmic Ref.15

Transmembrane

8 – 36

29

Helical; Name=Helix 1

Topological domain

37 – 48

12

Extracellular Ref.15

Transmembrane

49 – 66

18

Helical; Name=Helix 2

Topological domain

67 – 70

4

Cytoplasmic Ref.15

Intramembrane

71 – 76

6

Intramembrane

77 – 84

8

Helical; Name=Helix B

Topological domain

85 – 94

10

Cytoplasmic Ref.15

Transmembrane

95 – 115

21

Helical; Name=Helix 3

Topological domain

116 – 136

21

Extracellular Ref.15

Transmembrane

137 – 155

19

Helical; Name=Helix 4

Topological domain

156 – 166

11

Cytoplasmic Ref.15

Transmembrane

167 – 183

17

Helical; Name=Helix 5

Topological domain

184 – 186

3

Extracellular Ref.15

Intramembrane

187 – 192

6

Intramembrane

193 – 200

8

Helical; Name=Helix E

Topological domain

201 – 207

7

Extracellular Ref.15

Transmembrane

208 – 228

21

Helical; Name=Helix 6

Topological domain

229 – 269

41

Cytoplasmic Ref.15

Motif

76 – 78

3

NPA 1

Motif

192 – 194

3

NPA 2

Compositional bias

159 – 162

4

Poly-Arg

Sites

Site

56

1

Substrate discrimination

Site

180

1

Substrate discrimination

Site

189

1

Hg(2+)-sensitive residue

Site

195

1

Substrate discrimination

Amino acid modifications

Modified residue

246

1

Phosphothreonine By similarity

Modified residue

247

1

Phosphoserine By similarity

Modified residue

262

1

Phosphoserine By similarity

Glycosylation

42

1

N-linked (GlcNAc...)

Glycosylation

205

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

1 – 45

45

MASEF…NNQTA → MPGARPLPLVLVPQNTLAWM QLDAKAPAHPRPLQLLGRVG PGSRQ in isoform 2.

VSP_046109

Alternative sequence

46 – 128

83

Missing in isoform 2.

VSP_046110

Natural variant

38

1

P → L in Co(A-B-) antigen; non functional AQP1; red cells show low osmotic water permeability. Ref.22

VAR_013279

Natural variant

45

1

A → V in Co(A-B+) antigen. Ref.6 Ref.21
Corresponds to variant rs28362692 [ dbSNP | Ensembl ].

VAR_004400

Natural variant

165

1

G → D. Ref.6
Corresponds to variant rs28362731 [ dbSNP | Ensembl ].

VAR_022318

Experimental info

Sequence conflict

45

1

A → T in AAH22486. Ref.10

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

269

Helix Strand Turn

Details...

Helix

8 – 35

28

Beta strand

37 – 42

6

Helix

48 – 65

18

Beta strand

68 – 71

4

Helix

76 – 83

8

Helix

94 – 114

21

Turn

119 – 122

4

Beta strand

132 – 135

4

Helix

136 – 154

19

Helix

166 – 182

17

Turn

183 – 185

3

Helix

192 – 199

8

Helix

207 – 227

21

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: BA204D82FB26352E	FASTA	269	28,526
	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
	Isoform 2 [UniParc]. Checksum: 5C132B4A21FCC8BC	FASTA	186	19,956
	10 20 30 40 50 60 MPGARPLPLV LVPQNTLAWM QLDAKAPAHP RPLQLLGRVG PGSRQLADGV NSGQGLGIEI 70 80 90 100 110 120 IGTLQLVLCV LATTDRRRRD LGGSAPLAIG LSVALGHLLA IDYTGCGINP ARSFGSAVIT 130 140 150 160 170 180 HNFSNHWIFW VGPFIGGALA VLIYDFILAP RSSDLTDRVK VWTSGQVEEY DLDADDINSR VEMKPK

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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.

IPI

IPI00024689.
IPI00979161.

PIR

A41616.
I52366.

RefSeq

NP_001171989.1. NM_001185060.1.
NP_932766.1. NM_198098.2.

UniGene

Hs.76152.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FQY	X-ray	3.80	A	1-269	[»]
1H6I	X-ray	3.54	A	1-269	[»]
1IH5	X-ray	3.70	A	1-269	[»]

ProteinModelPortal

P29972.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29607N.

IntAct

P29972. 7 interactions.

MINT

MINT-1439356.

STRING

9606.ENSP00000311165.

Protein family/group databases

TCDB

1.A.8.8.1. major intrinsic protein (MIP) family.

PTM databases

PhosphoSite

P29972.

Polymorphism databases

DMDM

267412.

Proteomic databases

PaxDb

P29972.

PRIDE

P29972.

Protocols and materials databases

DNASU

358.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000311813; ENSP00000311165; ENSG00000240583.
ENST00000441328; ENSP00000405698; ENSG00000240583.

GeneID

358.

KEGG

hsa:358.

UCSC

uc003tbv.2. human.

Organism-specific databases

CTD

358.

GeneCards

GC07P030894.

HGNC

HGNC:633. AQP1.

HPA

CAB001707.
HPA019206.

MIM

107776. gene.
110450. phenotype.

neXtProt

NX_P29972.

PharmGKB

PA24918.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0580.

HOGENOM

HOG000288286.

HOVERGEN

HBG000312.

InParanoid

P29972.

KO

K09864.

OMA

GAAQDNV.

OrthoDB

EOG46T328.

PhylomeDB

P29972.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpress

P29972.

Bgee

P29972.

CleanEx

HS_AQP1.

Genevestigator

P29972.

GermOnline

ENSG00000106125. Homo sapiens.

Family and domain databases

Gene3D

1.20.1080.10. 1 hit.

InterPro

IPR023271. Aquaporin-like.
IPR023274. Aquaporin_1.
IPR000425. MIP.
IPR022357. MIP_CS.
[Graphical view]

PANTHER

PTHR19139. PTHR19139. 1 hit.

Pfam

PF00230. MIP. 1 hit.
[Graphical view]

PRINTS

PR02013. AQUAPORIN1.
PR00783. MINTRINSICP.

SUPFAM

SSF81338. MIP. 1 hit.

TIGRFAMs

TIGR00861. MIP. 1 hit.

PROSITE

PS00221. MIP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00819. Acetazolamide.

EvolutionaryTrace

P29972.

GenomeRNAi

358.

NextBio

1497.

SOURCE

Search...

Entry information

Entry name

AQP1_HUMAN

Accession

Primary (citable) accession number: P29972
Secondary accession number(s): B5BU39 , F5GY19, Q8TBI5, Q8TDC1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 151 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.