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Accession Number: | P29972 |
Protein Name: | AQP1 or CHIP28 |
Length: | 269 |
Molecular Weight: | 28526.00 |
Species: | Homo sapiens (Human) [9606] |
Number of TMSs: | 6 |
Location1 / Topology2 / Orientation3: | Membrane1 / Multi-pass membrane protein2 |
Substrate | monoatomic monocation, potassium(1+), hydrogen peroxide, dinitrogen oxide, water, ammonia, dioxygen, carbon dioxide |
Cross database links:
DIP: | DIP-29607N |
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RefSeq: | NP_932766.1 |
Entrez Gene ID: | 358 |
Pfam: | PF00230 |
OMIM: |
107776 gene 110450 phenotype |
KEGG: | hsa:358 |
Gene Ontology
GO:0016324
C:apical plasma membrane
GO:0009925
C:basal plasma membrane
GO:0031526
C:brush border membrane
GO:0005737
C:cytoplasm
GO:0005887
C:integral to plasma membrane
GO:0031965
C:nuclear membrane
GO:0042383
C:sarcolemma
GO:0051739
F:ammonia transmembrane transporter activity
GO:0035379
F:carbon dioxide transmembrane transporter ac...
GO:0015168
F:glycerol transmembrane transporter activity
GO:0005223
F:intracellular cGMP activated cation channel...
GO:0030184
F:nitric oxide transmembrane transporter acti...
GO:0005267
F:potassium channel activity
GO:0015079
F:potassium ion transmembrane transporter act...
GO:0005515
F:protein binding
GO:0015250
F:water channel activity
GO:0015696
P:ammonium transport
GO:0035378
P:carbon dioxide transmembrane transport
GO:0006884
P:cell volume homeostasis
GO:0071474
P:cellular hyperosmotic response
GO:0071320
P:cellular response to cAMP
GO:0071280
P:cellular response to copper ion
GO:0071549
P:cellular response to dexamethasone stimulus
GO:0070301
P:cellular response to hydrogen peroxide
GO:0071456
P:cellular response to hypoxia
GO:0071260
P:cellular response to mechanical stimulus
GO:0071288
P:cellular response to mercury ion
GO:0071300
P:cellular response to retinoic acid
GO:0071472
P:cellular response to salt stress
GO:0034644
P:cellular response to UV
GO:0033326
P:cerebrospinal fluid secretion
GO:0006182
P:cGMP biosynthetic process
GO:0030950
P:establishment or maintenance of actin cytos...
GO:0015793
P:glycerol transport
GO:0021670
P:lateral ventricle development
GO:0050891
P:multicellular organismal water homeostasis
GO:0043066
P:negative regulation of apoptosis
GO:0030185
P:nitric oxide transport
GO:0042476
P:odontogenesis
GO:0030157
P:pancreatic juice secretion
GO:0045766
P:positive regulation of angiogenesis
GO:0048146
P:positive regulation of fibroblast prolifera...
GO:0046878
P:positive regulation of saliva secretion
GO:0006813
P:potassium ion transport
GO:0003097
P:renal water transport
GO:0042493
P:response to drug
GO:0035377
P:transepithelial water transport
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References (19)[1] “Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family.” Preston G.M.et.al. 1722319 [2] “The human aquaporin-CHIP gene. Structure, organization, and chromosomal localization.” Moon C.et.al. 8340403 [3] “Characterization of the 3' UTR sequence encoded by the AQP-1 gene in human retinal pigment epithelium.” Ruiz A.C.et.al. 8703970 [4] “The water channel gene in human uterus.” Li X.et.al. 7517253 [5] “Human protein factory for converting the transcriptome into an in vitro-expressed proteome.” Goshima N.et.al. 19054851 [6] “The DNA sequence of human chromosome 7.” Hillier L.W.et.al. 12853948 [7] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).” The MGC Project Teamet.al. 15489334 [8] “Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins.” Smith B.L.et.al. 2007592 [9] “Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein.” Preston G.M.et.al. 1373524 [10] “The mercury-sensitive residue at cysteine 189 in the CHIP28 water channel.” Preston G.M.et.al. 7677994 [11] “Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis.” Preston G.M.et.al. 7507481 [12] “Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.” Daub H.et.al. 18691976 [13] “The three-dimensional structure of human erythrocyte aquaporin CHIP.” Walz T.et.al. 7518771 [14] “The three-dimensional structure of aquaporin-1.” Walz T.et.al. 9177353 | |
Structure: | |
External Searches:
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Analyze:
Predict TMSs (Predict number of transmembrane segments) | ||||
FASTA formatted sequence |
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1: MASEFKKKLF WRAVVAEFLA TTLFVFISIG SALGFKYPVG NNQTAVQDNV KVSLAFGLSI 61: ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS IFRALMYIIA QCVGAIVATA ILSGITSSLT 121: GNSLGRNDLA DGVNSGQGLG IEIIGTLQLV LCVLATTDRR RRDLGGSAPL AIGLSVALGH 181: LLAIDYTGCG INPARSFGSA VITHNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDLTD 241: RVKVWTSGQV EEYDLDADDI NSRVEMKPK