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 24-JAN-2024, entry version 241. DE RecName: Full=Aquaporin-1 {ECO:0000305}; 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 {ECO:0000312|HGNC:HGNC:633}; 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] {ECO:0007744|PDB:1FQY} 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] {ECO:0007744|PDB:1H6I} 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] {ECO:0007744|PDB:1IH5} 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] {ECO:0007744|PDB:7UZE, ECO:0007744|PDB:8CT2, ECO:0007744|PDB:8CTE} RP STRUCTURE BY ELECTRON MICROSCOPY (2.40 ANGSTROMS), FUNCTION, SUBUNIT, RP ANKYRIN-1 COMPLEX IDENTIFICATION, AND INTERACTION WITH ANK1 AND EPB42. RX PubMed=35835865; DOI=10.1038/s41594-022-00792-w; RA Vallese F., Kim K., Yen L.Y., Johnston J.D., Noble A.J., Cali T., RA Clarke O.B.; RT "Architecture of the human erythrocyte ankyrin-1 complex."; RL Nat. Struct. Mol. Biol. 29:706-718(2022). RN [23] 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 [24] 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 (PubMed:1373524). Component of the CC ankyrin-1 complex, a multiprotein complex involved in the stability and CC shape of the erythrocyte membrane (PubMed:35835865). CC {ECO:0000269|PubMed:1373524, ECO:0000269|PubMed:35835865}. CC -!- SUBUNIT: Homotetramer (PubMed:35835865). Component of the ankyrin-1 CC complex in the erythrocyte, composed of ANK1, RHCE, RHAG, SLC4A1, CC EPB42, GYPA, GYPB and AQP1 (PubMed:35835865). Interacts with EPHB2; CC involved in endolymph production in the inner ear (By similarity). CC Identified in a complex with STOM (PubMed:23219802). Interacts (via the CC N-terminal) with ANK1 (via ANK 1-5 repeats) (PubMed:35835865). CC Interacts (via the C-terminal) with EPB42 (PubMed:35835865). CC {ECO:0000250, ECO:0000250|UniProtKB:Q02013, CC ECO:0000269|PubMed:23219802, ECO:0000269|PubMed:35835865}. 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; 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; Q6PI77: GPRASP3; NbExp=3; IntAct=EBI-745213, EBI-11519926; 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"; 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; 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 PDB; 7UZE; EM; 2.40 A; A/B/C/D=1-269. DR PDB; 8CT2; EM; 3.10 A; A/B/C/D=1-269. DR PDB; 8CTE; EM; 2.90 A; M/O/R/S=1-269. DR PDBsum; 1FQY; -. DR PDBsum; 1H6I; -. DR PDBsum; 1IH5; -. DR PDBsum; 4CSK; -. DR PDBsum; 6POJ; -. DR PDBsum; 7UZE; -. DR PDBsum; 8CT2; -. DR PDBsum; 8CTE; -. DR AlphaFoldDB; P29972; -. DR EMDB; EMD-26886; -. DR EMDB; EMD-26978; -. DR EMDB; EMD-26988; -. DR SMR; P29972; -. DR BioGRID; 106854; 136. 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 GlyCosmos; P29972; 3 sites, 1 glycan. 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; 9606-ENSP00000311165; -. DR PeptideAtlas; P29972; -. DR ProteomicsDB; 16873; -. DR ProteomicsDB; 19345; -. DR ProteomicsDB; 24598; -. DR ProteomicsDB; 54613; -. [P29972-1] DR Antibodypedia; 35017; 655 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 AGR; HGNC:633; -. DR CTD; 358; -. DR DisGeNET; 358; -. DR GeneCards; AQP1; -. DR HGNC; HGNC:633; AQP1. DR HPA; ENSG00000240583; Tissue enhanced (choroid). 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; KMFWRAV; -. DR OrthoDB; 3236018at2759; -. 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; 14 hits in 1175 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 196 other cell types or tissues. DR ExpressionAtlas; P29972; baseline and differential. DR GO; GO:0170014; C:ankyrin-1 complex; IDA:UniProtKB. 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:0031965; C:nuclear membrane; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. 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: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:0009992; P:intracellular water homeostasis; IDA:UniProtKB. 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-level 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; Glycerol uptake facilitator protein; 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 NCBIfam; TIGR00861; MIP; 1. DR PANTHER; PTHR19139; AQUAPORIN TRANSPORTER; 1. DR PANTHER; PTHR19139:SF161; AQUAPORIN-1; 1. DR Pfam; PF00230; MIP; 1. DR PRINTS; PR02013; AQUAPORIN1. DR PRINTS; PR00783; MINTRINSICP. DR SUPFAM; SSF81338; Aquaporin-like; 1. DR PROSITE; PS00221; MIP; 1. DR Genevisible; P29972; HS. 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 4..6 FT /evidence="ECO:0007829|PDB:7UZE" FT HELIX 8..32 FT /evidence="ECO:0007829|PDB:7UZE" FT HELIX 34..36 FT /evidence="ECO:0007829|PDB:7UZE" FT STRAND 38..40 FT /evidence="ECO:0007829|PDB:7UZE" FT HELIX 49..71 FT /evidence="ECO:0007829|PDB:7UZE" FT HELIX 77..85 FT /evidence="ECO:0007829|PDB:7UZE" FT HELIX 91..115 FT /evidence="ECO:0007829|PDB:7UZE" FT TURN 116..118 FT /evidence="ECO:0007829|PDB:7UZE" FT STRAND 122..127 FT /evidence="ECO:0007829|PDB:6POJ" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:6POJ" FT HELIX 135..156 FT /evidence="ECO:0007829|PDB:7UZE" FT HELIX 168..187 FT /evidence="ECO:0007829|PDB:7UZE" FT HELIX 193..203 FT /evidence="ECO:0007829|PDB:7UZE" FT TURN 207..210 FT /evidence="ECO:0007829|PDB:7UZE" FT HELIX 211..229 FT /evidence="ECO:0007829|PDB:7UZE" FT HELIX 238..247 FT /evidence="ECO:0007829|PDB:7UZE" 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 //