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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 +// |