summaryrefslogtreecommitdiff
path: root/Master/texmf-dist/doc/latex/textopo/AQP1.SP
diff options
context:
space:
mode:
Diffstat (limited to 'Master/texmf-dist/doc/latex/textopo/AQP1.SP')
-rw-r--r--Master/texmf-dist/doc/latex/textopo/AQP1.SP138
1 files changed, 138 insertions, 0 deletions
diff --git a/Master/texmf-dist/doc/latex/textopo/AQP1.SP b/Master/texmf-dist/doc/latex/textopo/AQP1.SP
new file mode 100644
index 00000000000..305b461f9e9
--- /dev/null
+++ b/Master/texmf-dist/doc/latex/textopo/AQP1.SP
@@ -0,0 +1,138 @@
+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
+//