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ID AQP1_HUMAN STANDARD; PRT; 269 AA.
AC P29972;
DT 01-APR-1993 (Rel. 25, Created)
DT 01-APR-1993 (Rel. 25, Last sequence update)
DT 15-JUL-1998 (Rel. 36, Last annotation update)
DE AQUAPORIN-CHIP (WATER CHANNEL PROTEIN FOR RED BLOOD CELLS AND KIDNEY
DE PROXIMAL TUBULE) (AQUAPORIN 1) (URINE WATER CHANNEL).
GN AQP1 OR CHIP28.
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Mammalia;
OC Eutheria; Primates; Catarrhini; Hominidae; Homo.
RN [1]
RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE.
RX MEDLINE; 92107900.
RA PRESTON G.M., AGRE P.;
RT "Isolation of the cDNA for erythrocyte integral membrane protein of
RT 28 kilodaltons: member of an ancient channel family.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:11110-11114(1991).
RN [2]
RP SEQUENCE FROM N.A.
RX MEDLINE; 93340184.
RA MOON C., PRESTON G.M., GRIFFIN C.A., JABS E.W., AGRE P.;
RT "The human aquaporin-CHIP gene. Structure, organization, and
RT chromosomal localization.";
RL J. Biol. Chem. 268:15772-15778(1993).
RN [3]
RP SEQUENCE FROM N.A.
RC TISSUE=RETINA;
RA RUIZ A.C., BOK D.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP SEQUENCE FROM N.A.
RC TISSUE=UTERUS;
RX MEDLINE; 94290349.
RA LI X., YU H., KOIDE S.S.;
RT "The water channel gene in human uterus.";
RL Biochem. Mol. Biol. Int. 32:371-377(1994).
RN [5]
RP FUNCTION.
RX MEDLINE; 92229472.
RA PRESTON G.M., CARROLL T.P., GUGGINO W.B., AGRE P.;
RT "Appearance of water channels in Xenopus oocytes expressing red cell
RT CHIP28 protein.";
RL Science 256:385-387(1992).
RN [6]
RP TARGET OF MERCURY INHIBITION.
RX MEDLINE; 93106996.
RA PRESTON G.M., JUNG J.S., GUGGINO W.B., AGRE P.;
RT "The mercury-sensitive residue at cysteine 189 in the CHIP28 water
RT channel.";
RL J. Biol. Chem. 268:17-20(1993).
RN [7]
RP TOPOLOGY.
RX MEDLINE; 94124503.
RA PRESTON G.M., JUNG J.S., GUGGINO W.B., AGRE P.;
RT "Membrane topology of aquaporin CHIP. Analysis of functional epitope-
RT scanning mutants by vectorial proteolysis.";
RL J. Biol. Chem. 269:1668-1673(1994).
RN [8]
RP STRUCTURE BY ELECTRON CRYO-MICROSCOPY.
RX MEDLINE; 94313979.
RA WALZ T., SMITH B.L., AGRE P., ENGEL A.;
RT "The three-dimensional structure of human erythrocyte aquaporin
RT CHIP.";
RL EMBO J. 13:2985-2993(1994).
RN [9]
RP STRUCTURE BY ELECTRON CRYO-MICROSCOPY.
RX MEDLINE; 97320502.
RA WALZ T., HIRAI T., MURATA K., HEYMANN J.B., MITSUOKA K.,
RA FUJIYOSHI Y., SMITH B.L., AGRE P., ENGEL A.;
RT "The three-dimensional structure of aquaporin-1.";
RL Nature 387:624-627(1997).
RN [10]
RP VARIANT BLOOD GROUP COLTON.
RX MEDLINE; 94365170.
RA SMITH B.L., PRESTON G.M., SPRING F., ANSTEE D.J., AGRE P.;
RT "Human red cell aquaporin CHIP. I. Molecular characterization of ABH
RT and Colton blood group antigens.";
RL J. Clin. Invest. 94:1043-1049(1994).
CC -!- FUNCTION: FORMS A WATER-SPECIFIC CHANNEL THAT PROVIDES THE PLASMA
CC MEMBRANES OF RED CELLS AND KIDNEY PROXIMAL TUBULES WITH HIGH
CC PERMEABILITY TO WATER, THEREBY PERMITTING WATER TO MOVE IN THE
CC DIRECTION OF AN OSMOTIC GRADIENT.
CC -!- SUBUNIT: HOMOTETRAMER.
CC -!- SUBCELLULAR LOCATION: INTEGRAL MEMBRANE PROTEIN.
CC -!- TISSUE SPECIFICITY: ERYTHROCYTES AND RENAL TUBULES.
CC -!- POLYMORPHISM: AQP1 IS RESPONSIBLE FOR THE COLTON BLOOD GROUP
CC SYSTEM. APPROXIMATELY 92% OF CAUCASIANS ARE CO(A+B-) (ALA-45),
CC APPROXIMATELY 8% ARE CO(A+B+), AND ONLY 0.2% ARE CO(A-B+) (VAL-
CC 45). CO(A-B-) WHICH IS VERY RARE, IS DUE TO A COMPLETE ABSENCE OF
CC AQP1.
CC -!- MISCELLANEOUS: PHARMACOLOGICALLY INHIBITED BY SUBMILLIMOLAR
CC CONCENTRATIONS OF HG2+.
CC -!- SIMILARITY: BELONGS TO THE TRANSMEMBRANE CHANNEL MIP FAMILY.
CC --------------------------------------------------------------------------
CC This SWISS-PROT entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use by non-profit institutions as long as its content is in no way
CC modified and this statement is not removed. Usage by and for commercial
CC entities requires a license agreement (See http://www.isb-sib.ch/announce/
CC or send an email to license@isb-sib.ch).
CC --------------------------------------------------------------------------
DR EMBL; M77829; AAA58425.1; -.
DR EMBL; U41517; AAC50648.1; -.
DR EMBL; S73482; AAB31193.1; -.
DR PIR; A41616; A41616.
DR MIM; 107776; -.
DR MIM; 110450; -.
DR PFAM; PF00230; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
KW Transport; Transmembrane; Polymorphism; Blood group antigen.
FT DOMAIN 1 14 CYTOPLASMIC (POTENTIAL).
FT TRANSMEM 18 35 POTENTIAL.
FT DOMAIN 36 48 EXTRACELLULAR (POTENTIAL).
FT TRANSMEM 49 67 POTENTIAL.
FT DOMAIN 68 93 CYTOPLASMIC (POTENTIAL).
FT TRANSMEM 94 115 POTENTIAL.
FT DOMAIN 116 135 EXTRACELLULAR (POTENTIAL).
FT TRANSMEM 136 156 POTENTIAL.
FT DOMAIN 157 164 CYTOPLASMIC (POTENTIAL).
FT TRANSMEM 165 184 POTENTIAL.
FT DOMAIN 185 210 EXTRACELLULAR (POTENTIAL).
FT TRANSMEM 211 232 POTENTIAL.
FT DOMAIN 233 269 CYTOPLASMIC (POTENTIAL).
FT SITE 189 189 HG(2+)-SENSITIVE RESIDUE.
FT DOMAIN 159 162 POLY-ARG.
FT CARBOHYD 42 42 POTENTIAL.
FT CARBOHYD 205 205 POTENTIAL.
FT VARIANT 45 45 A -> V (IN CO(A-B+) ANTIGEN).
FT /FTId=VAR_004400.
SQ SEQUENCE 269 AA; 28526 MW; 8063A7AD CRC32;
MASEFKKKLF WRAVVAEFLA TTLFVFISIG SALGFKYPVG NNQTAVQDNV KVSLAFGLSI
ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS IFRALMYIIA QCVGAIVATA ILSGITSSLT
GNSLGRNDLA DGVNSGQGLG IEIIGTLQLV LCVLATTDRR RRDLGGSAPL AIGLSVALGH
LLAIDYTGCG INPARSFGSA VITHNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDLTD
RVKVWTSGQV EEYDLDADDI NSRVEMKPK
//
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