ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P29972


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name AQP1_HUMAN
Primary accession number P29972
Secondary accession numbers Q8TBI5 Q8TDC1
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    June 10, 2008 (Entry version 99)
Name and origin of the protein
Protein name Aquaporin-1
Synonyms AQP-1
Aquaporin-CHIP
Water channel protein for red blood cells and kidney proximal tubule
Urine water channel
Gene name
Name: AQP1
Synonyms: CHIP28
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=1722319 [NCBI, ExPASy, EBI, Israel, Japan]
Preston G.M., Agre P.;
"Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family.";
Proc. Natl. Acad. Sci. U.S.A. 88:11110-11114(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8340403 [NCBI, ExPASy, EBI, Israel, Japan]
Moon C., Preston G.M., Griffin C.A., Jabs E.W., Agre P.;
"The human aquaporin-CHIP gene. Structure, organization, and chromosomal localization.";
J. Biol. Chem. 268:15772-15778(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Retinal pigment epithelium;
DOI=10.1016/0005-2736(96)00076-4; PubMed=8703970 [NCBI, ExPASy, EBI, Israel, Japan]
Ruiz A.C., Bok D.;
"Characterization of the 3' UTR sequence encoded by the AQP-1 gene in human retinal pigment epithelium.";
Biochim. Biophys. Acta 1282:174-178(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Uterus;
PubMed=7517253 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Yu H., Koide S.S.;
"The water channel gene in human uterus.";
Biochem. Mol. Biol. Int. 32:371-377(1994).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-45 AND ASP-165.
SeattleSNPs program for genomic applications;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE OF 5-269.
TISSUE=Articular cartilage;
Trujillo E., Gonzalez T., Martin-Vasallo P., Marples D., Mobasheri A.;
"Human chondrocytes in situ express aquaporin water channels: changes in AQP1 abundance in pathologies of articular cartilage.";
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[9]
PROTEIN SEQUENCE OF 2-36.
PubMed=2007592 [NCBI, ExPASy, EBI, Israel, Japan]
Smith B.L., Agre P.;
"Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins.";
J. Biol. Chem. 266:6407-6415(1991).
[10]
FUNCTION.
PubMed=1373524 [NCBI, ExPASy, EBI, Israel, Japan]
Preston G.M., Carroll T.P., Guggino W.B., Agre P.;
"Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein.";
Science 256:385-387(1992).
[11]
TARGET OF MERCURY INHIBITION.
PubMed=7677994 [NCBI, ExPASy, EBI, Israel, Japan]
Preston G.M., Jung J.S., Guggino W.B., Agre P.;
"The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel.";
J. Biol. Chem. 268:17-20(1993).
[12]
TOPOLOGY.
PubMed=7507481 [NCBI, ExPASy, EBI, Israel, Japan]
Preston G.M., Jung J.S., Guggino W.B., Agre P.;
"Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis.";
J. Biol. Chem. 269:1668-1673(1994).
[13]
STRUCTURE BY ELECTRON MICROSCOPY (1.6 ANGSTROMS).
PubMed=7518771 [NCBI, ExPASy, EBI, Israel, Japan]
Walz T., Smith B.L., Agre P., Engel A.;
"The three-dimensional structure of human erythrocyte aquaporin CHIP.";
EMBO J. 13:2985-2993(1994).
[14]
STRUCTURE BY ELECTRON MICROSCOPY (6 ANGSTROMS).
DOI=10.1038/42512; PubMed=9177353 [NCBI, ExPASy, EBI, Israel, Japan]
Walz T., Hirai T., Murata K., Heymann J.B., Mitsuoka K., Fujiyoshi Y., Smith B.L., Agre P., Engel A.;
"The three-dimensional structure of aquaporin-1.";
Nature 387:624-627(1997).
[15]
STRUCTURE BY ELECTRON MICROSCOPY (3.8 ANGSTROMS).
DOI=10.1038/35036519; PubMed=11034202 [NCBI, ExPASy, EBI, Israel, Japan]
Murata K., Mitsuoka K., Hirai T., Walz T., Agre P., Heymann J.B., Engel A., Fujiyoshi Y.;
"Structural determinants of water permeation through aquaporin-1.";
Nature 407:599-605(2000).
[16]
STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS).
DOI=10.1016/S0014-5793(01)02743-0; PubMed=11532455 [NCBI, ExPASy, EBI, Israel, Japan]
de Groot B.L., Engel A., Grubmueller H.;
"A refined structure of human aquaporin-1.";
FEBS Lett. 504:206-211(2001).
[17]
STRUCTURE BY ELECTRON MICROSCOPY (3.7 ANGSTROMS).
DOI=10.1073/pnas.041489198; PubMed=11171962 [NCBI, ExPASy, EBI, Israel, Japan]
Ren G., Reddy V.S., Cheng A., Melnyk P., Mitra A.K.;
"Visualization of a water-selective pore by electron crystallography in vitreous ice.";
Proc. Natl. Acad. Sci. U.S.A. 98:1398-1403(2001).
[18]
VARIANT BLOOD GROUP COLTON VAL-45.
PubMed=7521882 [NCBI, ExPASy, EBI, Israel, Japan]
Smith B.L., Preston G.M., Spring F., Anstee D.J., Agre P.;
"Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens.";
J. Clin. Invest. 94:1043-1049(1994).
[19]
VARIANT LEU-38.
PubMed=7521540 [NCBI, ExPASy, EBI, Israel, Japan]
Preston G.M., Smith B.L., Zeidel M.L., Moulds J.J., Agre P.;
"Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels.";
Science 265:1585-1587(1994).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M77829; AAA58425.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U41517; AAC50648.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U41518; AAC50649.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S73482; AAB31193.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004691; AAC16481.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005155; AAC23788.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY953319; AAX24129.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC022486; AAH22486.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF480415; AAL87136.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A41616; A41616.
I52366; I52366.
RefSeq NP_932766.1; -.
UniGene Hs.76152
3D structure databases
PDB
1FQY; EM; 3.80 A; A=1-269.[ExPASy / RCSB / EBI]
1H6I; EM; 3.54 A; A=1-269.[ExPASy / RCSB / EBI]
1IH5; EM; 3.70 A; A=1-269.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FQY; -.
1H6I; -.
1IH5; -.
SMR P29972; 1-247.
ModBase P29972.
PTM databases
PhosphoSite P29972; -.
Organism-specific databases
H-InvDB HIX0006573; -.
HGNC HGNC:633; AQP1.
GeneLynx AQP1; Homo sapiens.
GenAtlas AQP1.
HPA CAB001707; -.
MIM 107776; gene. [NCBI / EBI]
110450; phenotype. [NCBI / EBI]
PharmGKB PA24918; -.
GeneCards P29972.
Gene expression databases
ArrayExpress P29972; -.
CleanEx HS_AQP1; -.
GermOnline ENSG00000106125; Homo sapiens.
Ontologies
GO
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0005372; Molecular function: water transporter activity (traceable author statement from ProtInc).
GO:0007588; Biological process: excretion (traceable author statement from ProtInc).
GO:0006833; Biological process: water transport (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR012269; Aquaporin.
IPR000425; MIP.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1080.10; MIP; 1.
PANTHER PTHR19139; MIP; 1.
Pfam PF00230; MIP; 1.
Pfam graphical view of domain structure.
PRINTS PR00783; MINTRINSICP.
ProDom PD000295; MIP; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR00861; MIP; 1.
PROSITE PS00221; MIP; 1.
BLOCKS P29972.
Genome annotation databases
Ensembl ENSG00000106125; Homo sapiens. [Contig view]
GeneID 358; -.
KEGG hsa:358; -.
Phylogenomic databases
HOGENOM P29972; -.
HOVERGEN P29972; -.
Other
DrugBank DB00819; Acetazolamide.
SOURCE AQP1; Homo sapiens.
ProtoNet P29972.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Blood group antigen; Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Repeat; Transmembrane; Transport.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   269  268     Aquaporin-1. PRO_0000063920
TOPO_DOM   2     7  6     Cytoplasmic. 
TRANSMEM   8    36  29     Helix 1. 
TOPO_DOM   37    48  12     Extracellular. 
TRANSMEM   49    66  18     Helix 2. 
TOPO_DOM   67    70  4     Cytoplasmic. 
TOPO_DOM   71    76  6     In membrane. 
TRANSMEM   77    84  8     Helix B. 
TOPO_DOM   85    94  10     Cytoplasmic. 
TRANSMEM   95   115  21     Helix 3. 
TOPO_DOM   116   136  21     Extracellular. 
TRANSMEM   137   155  19     Helix 4. 
TOPO_DOM   156   166  11     Cytoplasmic. 
TRANSMEM   167   183  17     Helix 5. 
TOPO_DOM   184   186  3     Extracellular. 
TOPO_DOM   187   192  6     In membrane. 
TRANSMEM   193   200  8     Helix E. 
TOPO_DOM   201   207  7     Extracellular. 
TRANSMEM   208   228  21     Helix 6. 
TOPO_DOM   229   269  41     Cytoplasmic. 
MOTIF   76    78  3     NPA 1. 
MOTIF   192   194  3     NPA 2. 
COMPBIAS   159   162  4     Poly-Arg. 
SITE   56    56  1     Substrate discrimination. 
SITE   180   180  1     Substrate discrimination. 
SITE   189   189  1     Hg(2+)-sensitive residue. 
SITE   195   195  1     Substrate discrimination. 
MOD_RES   246   246        Phosphothreonine (By similarity). 
MOD_RES   247   247        Phosphoserine (By similarity). 
MOD_RES   262   262        Phosphoserine (By similarity). 
CARBOHYD   42    42        N-linked (GlcNAc...). 
CARBOHYD   205   205        N-linked (GlcNAc...) (Potential). 
VARIANT   38    38  1     P -> L (in Co(A-B-) antigen; non functional AQP1; red cells show low osmotic water permeability). VAR_013279 [3D]
VARIANT   45    45  1     A -> V (in Co(A-B+) antigen). VAR_004400 [3D]
VARIANT   165   165  1     G -> D. VAR_022318 [3D]
CONFLICT   45    45        A -> T (in Ref. 7; AAH22486). 
HELIX   8    35  28      
STRAND   37    42  6      
HELIX   48    65  18      
STRAND   68    71  4      
HELIX   76    83  8      
HELIX   94   114  21      
TURN   119   122  4      
STRAND   132   135  4      
HELIX   136   154  19      
HELIX   166   182  17      
TURN   183   185  3      
HELIX   192   199  8      
HELIX   207   227  21      
Sequence information
Length: 269 AA [This is the length of the unprocessed precursor] Molecular weight: 28526 Da [This is the MW of the unprocessed precursor] CRC64: BA204D82FB26352E [This is a checksum on the sequence]
        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 

P29972 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!