Q02013 (AQP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aquaporin-1
Short name=AQP-1

Alternative name(s):
Aquaporin-CHIP
Delayed early response protein 2
Short name=DER2
Water channel protein for red blood cells and kidney proximal tubule

Gene names

Name:

Aqp1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.
Subunit structure	Homotetramer By similarity. Interacts with EPHB2; involved in endolymph production in the inner ear. Ref.4
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Erythrocytes and renal tubules.
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).
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
Domain	Repeat Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ammonium transport Inferred from sequence or structural similarity. Source: UniProtKB cGMP biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB camera-type eye morphogenesis Inferred from mutant phenotype PubMed 11891232. Source: MGI cell volume homeostasis Inferred from sequence or structural similarity. Source: UniProtKB cellular hyperosmotic response Inferred from sequence or structural similarity. Source: UniProtKB cellular response to UV Inferred from sequence or structural similarity. Source: UniProtKB cellular response to cAMP Inferred from sequence or structural similarity. Source: UniProtKB cellular response to copper ion Inferred from sequence or structural similarity. Source: UniProtKB cellular response to dexamethasone stimulus Inferred from sequence or structural similarity. Source: UniProtKB cellular response to hydrogen peroxide Inferred from sequence or structural similarity. Source: UniProtKB cellular response to hypoxia Inferred from sequence or structural similarity. Source: UniProtKB cellular response to mechanical stimulus Inferred from sequence or structural similarity. Source: UniProtKB cellular response to mercury ion Inferred from sequence or structural similarity. Source: UniProtKB cellular response to retinoic acid Inferred from sequence or structural similarity. Source: UniProtKB cellular response to salt stress Inferred from sequence or structural similarity. Source: UniProtKB corticotropin secretion Inferred from mutant phenotype PubMed 18511498. Source: MGI establishment or maintenance of actin cytoskeleton polarity Inferred from sequence or structural similarity. Source: UniProtKB glomerular filtration Inferred from mutant phenotype PubMed 15283758. Source: MGI hyperosmotic salinity response Inferred from electronic annotation. Source: Compara lateral ventricle development Inferred from expression pattern PubMed 16133142. Source: UniProtKB lipid digestion Inferred from mutant phenotype PubMed 11121384. Source: MGI maintenance of symbiont-containing vacuole by host Inferred from mutant phenotype PubMed 18665841. Source: UniProtKB metanephric descending thin limb development Inferred from expression pattern PubMed 18618131. Source: UniProtKB metanephric glomerulus vasculature development Inferred from expression pattern PubMed 18618131. Source: UniProtKB metanephric proximal convoluted tubule segment 2 development Inferred from expression pattern PubMed 18618131. Source: UniProtKB metanephric proximal straight tubule development Inferred from expression pattern PubMed 18618131. Source: UniProtKB negative regulation of apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of angiogenesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell migration Inferred from mutant phenotype PubMed 19298815. Source: MGI positive regulation of epithelial cell migration Inferred from electronic annotation. Source: Compara positive regulation of fibroblast proliferation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of lamellipodium assembly Inferred from electronic annotation. Source: Compara positive regulation of saliva secretion Inferred from sequence or structural similarity. Source: UniProtKB renal water absorption Inferred from mutant phenotype PubMed 10021457PubMed 10662735PubMed 10724035PubMed 10795927PubMed 11035042PubMed 12133842PubMed 16525162PubMed 9468475. Source: MGI response to drug Inferred from sequence or structural similarity. Source: UniProtKB response to estrogen stimulus Inferred from electronic annotation. Source: Compara secretory granule organization Inferred from mutant phenotype PubMed 18511498. Source: MGI sensory perception of pain Inferred from mutant phenotype PubMed 16476579. Source: MGI transepithelial water transport Inferred from sequence or structural similarity. Source: UniProtKB wound healing Inferred from mutant phenotype PubMed 19298815. Source: MGI
Cellular_component	apical plasma membrane Inferred from direct assay PubMed 16133142. Source: UniProtKB axon part Inferred from direct assay PubMed 17257750. Source: MGI axon terminus Inferred from electronic annotation. Source: Compara basal plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB brush border membrane Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB extracellular vesicular exosome Inferred from direct assay PubMed 19724054. Source: MGI integral to plasma membrane Traceable author statement PubMed 11066060. Source: MGI neuronal cell body membrane Inferred from electronic annotation. Source: Compara nuclear membrane Inferred from sequence or structural similarity. Source: UniProtKB sarcolemma Inferred from sequence or structural similarity. Source: UniProtKB symbiont-containing vacuole Inferred from direct assay PubMed 18665841. Source: UniProtKB
Molecular_function	ammonia transmembrane transporter activity Inferred from sequence or structural similarity. Source: UniProtKB carbon dioxide transmembrane transporter activity Inferred from sequence or structural similarity. Source: UniProtKB glycerol transmembrane transporter activity Inferred from sequence or structural similarity. Source: UniProtKB intracellular cGMP activated cation channel activity Inferred from sequence or structural similarity. Source: UniProtKB nitric oxide transmembrane transporter activity Inferred from sequence or structural similarity. Source: UniProtKB potassium channel activity Inferred from sequence or structural similarity. Source: UniProtKB water channel activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 269	268	Aquaporin-1		PRO_0000063921
Regions
	Topological domain	2 – 7	6	Cytoplasmic By similarity
	Transmembrane	8 – 36	29	Helical; Name=Helix 1; By similarity
	Topological domain	37 – 48	12	Extracellular By similarity
	Transmembrane	49 – 66	18	Helical; Name=Helix 2; By similarity
	Topological domain	67 – 70	4	Cytoplasmic By similarity
	Intramembrane	71 – 76	6	By similarity
	Intramembrane	77 – 84	8	Helical; Name=Helix B; By similarity
	Topological domain	85 – 94	10	Cytoplasmic By similarity
	Transmembrane	95 – 115	21	Helical; Name=Helix 3; By similarity
	Topological domain	116 – 136	21	Extracellular By similarity
	Transmembrane	137 – 155	19	Helical; Name=Helix 4; By similarity
	Topological domain	156 – 166	11	Cytoplasmic By similarity
	Transmembrane	167 – 183	17	Helical; Name=Helix 5; By similarity
	Topological domain	184 – 186	3	Extracellular By similarity
	Intramembrane	187 – 192	6	By similarity
	Intramembrane	193 – 200	8	Helical; Name=Helix E; By similarity
	Topological domain	201 – 207	7	Extracellular By similarity
	Transmembrane	208 – 228	21	Helical; Name=Helix 6; By similarity
	Topological domain	229 – 269	41	Cytoplasmic By similarity
	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 By similarity
	Site	180	1	Substrate discrimination By similarity
	Site	189	1	Hg(2+)-sensitive residue By similarity
	Site	195	1	Substrate discrimination By similarity
Amino acid modifications
	Modified residue	246	1	Phosphothreonine Ref.6
	Modified residue	247	1	Phosphoserine Ref.6
	Modified residue	262	1	Phosphoserine Ref.5
	Glycosylation	205	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	190	1	G → S in AAH07125. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q02013 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F0499724AD4AB5F6	FASTA	269	28,793
	10 20 30 40 50 60 MASEIKKKLF WRAVVAEFLA MTLFVFISIG SALGFNYPLE RNQTLVQDNV KVSLAFGLSI 70 80 90 100 110 120 ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS ILRAVMYIIA QCVGAIVATA ILSGITSSLV 130 140 150 160 170 180 DNSLGRNDLA HGVNSGQGLG IEIIGTLQLV LCVLATTDRR RRDLGGSAPL AIGLSVALGH 190 200 210 220 230 240 LLAIDYTGCG INPARSFGSA VLTRNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDFTD 250 260 RMKVWTSGQV EEYDLDADDI NSRVEMKPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Growth factor-induced delayed early response genes." Lanahan A.A., Williams J.B., Sanders L.K., Nathans D. Mol. Cell. Biol. 12:3919-3929(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Head, Inner ear and Spleen.
[3]	"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]. Tissue: Mammary tumor.
[4]	"EphB2 guides axons at the midline and is necessary for normal vestibular function." Cowan C.A., Yokoyama N., Bianchi L.M., Henkemeyer M., Fritzsch B. Neuron 26:417-430(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EPHB2.
[5]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, MASS SPECTROMETRY. Tissue: Liver.
[6]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246 AND SER-247, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L02914 mRNA. Translation: AAB53928.1. AK081886 mRNA. Translation: BAC38360.1. AK086688 mRNA. Translation: BAC39719.1. AK157333 mRNA. Translation: BAE34051.1. AK158226 mRNA. Translation: BAE34412.1. AK158389 mRNA. Translation: BAE34482.1. AK171627 mRNA. Translation: BAE42573.1. AK172361 mRNA. Translation: BAE42966.1. BC007125 mRNA. Translation: AAH07125.1.
IPI	IPI00123183.
PIR	B44499.
RefSeq	NP_031498.1. NM_007472.2.
UniGene	Mm.18625.
3D structure databases
ProteinModelPortal	Q02013.
SMR	Q02013. Positions 9-233.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4088080.
PTM databases
PhosphoSite	Q02013.
Proteomic databases
PaxDb	Q02013.
PRIDE	Q02013.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000004774; ENSMUSP00000004774; ENSMUSG00000004655.
GeneID	11826.
KEGG	mmu:11826.
UCSC	uc009caq.1. mouse.
Organism-specific databases
CTD	358.
MGI	MGI:103201. Aqp1.
Phylogenomic databases
eggNOG	COG0580.
GeneTree	ENSGT00550000074347.
HOGENOM	HOG000288286.
HOVERGEN	HBG000312.
InParanoid	Q02013.
KO	K09864.
OMA	GAAQDNV.
OrthoDB	EOG46T328.
Gene expression databases
Bgee	Q02013.
CleanEx	MM_AQP1.
Genevestigator	Q02013.
GermOnline	ENSMUSG00000004655. Mus musculus.
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
ChiTaRS	AQP1. mouse.
NextBio	279727.
SOURCE	Search...

Entry information

Entry name

AQP1_MOUSE

Accession

Primary (citable) accession number: Q02013
Secondary accession number(s): Q542P1, Q91VY8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program