ID AQP1_MOUSE Reviewed; 269 AA. AC Q02013; Q542P1; Q91VY8; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 10-JUN-2026, entry version 201. DE RecName: Full=Aquaporin-1 {ECO:0000305}; DE Short=AQP-1; DE AltName: Full=Aquaporin-CHIP; DE AltName: Full=Delayed early response protein 2 {ECO:0000303|PubMed:1508193}; DE Short=DER2 {ECO:0000303|PubMed:1508193}; GN Name=Aqp1 {ECO:0000312|MGI:MGI:103201}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/cJ; RX PubMed=1508193; DOI=10.1128/mcb.12.9.3919-3929.1992; RA Lanahan A.A., Williams J.B., Sanders L.K., Nathans D.; RT "Growth factor-induced delayed early response genes."; RL Mol. Cell. Biol. 12:3919-3929(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Head, Inner ear, and Spleen; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary tumor; 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 [4] RP INTERACTION WITH EPHB2. RX PubMed=10839360; DOI=10.1016/s0896-6273(00)81174-5; RA Cowan C.A., Yokoyama N., Bianchi L.M., Henkemeyer M., Fritzsch B.; RT "EphB2 guides axons at the midline and is necessary for normal vestibular RT function."; RL Neuron 26:417-430(2000). RN [5] RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=12133842; DOI=10.1074/jbc.m206948200; RA Yang B., Verkman A.S.; RT "Analysis of double knockout mice lacking aquaporin-1 and urea transporter RT UT-B. Evidence for UT-B-facilitated water transport in erythrocytes."; RL J. Biol. Chem. 277:36782-36786(2002). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; TYR-253 AND SER-262, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [8] RP TISSUE SPECIFICITY. RX PubMed=31605441; DOI=10.1111/febs.15088; RA Kumaran G.K., Hanukoglu I.; RT "Identification and classification of epithelial cells in nephron segments RT by actin cytoskeleton patterns."; RL FEBS J. 287:1176-1194(2020). CC -!- FUNCTION: Forms a water channel that facilitates the transport of water CC across cell membranes, playing a crucial role in water homeostasis in CC various tissues (PubMed:12133842). Could also be permeable to small CC solutes including hydrogen peroxide, glycerol and gases such as amonnia CC (NH3), nitric oxide (NO) and carbon dioxide (CO2). Recruited to the CC ankyrin-1 complex, a multiprotein complex of the erythrocyte membrane, CC it could be part of a CO2 metabolon, linking facilitated diffusion of CC CO2 across the membrane, anion exchange of Cl(-)/HCO3(-) and CC interconversion of dissolved CO2 and carbonic acid in the cytosol. In CC vitro, it shows non-selective gated cation channel activity and may be CC permeable to cations like K(+) and Na(+) in vivo (By similarity). CC {ECO:0000250|UniProtKB:P29972, ECO:0000269|PubMed:12133842}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O(in) = H2O(out); Xref=Rhea:RHEA:29667, ChEBI:CHEBI:15377; CC Evidence={ECO:0000250|UniProtKB:P29972}; CC -!- CATALYTIC ACTIVITY: CC Reaction=nitric oxide(out) = nitric oxide(in); Xref=Rhea:RHEA:74895, CC ChEBI:CHEBI:16480; Evidence={ECO:0000250|UniProtKB:P29972}; CC -!- CATALYTIC ACTIVITY: CC Reaction=CO2(out) = CO2(in); Xref=Rhea:RHEA:74891, ChEBI:CHEBI:16526; CC Evidence={ECO:0000250|UniProtKB:P29972}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glycerol(in) = glycerol(out); Xref=Rhea:RHEA:29675, CC ChEBI:CHEBI:17754; Evidence={ECO:0000250|UniProtKB:P29972}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O2(out) = H2O2(in); Xref=Rhea:RHEA:74375, ChEBI:CHEBI:16240; CC Evidence={ECO:0000250|UniProtKB:P29972}; CC -!- CATALYTIC ACTIVITY: CC Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; CC Evidence={ECO:0000250|UniProtKB:P29972}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, CC ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:P29972}; CC -!- SUBUNIT: Homotetramer; each monomer provides an independent water pore. CC Component of the ankyrin-1 complex in the erythrocyte, composed of CC ANK1, RHCE, RHAG, SLC4A1, EPB42, GYPA, GYPB and AQP1 (By similarity). CC Interacts with EPHB2; involved in endolymph production in the inner ear CC (PubMed:10839360). Identified in a complex with STOM. Interacts (via CC the N-terminal) with ANK1 (via ANK 1-5 repeats). Interacts (via the C- CC terminal) with EPB42 (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:P29972, ECO:0000269|PubMed:10839360}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12133842}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P29972}. CC -!- TISSUE SPECIFICITY: Detected in erythrocytes (at protein level) CC (PubMed:12133842). In the kidney, expressed on luminal and basal CC borders of proximal tubules and in the thin limb of Henle's loop (at CC protein level) (PubMed:31605441). {ECO:0000269|PubMed:12133842, CC ECO:0000269|PubMed:31605441}. 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). {ECO:0000250|UniProtKB:P29972}. CC -!- DISRUPTION PHENOTYPE: Mutant mice are born at the expected Mendelian CC rate and appear healthy and normal, but display strongly reduced urine CC osmolality. Besides, their erythrocytes show reduced water CC permeability. Mice lacking both Aqp1 and Slc14a1 are born at the CC expected Mendelian ratio, but do not thrive; half of them die within CC ten days after birth and none are alive after two weeks. Urine CC osmolality is somewhat lower than that observed with mice lacking only CC Aqp1. Besides, erythrocyte water permeability is significantly lower CC than in mice lacking only Aqp1. {ECO:0000269|PubMed:12133842}. CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. CC {ECO:0000305}. 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; L02914; AAB53928.1; -; mRNA. DR EMBL; AK081886; BAC38360.1; -; mRNA. DR EMBL; AK086688; BAC39719.1; -; mRNA. DR EMBL; AK157333; BAE34051.1; -; mRNA. DR EMBL; AK158226; BAE34412.1; -; mRNA. DR EMBL; AK158389; BAE34482.1; -; mRNA. DR EMBL; AK171627; BAE42573.1; -; mRNA. DR EMBL; AK172361; BAE42966.1; -; mRNA. DR EMBL; BC007125; AAH07125.1; -; mRNA. DR CCDS; CCDS20164.1; -. DR PIR; B44499; B44499. DR RefSeq; NP_031498.1; NM_007472.2. DR AlphaFoldDB; Q02013; -. DR SMR; Q02013; -. DR FunCoup; Q02013; 76. DR IntAct; Q02013; 1. DR STRING; 10090.ENSMUSP00000004774; -. DR GlyCosmos; Q02013; 1 site, No reported glycans. DR GlyGen; Q02013; 3 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q02013; -. DR PhosphoSitePlus; Q02013; -. DR SwissPalm; Q02013; -. DR jPOST; Q02013; -. DR PaxDb; 10090-ENSMUSP00000004774; -. DR PeptideAtlas; Q02013; -. DR ProteomicsDB; 283194; -. DR Pumba; Q02013; -. DR DNASU; 11826; -. DR Ensembl; ENSMUST00000004774.4; ENSMUSP00000004774.4; ENSMUSG00000004655.6. DR GeneID; 11826; -. DR KEGG; mmu:11826; -. DR UCSC; uc009caq.1; mouse. DR AGR; MGI:103201; -. DR CTD; 358; -. DR MGI; MGI:103201; Aqp1. DR VEuPathDB; HostDB:ENSMUSG00000004655; -. DR eggNOG; KOG0223; Eukaryota. DR GeneTree; ENSGT00940000157015; -. DR HOGENOM; CLU_020019_3_3_1; -. DR InParanoid; Q02013; -. DR OMA; FKKKMFW; -. DR OrthoDB; 3222at2759; -. DR PhylomeDB; Q02013; -. DR Reactome; R-MMU-1237044; Erythrocytes take up carbon dioxide and release oxygen. DR Reactome; R-MMU-1247673; Erythrocytes take up oxygen and release carbon dioxide. DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins. DR Reactome; R-MMU-432047; Passive transport by Aquaporins. DR BioGRID-ORCS; 11826; 1 hit in 78 CRISPR screens. DR PRO; PR:Q02013; -. DR Proteomes; UP000000589; Chromosome 6. DR RNAct; Q02013; protein. DR Bgee; ENSMUSG00000004655; Expressed in right lung and 215 other cell types or tissues. DR GO; GO:0170014; C:ankyrin-1 complex; ISS:UniProtKB. DR GO; GO:0045177; C:apical part of cell; ISO:GO_Central. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0030424; C:axon; IDA:MGI. DR GO; GO:0043679; C:axon terminus; ISO:GO_Central. DR GO; GO:0009925; C:basal plasma membrane; IDA:BHF-UCL. 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; ISS:UniProtKB. DR GO; GO:0005901; C:caveola; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0032127; C:dense core granule membrane; ISO:MGI. DR GO; GO:0070062; C:extracellular exosome; IDA:MGI. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0032809; C:neuronal cell body membrane; ISO:GO_Central. DR GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB. DR GO; GO:0008519; F:ammonium channel activity; ISS:UniProtKB. DR GO; GO:0035379; F:carbon dioxide transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB. DR GO; GO:0015168; F:glycerol transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0140070; F:hydrogen peroxide channel activity; ISO:GO_Central. DR GO; GO:0042802; F:identical protein binding; ISO:GO_Central. DR GO; GO:0005223; F:intracellularly cGMP-activated cation channel activity; ISS:UniProtKB. DR GO; GO:0030184; F:nitric oxide transmembrane transporter activity; ISS:UniProtKB. DR GO; GO:0005267; F:potassium channel activity; ISS:UniProtKB. DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0022857; F:transmembrane transporter activity; ISO:GO_Central. DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB. DR GO; GO:0005372; F:water transmembrane transporter activity; IDA:MGI. DR GO; GO:0072488; P:ammonium transmembrane transport; ISS:UniProtKB. DR GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI. DR GO; GO:0035378; P:carbon dioxide transmembrane transport; ISS:UniProtKB. DR GO; GO:0015670; P:carbon dioxide transport; ISS:UniProtKB. DR GO; GO:0006884; P:cell volume homeostasis; ISS:UniProtKB. DR GO; GO:0019725; P:cellular homeostasis; ISS:UniProtKB. DR GO; GO:0071474; P:cellular hyperosmotic response; ISS:UniProtKB. DR GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB. DR GO; GO:0071280; P:cellular response to copper ion; ISS:UniProtKB. DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; ISS:UniProtKB. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB. DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB. DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISS:UniProtKB. DR GO; GO:0071288; P:cellular response to mercury ion; ISS:UniProtKB. DR GO; GO:0071732; P:cellular response to nitric oxide; ISO:GO_Central. DR GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB. DR GO; GO:0071472; P:cellular response to salt stress; ISS:UniProtKB. DR GO; GO:0034644; P:cellular response to UV; ISS:UniProtKB. DR GO; GO:0033326; P:cerebrospinal fluid secretion; IEA:Ensembl. DR GO; GO:0051458; P:corticotropin secretion; IMP:MGI. DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB. DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; ISS:UniProtKB. DR GO; GO:0003094; P:glomerular filtration; IMP:MGI. DR GO; GO:0015793; P:glycerol transmembrane transport; ISS:UniProtKB. DR GO; GO:0006972; P:hyperosmotic response; IBA:GO_Central. DR GO; GO:0009992; P:intracellular water homeostasis; ISS:UniProtKB. DR GO; GO:0021670; P:lateral ventricle development; IEP:UniProtKB. DR GO; GO:0044241; P:lipid digestion; IMP:MGI. DR GO; GO:0072220; P:metanephric descending thin limb development; IEP:UniProtKB. DR GO; GO:0072239; P:metanephric glomerulus vasculature development; IEP:UniProtKB. DR GO; GO:0072232; P:metanephric proximal convoluted tubule segment 2 development; IEP:UniProtKB. DR GO; GO:0072230; P:metanephric proximal straight tubule development; IEP:UniProtKB. DR GO; GO:0050891; P:multicellular organismal-level water homeostasis; IMP:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:0030185; P:nitric oxide transport; ISS:UniProtKB. DR GO; GO:0042476; P:odontogenesis; IEA:Ensembl. DR GO; GO:0030157; P:pancreatic juice secretion; IEA:Ensembl. DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; IMP:MGI. DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:GO_Central. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB. DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:GO_Central. DR GO; GO:0046878; P:positive regulation of saliva secretion; ISS:UniProtKB. DR GO; GO:0006813; P:potassium ion transport; IDA:UniProtKB. DR GO; GO:0070295; P:renal water absorption; IMP:MGI. DR GO; GO:0003097; P:renal water transport; ISO:GO_Central. DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl. DR GO; GO:0032940; P:secretion by cell; IMP:MGI. DR GO; GO:0033363; P:secretory granule organization; IMP:MGI. DR GO; GO:0019233; P:sensory perception of pain; IMP:MGI. DR GO; GO:0035377; P:transepithelial water transport; ISS:UniProtKB. DR GO; GO:0006833; P:water transport; IDA:MGI. DR GO; GO:0042060; P:wound healing; IMP:MGI. DR CDD; cd00333; MIP; 1. DR FunFam; 1.20.1080.10:FF:000012; Aquaporin-1; 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. PE 1: Evidence at protein level; KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome; KW Repeat; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..269 FT /note="Aquaporin-1" FT /id="PRO_0000063921" FT TOPO_DOM 1..11 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 12..29 FT /note="Helical; Name=Helix 1" FT /evidence="ECO:0000250|UniProtKB:P29972" FT TOPO_DOM 30..46 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 47..65 FT /note="Helical; Name=Helix 2" FT /evidence="ECO:0000250|UniProtKB:P29972" FT TOPO_DOM 66..68 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT INTRAMEM 69..82 FT /evidence="ECO:0000250|UniProtKB:P29972" FT TOPO_DOM 83..90 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 91..109 FT /note="Helical; Name=Helix 3" FT /evidence="ECO:0000250|UniProtKB:P29972" FT TOPO_DOM 110..133 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 134..153 FT /note="Helical; Name=Helix 4" FT /evidence="ECO:0000250|UniProtKB:P29972" FT TOPO_DOM 154..163 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 164..181 FT /note="Helical; Name=Helix 5" FT /evidence="ECO:0000250|UniProtKB:P29972" FT TOPO_DOM 182..186 FT /note="Extracellular" FT /evidence="ECO:0000305" FT INTRAMEM 187..199 FT /evidence="ECO:0000250|UniProtKB:P29972" FT TOPO_DOM 200..206 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 207..224 FT /note="Helical; Name=Helix 6" FT /evidence="ECO:0000250|UniProtKB:P29972" FT TOPO_DOM 225..269 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT MOTIF 76..78 FT /note="NPA 1" FT /evidence="ECO:0000250|UniProtKB:P29972" FT MOTIF 192..194 FT /note="NPA 2" FT /evidence="ECO:0000250|UniProtKB:P29972" FT MOD_RES 247 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 253 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 262 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT CARBOHYD 205 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 190 FT /note="G -> S (in Ref. 3; AAH07125)" FT /evidence="ECO:0000305" SQ SEQUENCE 269 AA; 28793 MW; F0499724AD4AB5F6 CRC64; MASEIKKKLF WRAVVAEFLA MTLFVFISIG SALGFNYPLE RNQTLVQDNV KVSLAFGLSI ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS ILRAVMYIIA QCVGAIVATA ILSGITSSLV DNSLGRNDLA HGVNSGQGLG IEIIGTLQLV LCVLATTDRR RRDLGGSAPL AIGLSVALGH LLAIDYTGCG INPARSFGSA VLTRNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDFTD RMKVWTSGQV EEYDLDADDI NSRVEMKPK //