AQP1_HUMAN
ID AQP1_HUMAN Reviewed; 269 AA.
AC P29972; B5BU39; E7EM69; E9PC21; F5GY19; Q8TBI5; Q8TDC1;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=Aquaporin-1;
DE Short=AQP-1;
DE AltName: Full=Aquaporin-CHIP;
DE AltName: Full=Urine water channel;
DE AltName: Full=Water channel protein for red blood cells and kidney proximal tubule;
GN Name=AQP1; Synonyms=CHIP28;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1722319; DOI=10.1073/pnas.88.24.11110;
RA Preston G.M., Agre P.;
RT "Isolation of the cDNA for erythrocyte integral membrane protein of 28
RT kilodaltons: member of an ancient channel family.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:11110-11114(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8340403; DOI=10.1016/s0021-9258(18)82322-5;
RA Moon C., Preston G.M., Griffin C.A., Jabs E.W., Agre P.;
RT "The human aquaporin-CHIP gene. Structure, organization, and chromosomal
RT localization.";
RL J. Biol. Chem. 268:15772-15778(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Retinal pigment epithelium;
RX PubMed=8703970; DOI=10.1016/0005-2736(96)00076-4;
RA Ruiz A.C., Bok D.;
RT "Characterization of the 3' UTR sequence encoded by the AQP-1 gene in human
RT retinal pigment epithelium.";
RL Biochim. Biophys. Acta 1282:174-178(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=7517253;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mesangial cell;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-45 AND ASP-165.
RG SeattleSNPs variation discovery resource;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-269.
RC TISSUE=Articular cartilage;
RA Trujillo E., Gonzalez T., Martin-Vasallo P., Marples D., Mobasheri A.;
RT "Human chondrocytes in situ express aquaporin water channels: changes in
RT AQP1 abundance in pathologies of articular cartilage.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP PROTEIN SEQUENCE OF 2-36.
RX PubMed=2007592; DOI=10.1016/s0021-9258(18)38133-x;
RA Smith B.L., Agre P.;
RT "Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit
RT oligomer similar to channel proteins.";
RL J. Biol. Chem. 266:6407-6415(1991).
RN [13]
RP FUNCTION.
RX PubMed=1373524; DOI=10.1126/science.256.5055.385;
RA Preston G.M., Carroll T.P., Guggino W.B., Agre P.;
RT "Appearance of water channels in Xenopus oocytes expressing red cell CHIP28
RT protein.";
RL Science 256:385-387(1992).
RN [14]
RP TARGET OF MERCURY INHIBITION.
RX PubMed=7677994; DOI=10.1016/s0021-9258(18)54108-9;
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 [15]
RP TOPOLOGY.
RX PubMed=7507481; DOI=10.1016/s0021-9258(17)42079-5;
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 [16]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION IN A COMPLEX WITH
RP STOM, AND SUBUNIT.
RX PubMed=23219802; DOI=10.1016/j.bbamem.2012.11.030;
RA Rungaldier S., Oberwagner W., Salzer U., Csaszar E., Prohaska R.;
RT "Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in
RT human erythrocyte membrane domains.";
RL Biochim. Biophys. Acta 1828:956-966(2013).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (1.6 ANGSTROMS).
RX PubMed=7518771; DOI=10.1002/j.1460-2075.1994.tb06597.x;
RA Walz T., Smith B.L., Agre P., Engel A.;
RT "The three-dimensional structure of human erythrocyte aquaporin CHIP.";
RL EMBO J. 13:2985-2993(1994).
RN [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (6 ANGSTROMS).
RX PubMed=9177353; DOI=10.1038/42512;
RA Walz T., Hirai T., Murata K., Heymann J.B., Mitsuoka K., Fujiyoshi Y.,
RA Smith B.L., Agre P., Engel A.;
RT "The three-dimensional structure of aquaporin-1.";
RL Nature 387:624-627(1997).
RN [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.8 ANGSTROMS).
RX PubMed=11034202; DOI=10.1038/35036519;
RA Murata K., Mitsuoka K., Hirai T., Walz T., Agre P., Heymann J.B., Engel A.,
RA Fujiyoshi Y.;
RT "Structural determinants of water permeation through aquaporin-1.";
RL Nature 407:599-605(2000).
RN [20]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.54 ANGSTROMS).
RX PubMed=11532455; DOI=10.1016/s0014-5793(01)02743-0;
RA de Groot B.L., Engel A., Grubmueller H.;
RT "A refined structure of human aquaporin-1.";
RL FEBS Lett. 504:206-211(2001).
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.7 ANGSTROMS).
RX PubMed=11171962; DOI=10.1073/pnas.98.4.1398;
RA Ren G., Reddy V.S., Cheng A., Melnyk P., Mitra A.K.;
RT "Visualization of a water-selective pore by electron crystallography in
RT vitreous ice.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:1398-1403(2001).
RN [22]
RP VARIANT VAL-45, AND INVOLVEMENT IN COLTON BLOOD GROUP SYSTEM.
RX PubMed=7521882; DOI=10.1172/jci117418;
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 and
RT Colton blood group antigens.";
RL J. Clin. Invest. 94:1043-1049(1994).
RN [23]
RP VARIANT LEU-38, AND INVOLVEMENT IN COLTON BLOOD GROUP SYSTEM.
RX PubMed=7521540; DOI=10.1126/science.7521540;
RA Preston G.M., Smith B.L., Zeidel M.L., Moulds J.J., Agre P.;
RT "Mutations in aquaporin-1 in phenotypically normal humans without
RT functional CHIP water channels.";
RL Science 265:1585-1587(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. {ECO:0000269|PubMed:1373524}.
CC -!- SUBUNIT: Homotetramer. Interacts with EPHB2; involved in endolymph
CC production in the inner ear (By similarity). Identified in a complex
CC with STOM. {ECO:0000250, ECO:0000269|PubMed:23219802}.
CC -!- INTERACTION:
CC P29972; A2BDD9: AMOT; NbExp=3; IntAct=EBI-745213, EBI-17286414;
CC P29972; P29972: AQP1; NbExp=3; IntAct=EBI-745213, EBI-745213;
CC P29972; Q13520: AQP6; NbExp=3; IntAct=EBI-745213, EBI-13059134;
CC P29972; Q9BXK5: BCL2L13; NbExp=3; IntAct=EBI-745213, EBI-747430;
CC P29972; Q9BUH8: BEGAIN; NbExp=3; IntAct=EBI-745213, EBI-742722;
CC P29972; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-745213, EBI-11519926;
CC P29972; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-745213, EBI-2548012;
CC P29972; Q96LC9: BMF; NbExp=3; IntAct=EBI-745213, EBI-3919268;
CC P29972; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-745213, EBI-10171416;
CC P29972; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-745213, EBI-2808286;
CC P29972; O95273: CCNDBP1; NbExp=3; IntAct=EBI-745213, EBI-748961;
CC P29972; P11912: CD79A; NbExp=3; IntAct=EBI-745213, EBI-7797864;
CC P29972; Q01850: CDR2; NbExp=3; IntAct=EBI-745213, EBI-1181367;
CC P29972; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-745213, EBI-744115;
CC P29972; O00501: CLDN5; NbExp=3; IntAct=EBI-745213, EBI-18400628;
CC P29972; P49747: COMP; NbExp=3; IntAct=EBI-745213, EBI-2531022;
CC P29972; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-745213, EBI-18013275;
CC P29972; O43889-2: CREB3; NbExp=3; IntAct=EBI-745213, EBI-625022;
CC P29972; Q9NQ79: CRTAC1; NbExp=3; IntAct=EBI-745213, EBI-10205543;
CC P29972; Q96S65: CSRNP1; NbExp=3; IntAct=EBI-745213, EBI-4311573;
CC P29972; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-745213, EBI-3867333;
CC P29972; Q9NQ30: ESM1; NbExp=3; IntAct=EBI-745213, EBI-12260294;
CC P29972; P34910-2: EVI2B; NbExp=3; IntAct=EBI-745213, EBI-17640610;
CC P29972; Q3B820: FAM161A; NbExp=3; IntAct=EBI-745213, EBI-719941;
CC P29972; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-745213, EBI-18304435;
CC P29972; Q8TBE3: FNDC9; NbExp=3; IntAct=EBI-745213, EBI-12142257;
CC P29972; Q6FG41: FOS; NbExp=3; IntAct=EBI-745213, EBI-10198738;
CC P29972; A1L4K1: FSD2; NbExp=3; IntAct=EBI-745213, EBI-5661036;
CC P29972; O00258: GET1; NbExp=3; IntAct=EBI-745213, EBI-18908258;
CC P29972; O95377: GJB5; NbExp=3; IntAct=EBI-745213, EBI-3909454;
CC P29972; P08151: GLI1; NbExp=3; IntAct=EBI-745213, EBI-308084;
CC P29972; Q08379: GOLGA2; NbExp=3; IntAct=EBI-745213, EBI-618309;
CC P29972; O60883: GPR37L1; NbExp=3; IntAct=EBI-745213, EBI-2927498;
CC P29972; Q8TED1: GPX8; NbExp=3; IntAct=EBI-745213, EBI-11721746;
CC P29972; Q8IY31-3: IFT20; NbExp=3; IntAct=EBI-745213, EBI-9091197;
CC P29972; P24592: IGFBP6; NbExp=3; IntAct=EBI-745213, EBI-947015;
CC P29972; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-745213, EBI-8638439;
CC P29972; Q9UKS7: IKZF2; NbExp=3; IntAct=EBI-745213, EBI-3893057;
CC P29972; Q9UKT9: IKZF3; NbExp=6; IntAct=EBI-745213, EBI-747204;
CC P29972; Q9HBE5: IL21R; NbExp=3; IntAct=EBI-745213, EBI-12558959;
CC P29972; O95279: KCNK5; NbExp=3; IntAct=EBI-745213, EBI-3934936;
CC P29972; Q7L273: KCTD9; NbExp=3; IntAct=EBI-745213, EBI-4397613;
CC P29972; O75525: KHDRBS3; NbExp=3; IntAct=EBI-745213, EBI-722504;
CC P29972; Q8N8K9: KIAA1958; NbExp=3; IntAct=EBI-745213, EBI-10181113;
CC P29972; Q53HC5: KLHL26; NbExp=3; IntAct=EBI-745213, EBI-724915;
CC P29972; Q15323: KRT31; NbExp=3; IntAct=EBI-745213, EBI-948001;
CC P29972; Q14525: KRT33B; NbExp=3; IntAct=EBI-745213, EBI-1049638;
CC P29972; O76014: KRT37; NbExp=3; IntAct=EBI-745213, EBI-1045716;
CC P29972; Q6A162: KRT40; NbExp=3; IntAct=EBI-745213, EBI-10171697;
CC P29972; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-745213, EBI-11959885;
CC P29972; Q9BYS1: KRTAP1-5; NbExp=3; IntAct=EBI-745213, EBI-11741292;
CC P29972; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-745213, EBI-10172290;
CC P29972; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-745213, EBI-10171774;
CC P29972; P60329: KRTAP12-4; NbExp=3; IntAct=EBI-745213, EBI-10176396;
CC P29972; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-745213, EBI-751260;
CC P29972; Q9BYR5: KRTAP4-2; NbExp=6; IntAct=EBI-745213, EBI-10172511;
CC P29972; Q9BYR3: KRTAP4-4; NbExp=3; IntAct=EBI-745213, EBI-11958132;
CC P29972; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-745213, EBI-11962084;
CC P29972; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-745213, EBI-1044640;
CC P29972; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-745213, EBI-11958364;
CC P29972; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-745213, EBI-11962058;
CC P29972; Q5T700: LDLRAD1; NbExp=3; IntAct=EBI-745213, EBI-10173166;
CC P29972; O95751: LDOC1; NbExp=3; IntAct=EBI-745213, EBI-740738;
CC P29972; Q9H400: LIME1; NbExp=3; IntAct=EBI-745213, EBI-2830566;
CC P29972; O60711: LPXN; NbExp=3; IntAct=EBI-745213, EBI-744222;
CC P29972; Q96AG4: LRRC59; NbExp=3; IntAct=EBI-745213, EBI-358888;
CC P29972; Q99750: MDFI; NbExp=7; IntAct=EBI-745213, EBI-724076;
CC P29972; O14880: MGST3; NbExp=3; IntAct=EBI-745213, EBI-724754;
CC P29972; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-745213, EBI-10172526;
CC P29972; A9UHW6-2: MIF4GD; NbExp=3; IntAct=EBI-745213, EBI-9118295;
CC P29972; Q13064: MKRN3; NbExp=3; IntAct=EBI-745213, EBI-2340269;
CC P29972; Q6IN84: MRM1; NbExp=3; IntAct=EBI-745213, EBI-5454865;
CC P29972; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-745213, EBI-742948;
CC P29972; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-745213, EBI-11522433;
CC P29972; P15941-11: MUC1; NbExp=3; IntAct=EBI-745213, EBI-17263240;
CC P29972; P13349: MYF5; NbExp=3; IntAct=EBI-745213, EBI-17491620;
CC P29972; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-745213, EBI-945833;
CC P29972; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-745213, EBI-22310682;
CC P29972; Q9NXJ5-2: PGPEP1; NbExp=3; IntAct=EBI-745213, EBI-12813581;
CC P29972; O15496: PLA2G10; NbExp=3; IntAct=EBI-745213, EBI-726466;
CC P29972; Q9NRY7: PLSCR2; NbExp=3; IntAct=EBI-745213, EBI-3937430;
CC P29972; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-745213, EBI-3957793;
CC P29972; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-745213, EBI-11320284;
CC P29972; Q9NYW8: RBAK; NbExp=3; IntAct=EBI-745213, EBI-1210429;
CC P29972; Q04864-2: REL; NbExp=3; IntAct=EBI-745213, EBI-10829018;
CC P29972; Q9UGC6: RGS17; NbExp=6; IntAct=EBI-745213, EBI-3918154;
CC P29972; O76081: RGS20; NbExp=3; IntAct=EBI-745213, EBI-1052678;
CC P29972; O76081-6: RGS20; NbExp=3; IntAct=EBI-745213, EBI-10178530;
CC P29972; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-745213, EBI-10182375;
CC P29972; Q9H9V4: RNF122; NbExp=3; IntAct=EBI-745213, EBI-2129998;
CC P29972; Q9NR31: SAR1A; NbExp=3; IntAct=EBI-745213, EBI-3920694;
CC P29972; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-745213, EBI-747107;
CC P29972; O15304-2: SIVA1; NbExp=3; IntAct=EBI-745213, EBI-12372219;
CC P29972; Q16348: SLC15A2; NbExp=3; IntAct=EBI-745213, EBI-12806032;
CC P29972; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-745213, EBI-12898013;
CC P29972; Q5MJ70: SPDYA; NbExp=3; IntAct=EBI-745213, EBI-7125479;
CC P29972; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-745213, EBI-5235340;
CC P29972; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-745213, EBI-7082156;
CC P29972; O43597: SPRY2; NbExp=3; IntAct=EBI-745213, EBI-742487;
CC P29972; O43610: SPRY3; NbExp=3; IntAct=EBI-745213, EBI-12290641;
CC P29972; Q5W111-2: SPRYD7; NbExp=3; IntAct=EBI-745213, EBI-12408727;
CC P29972; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-745213, EBI-17280858;
CC P29972; P15884: TCF4; NbExp=3; IntAct=EBI-745213, EBI-533224;
CC P29972; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-745213, EBI-10982110;
CC P29972; Q9NVV0: TMEM38B; NbExp=3; IntAct=EBI-745213, EBI-1055114;
CC P29972; Q96B21: TMEM45B; NbExp=3; IntAct=EBI-745213, EBI-3923061;
CC P29972; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-745213, EBI-11742770;
CC P29972; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-745213, EBI-12345267;
CC P29972; Q07912: TNK2; NbExp=3; IntAct=EBI-745213, EBI-603457;
CC P29972; Q63HR2: TNS2; NbExp=3; IntAct=EBI-745213, EBI-949753;
CC P29972; Q13077: TRAF1; NbExp=3; IntAct=EBI-745213, EBI-359224;
CC P29972; Q12933: TRAF2; NbExp=3; IntAct=EBI-745213, EBI-355744;
CC P29972; P36406: TRIM23; NbExp=6; IntAct=EBI-745213, EBI-740098;
CC P29972; O94972: TRIM37; NbExp=3; IntAct=EBI-745213, EBI-741602;
CC P29972; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-745213, EBI-725997;
CC P29972; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-745213, EBI-5235829;
CC P29972; Q9C029: TRIM7; NbExp=3; IntAct=EBI-745213, EBI-2813981;
CC P29972; Q15654: TRIP6; NbExp=7; IntAct=EBI-745213, EBI-742327;
CC P29972; Q86WV8: TSC1; NbExp=3; IntAct=EBI-745213, EBI-12806590;
CC P29972; O15060: ZBTB39; NbExp=3; IntAct=EBI-745213, EBI-9995672;
CC P29972; Q9NZV7: ZIM2; NbExp=3; IntAct=EBI-745213, EBI-11962760;
CC P29972; P17020: ZNF16; NbExp=3; IntAct=EBI-745213, EBI-3921553;
CC P29972; Q8TD17: ZNF398; NbExp=3; IntAct=EBI-745213, EBI-8643207;
CC P29972; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-745213, EBI-10240849;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23219802};
CC Multi-pass membrane protein {ECO:0000269|PubMed:23219802}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P29972-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P29972-2; Sequence=VSP_046109, VSP_046110;
CC Name=3;
CC IsoId=P29972-3; Sequence=VSP_046679;
CC Name=4;
CC IsoId=P29972-4; Sequence=VSP_046680, VSP_046681;
CC -!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level).
CC Expressed in a number of tissues including erythrocytes, renal tubules,
CC retinal pigment epithelium, heart, lung, skeletal muscle, kidney and
CC pancreas. Weakly expressed in brain, placenta and liver.
CC {ECO:0000269|PubMed:23219802}.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC membrane-spanning domains and a pore-forming loop with the signature
CC motif Asn-Pro-Ala (NPA).
CC -!- POLYMORPHISM: AQP1 is responsible for the Colton blood group system
CC [MIM:110450]. 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-45).
CC Co(A-B-) which is very rare, is due to a complete absence of AQP1.
CC {ECO:0000269|PubMed:7521540, ECO:0000269|PubMed:7521882}.
CC -!- MISCELLANEOUS: Pharmacologically inhibited by submillimolar
CC concentrations of mercury. {ECO:0000305|PubMed:7677994}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation
CC database;
CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=colton";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/aqp1/";
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Liquid states - Issue 36 of
CC July 2003;
CC URL="https://web.expasy.org/spotlight/back_issues/036";
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DR EMBL; M77829; AAA58425.1; -; mRNA.
DR EMBL; U41517; AAC50648.1; -; mRNA.
DR EMBL; U41518; AAC50649.1; -; mRNA.
DR EMBL; S73482; AAB31193.1; -; mRNA.
DR EMBL; AK309608; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY953319; AAX24129.1; -; Genomic_DNA.
DR EMBL; AC004691; AAC16481.1; -; Genomic_DNA.
DR EMBL; AC005155; AAC23788.1; -; Genomic_DNA.
DR EMBL; AB451275; BAG70089.1; -; mRNA.
DR EMBL; AB451402; BAG70216.1; -; mRNA.
DR EMBL; CH471073; EAW93971.1; -; Genomic_DNA.
DR EMBL; BC022486; AAH22486.1; -; mRNA.
DR EMBL; AF480415; AAL87136.1; -; Genomic_DNA.
DR CCDS; CCDS5431.1; -. [P29972-1]
DR PIR; A41616; A41616.
DR PIR; I52366; I52366.
DR RefSeq; NP_932766.1; NM_198098.3. [P29972-1]
DR PDB; 1FQY; X-ray; 3.80 A; A=1-269.
DR PDB; 1H6I; X-ray; 3.54 A; A=1-269.
DR PDB; 1IH5; X-ray; 3.70 A; A=1-269.
DR PDB; 4CSK; X-ray; 3.28 A; A=1-269.
DR PDB; 6POJ; NMR; -; A=1-269.
DR PDBsum; 1FQY; -.
DR PDBsum; 1H6I; -.
DR PDBsum; 1IH5; -.
DR PDBsum; 4CSK; -.
DR PDBsum; 6POJ; -.
DR AlphaFoldDB; P29972; -.
DR SMR; P29972; -.
DR BioGRID; 106854; 135.
DR CORUM; P29972; -.
DR DIP; DIP-29607N; -.
DR IntAct; P29972; 144.
DR MINT; P29972; -.
DR STRING; 9606.ENSP00000311165; -.
DR BindingDB; P29972; -.
DR ChEMBL; CHEMBL4523210; -.
DR DrugBank; DB00819; Acetazolamide.
DR DrugBank; DB02451; B-nonylglucoside.
DR DrugBank; DB09338; Mersalyl.
DR DrugCentral; P29972; -.
DR GuidetoPHARMACOLOGY; 688; -.
DR TCDB; 1.A.8.8.1; the major intrinsic protein (mip) family.
DR GlyGen; P29972; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P29972; -.
DR PhosphoSitePlus; P29972; -.
DR BioMuta; AQP1; -.
DR DMDM; 267412; -.
DR EPD; P29972; -.
DR jPOST; P29972; -.
DR MassIVE; P29972; -.
DR PaxDb; P29972; -.
DR PeptideAtlas; P29972; -.
DR PRIDE; P29972; -.
DR ProteomicsDB; 16873; -.
DR ProteomicsDB; 19345; -.
DR ProteomicsDB; 24598; -.
DR ProteomicsDB; 54613; -. [P29972-1]
DR Antibodypedia; 35017; 592 antibodies from 38 providers.
DR DNASU; 358; -.
DR Ensembl; ENST00000311813.11; ENSP00000311165.4; ENSG00000240583.14. [P29972-1]
DR Ensembl; ENST00000409611.1; ENSP00000387178.1; ENSG00000240583.14. [P29972-3]
DR Ensembl; ENST00000409899.5; ENSP00000386712.1; ENSG00000240583.14. [P29972-4]
DR Ensembl; ENST00000652696.1; ENSP00000498672.1; ENSG00000240583.14. [P29972-1]
DR GeneID; 358; -.
DR KEGG; hsa:358; -.
DR MANE-Select; ENST00000311813.11; ENSP00000311165.4; NM_198098.4; NP_932766.1.
DR UCSC; uc003tbv.3; human. [P29972-1]
DR CTD; 358; -.
DR DisGeNET; 358; -.
DR GeneCards; AQP1; -.
DR HGNC; HGNC:633; AQP1.
DR HPA; ENSG00000240583; Low tissue specificity.
DR MalaCards; AQP1; -.
DR MIM; 107776; gene.
DR MIM; 110450; phenotype.
DR neXtProt; NX_P29972; -.
DR OpenTargets; ENSG00000240583; -.
DR PharmGKB; PA24918; -.
DR VEuPathDB; HostDB:ENSG00000240583; -.
DR eggNOG; KOG0223; Eukaryota.
DR GeneTree; ENSGT00940000157015; -.
DR HOGENOM; CLU_020019_3_3_1; -.
DR InParanoid; P29972; -.
DR OMA; IFKALMY; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P29972; -.
DR TreeFam; TF312940; -.
DR PathwayCommons; P29972; -.
DR Reactome; R-HSA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR Reactome; R-HSA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-HSA-432047; Passive transport by Aquaporins.
DR SignaLink; P29972; -.
DR SIGNOR; P29972; -.
DR BioGRID-ORCS; 358; 13 hits in 1084 CRISPR screens.
DR ChiTaRS; AQP1; human.
DR EvolutionaryTrace; P29972; -.
DR GeneWiki; Aquaporin_1; -.
DR GenomeRNAi; 358; -.
DR Pharos; P29972; Tbio.
DR PRO; PR:P29972; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P29972; protein.
DR Bgee; ENSG00000240583; Expressed in descending thoracic aorta and 194 other tissues.
DR ExpressionAtlas; P29972; baseline and differential.
DR Genevisible; P29972; HS.
DR GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0035379; F:carbon dioxide transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0046875; F:ephrin receptor binding; IEA:Ensembl.
DR GO; GO:0015168; F:glycerol transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005223; F:intracellular cGMP-activated cation channel activity; IDA:UniProtKB.
DR GO; GO:0030184; F:nitric oxide transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0005267; F:potassium channel activity; IMP:UniProtKB.
DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015250; F:water channel activity; IDA:UniProtKB.
DR GO; GO:0005372; F:water transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0072488; P:ammonium transmembrane transport; IDA:UniProtKB.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0035378; P:carbon dioxide transmembrane transport; IDA:UniProtKB.
DR GO; GO:0015670; P:carbon dioxide transport; IDA:UniProtKB.
DR GO; GO:0006884; P:cell volume homeostasis; IMP:UniProtKB.
DR GO; GO:0019725; P:cellular homeostasis; IDA:UniProtKB.
DR GO; GO:0071474; P:cellular hyperosmotic response; IMP:UniProtKB.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
DR GO; GO:0071280; P:cellular response to copper ion; IDA:UniProtKB.
DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IDA:UniProtKB.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
DR GO; GO:0071241; P:cellular response to inorganic substance; IDA:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IDA:UniProtKB.
DR GO; GO:0071288; P:cellular response to mercury ion; IDA:UniProtKB.
DR GO; GO:0071732; P:cellular response to nitric oxide; IDA:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB.
DR GO; GO:0071472; P:cellular response to salt stress; IDA:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
DR GO; GO:0009992; P:cellular water homeostasis; IDA:UniProtKB.
DR GO; GO:0033326; P:cerebrospinal fluid secretion; IEP:UniProtKB.
DR GO; GO:0019934; P:cGMP-mediated signaling; IDA:UniProtKB.
DR GO; GO:0051458; P:corticotropin secretion; IEA:Ensembl.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:UniProtKB.
DR GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR GO; GO:0003094; P:glomerular filtration; IEA:Ensembl.
DR GO; GO:0015793; P:glycerol transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006972; P:hyperosmotic response; IBA:GO_Central.
DR GO; GO:0021670; P:lateral ventricle development; IEP:UniProtKB.
DR GO; GO:0044241; P:lipid digestion; IEA:Ensembl.
DR GO; GO:0072220; P:metanephric descending thin limb development; IEA:Ensembl.
DR GO; GO:0072239; P:metanephric glomerulus vasculature development; IEA:Ensembl.
DR GO; GO:0072232; P:metanephric proximal convoluted tubule segment 2 development; IEA:Ensembl.
DR GO; GO:0072230; P:metanephric proximal straight tubule development; IEA:Ensembl.
DR GO; GO:0050891; P:multicellular organismal water homeostasis; IEP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0030185; P:nitric oxide transport; IDA:UniProtKB.
DR GO; GO:0042476; P:odontogenesis; IEP:UniProtKB.
DR GO; GO:0030157; P:pancreatic juice secretion; IEP:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB.
DR GO; GO:0046878; P:positive regulation of saliva secretion; IMP:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; ISS:UniProtKB.
DR GO; GO:0070295; P:renal water absorption; IEA:Ensembl.
DR GO; GO:0003091; P:renal water homeostasis; TAS:Reactome.
DR GO; GO:0003097; P:renal water transport; IDA:UniProtKB.
DR GO; GO:0033363; P:secretory granule organization; IEA:Ensembl.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR GO; GO:0035377; P:transepithelial water transport; IDA:UniProtKB.
DR GO; GO:0006833; P:water transport; IDA:UniProtKB.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR023274; Aquaporin_1.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR19139; PTHR19139; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR02013; AQUAPORIN1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR TIGRFAMs; TIGR00861; MIP; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Blood group antigen; Cell membrane;
KW Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2007592"
FT CHAIN 2..269
FT /note="Aquaporin-1"
FT /id="PRO_0000063920"
FT TOPO_DOM 2..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:7507481"
FT TRANSMEM 8..36
FT /note="Helical; Name=Helix 1"
FT TOPO_DOM 37..48
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:7507481"
FT TRANSMEM 49..66
FT /note="Helical; Name=Helix 2"
FT TOPO_DOM 67..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:7507481"
FT INTRAMEM 71..76
FT INTRAMEM 77..84
FT /note="Helical; Name=Helix B"
FT TOPO_DOM 85..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:7507481"
FT TRANSMEM 95..115
FT /note="Helical; Name=Helix 3"
FT TOPO_DOM 116..136
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:7507481"
FT TRANSMEM 137..155
FT /note="Helical; Name=Helix 4"
FT TOPO_DOM 156..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:7507481"
FT TRANSMEM 167..183
FT /note="Helical; Name=Helix 5"
FT TOPO_DOM 184..186
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:7507481"
FT INTRAMEM 187..192
FT INTRAMEM 193..200
FT /note="Helical; Name=Helix E"
FT TOPO_DOM 201..207
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:7507481"
FT TRANSMEM 208..228
FT /note="Helical; Name=Helix 6"
FT TOPO_DOM 229..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:7507481"
FT MOTIF 76..78
FT /note="NPA 1"
FT MOTIF 192..194
FT /note="NPA 2"
FT SITE 56
FT /note="Substrate discrimination"
FT SITE 180
FT /note="Substrate discrimination"
FT SITE 189
FT /note="Hg(2+)-sensitive residue"
FT SITE 195
FT /note="Substrate discrimination"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02013"
FT MOD_RES 253
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q02013"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02013"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..128
FT /note="MASEFKKKLFWRAVVAEFLATTLFVFISIGSALGFKYPVGNNQTAVQDNVKV
FT SLAFGLSIATLAQSVGHISGAHLNPAVTLGLLLSCQISIFRALMYIIAQCVGAIVATAI
FT LSGITSSLTGNSLGRND -> MFWTFGYEAVSPAGPSHLFASLLLGVLLTITFMPGARP
FT LPLVLVPQNTLAWMQLDAKAPAHPRPLQLLGRVGPGSRQ (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_046679"
FT VAR_SEQ 1..45
FT /note="MASEFKKKLFWRAVVAEFLATTLFVFISIGSALGFKYPVGNNQTA -> MPG
FT ARPLPLVLVPQNTLAWMQLDAKAPAHPRPLQLLGRVGPGSRQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046109"
FT VAR_SEQ 1..13
FT /note="MASEFKKKLFWRA -> MQSGMGWNVLDFW (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_046680"
FT VAR_SEQ 14..128
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_046681"
FT VAR_SEQ 46..128
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046110"
FT VARIANT 38
FT /note="P -> L (in Co(A-B-) antigen; non functional AQP1;
FT red cells show low osmotic water permeability;
FT dbSNP:rs104894004)"
FT /evidence="ECO:0000269|PubMed:7521540"
FT /id="VAR_013279"
FT VARIANT 45
FT /note="A -> V (in Co(A-B+) antigen; dbSNP:rs28362692)"
FT /evidence="ECO:0000269|PubMed:7521882, ECO:0000269|Ref.6"
FT /id="VAR_004400"
FT VARIANT 165
FT /note="G -> D (in dbSNP:rs28362731)"
FT /evidence="ECO:0000269|Ref.6"
FT /id="VAR_022318"
FT CONFLICT 45
FT /note="A -> T (in Ref. 10; AAH22486)"
FT /evidence="ECO:0000305"
FT HELIX 6..32
FT /evidence="ECO:0007829|PDB:4CSK"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:4CSK"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:4CSK"
FT HELIX 49..67
FT /evidence="ECO:0007829|PDB:4CSK"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:4CSK"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:4CSK"
FT HELIX 93..115
FT /evidence="ECO:0007829|PDB:4CSK"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:6POJ"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:6POJ"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6POJ"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:4CSK"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:4CSK"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:4CSK"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:4CSK"
FT HELIX 168..174
FT /evidence="ECO:0007829|PDB:4CSK"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:4CSK"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:4CSK"
FT HELIX 193..197
FT /evidence="ECO:0007829|PDB:4CSK"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:4CSK"
FT TURN 207..210
FT /evidence="ECO:0007829|PDB:4CSK"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:4CSK"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:4CSK"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:4CSK"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:6POJ"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:6POJ"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6POJ"
SQ SEQUENCE 269 AA; 28526 MW; BA204D82FB26352E CRC64;
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
