ID AQP4_HUMAN STANDARD; PRT; 323 AA. AC P55087; P78564; DT 01-OCT-1996 (Rel. 34, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Aquaporin 4 (WCH4) (Mercurial-insensitive water channel) (MIWC). GN Name=AQP4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Fetal brain; RX MEDLINE=96032721; PubMed=7559426; DOI=10.1074/jbc.270.39.22907; RA Yang B., Ma T., Verkman A.S.; RT "cDNA cloning, gene organization, and chromosomal localization of a RT human mercurial insensitive water channel. Evidence for distinct RT transcriptional units."; RL J. Biol. Chem. 270:22907-22913(1995). RN [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=96176324; PubMed=8601457; DOI=10.1016/0014-5793(96)00092-0; RA Misaka T., Abe K., Iwabuchi K., Kusakabe Y., Ichinose M., Miki K., RA Emori Y., Arai S.; RT "A water channel closely related to rat brain aquaporin 4 is expressed RT in acid- and pepsinogen-secretory cells of human stomach."; RL FEBS Lett. 381:208-212(1996). RN [3] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=97008105; PubMed=8855281; DOI=10.1073/pnas.93.20.10908; RA Lu M., Lee M.D., Smith B.L., Jung J.S., Agre P., Verdijk M.A.J., RA Merkx G., Rijss J.P.L., Deen P.M.T.; RT "The human AQP4 gene: definition of the locus encoding two water RT channel polypeptides in brain."; RL Proc. Natl. Acad. Sci. U.S.A. 93:10908-10912(1996). RN [4] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Lung; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: Forms a water-specific channel. Osmoreceptor which CC regulates body water balance and mediates water flow within the CC central nervous system. CC -!- SUBCELLULAR LOCATION: Integral membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=2; CC IsoId=P55087-1; Sequence=Displayed; CC Name=1; CC IsoId=P55087-2; Sequence=VSP_003232; CC -!- TISSUE SPECIFICITY: Brain - muscle >> heart, kidney, lung, and CC trachea. CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing CC three membrane-spanning domains and a pore-forming loop with the CC signature motif Asn-Pro-Ala (NPA). CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U34846; AAC52112.1; ALT_INIT. DR EMBL; U34845; AAC50284.1; ALT_INIT. DR EMBL; D63412; BAA09715.1; -. DR EMBL; U63622; AAB26957.1; -. DR EMBL; U63623; AAB26958.1; -. DR EMBL; BC022286; AAH22286.1; -. DR PIR; I39178; I39178. DR HSSP; P29972; 1FQY. DR Genew; HGNC:637; AQP4. DR H-InvDB; HIX0014377; -. DR MIM; 600308; -. DR GO; GO:0005887; C:integral to plasma membrane; TAS. DR GO; GO:0005372; F:water transporter activity; TAS. DR GO; GO:0007588; P:excretion; TAS. DR GO; GO:0007399; P:neurogenesis; TAS. DR GO; GO:0006810; P:transport; TAS. DR InterPro; IPR000425; MIP. DR Pfam; PF00230; MIP; 1. DR PRINTS; PR00783; MINTRINSICP. DR ProDom; PD000295; MIP; 1. DR TIGRFAMs; TIGR00861; MIP; 1. DR PROSITE; PS00221; MIP; 1. KW Alternative splicing; Phosphorylation; Repeat; Transmembrane; KW Transport. FT DOMAIN 1 36 Cytoplasmic (Potential). FT TRANSMEM 37 57 Potential. FT DOMAIN 58 64 Extracellular (Potential). FT TRANSMEM 65 85 Potential. FT DOMAIN 86 115 Cytoplasmic (Potential). FT TRANSMEM 116 136 Potential. FT DOMAIN 137 155 Extracellular (Potential). FT TRANSMEM 156 176 Potential. FT DOMAIN 177 184 Cytoplasmic (Potential). FT TRANSMEM 185 205 Potential. FT DOMAIN 206 231 Extracellular (Potential). FT TRANSMEM 232 252 Potential. FT DOMAIN 253 323 Cytoplasmic (Potential). FT SITE 97 99 NPA 1. FT SITE 213 215 NPA 2. FT MOD_RES 285 285 Phosphoserine (By similarity). FT CARBOHYD 153 153 N-linked (GlcNAc...) (Potential). FT CARBOHYD 206 206 N-linked (GlcNAc...) (Potential). FT VARSPLIC 1 22 Missing (in isoform 1). FT /FTId=VSP_003232. FT CONFLICT 246 246 G -> A (in Ref. 1). FT CONFLICT 287 288 VE -> AK (in Ref. 1). FT CONFLICT 296 296 P -> L (in Ref. 1). SQ SEQUENCE 323 AA; 34830 MW; 1A1600CF0DC11052 CRC64; MSDRPTARRW GKCGPLCTRE NIMVAFKGVW TQAFWKAVTA EFLAMLIFVL LSLGSTINWG GTEKPLPVDM VLISLCFGLS IATMVQCFGH ISGGHINPAV TVAMVCTRKI SIAKSVFYIA AQCLGAIIGA GILYLVTPPS VVGGLGVTMV HGNLTAGHGL LVELIITFQL VFTIFASCDS KRTDVTGSIA LAIGFSVAIG HLFAINYTGA SMNPARSFGP AVIMGNWENH WIYWVGPIIG AVLAGGLYEY VFCPDVEFKR RFKEAFSKAA QQTKGSYMEV EDNRSQVETD DLILKPGVVH VIDVDRGEEK KGKDQSGEVL SSV //