AQP1_MOUSE
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 03-AUG-2022, entry version 186.
DE RecName: Full=Aquaporin-1;
DE Short=AQP-1;
DE AltName: Full=Aquaporin-CHIP;
DE AltName: Full=Delayed early response protein 2;
DE Short=DER2;
DE AltName: Full=Water channel protein for red blood cells and kidney proximal tubule;
GN Name=Aqp1;
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, Pancreas,
RC 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-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:12133842}.
CC -!- SUBUNIT: Homotetramer. Identified in a complex with STOM (By
CC similarity). Interacts with EPHB2; involved in endolymph production in
CC the inner ear. {ECO:0000250, ECO:0000269|PubMed:10839360}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12133842};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12133842}.
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).
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 -!- MISCELLANEOUS: Pharmacologically inhibited by submillimolar
CC concentrations of mercury.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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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 IntAct; Q02013; 1.
DR STRING; 10090.ENSMUSP00000004774; -.
DR GlyGen; Q02013; 1 site.
DR iPTMnet; Q02013; -.
DR PhosphoSitePlus; Q02013; -.
DR SwissPalm; Q02013; -.
DR jPOST; Q02013; -.
DR MaxQB; Q02013; -.
DR PaxDb; Q02013; -.
DR PeptideAtlas; Q02013; -.
DR PRIDE; Q02013; -.
DR ProteomicsDB; 283194; -.
DR DNASU; 11826; -.
DR Ensembl; ENSMUST00000004774; ENSMUSP00000004774; ENSMUSG00000004655.
DR GeneID; 11826; -.
DR KEGG; mmu:11826; -.
DR UCSC; uc009caq.1; mouse.
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; IFKALMY; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; Q02013; -.
DR TreeFam; TF312940; -.
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; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Aqp1; mouse.
DR PRO; PR:Q02013; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q02013; protein.
DR Bgee; ENSMUSG00000004655; Expressed in right lung and 214 other tissues.
DR Genevisible; Q02013; MM.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
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:MGI.
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:0016021; C:integral component of membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0032809; C:neuronal cell body membrane; ISO:MGI.
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 transmembrane transporter 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:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0005223; F:intracellular 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:MGI.
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:0016477; P:cell migration; IMP:MGI.
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:0071241; P:cellular response to inorganic substance; 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:MGI.
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:0009992; P:cellular water homeostasis; ISS:UniProtKB.
DR GO; GO:0033326; P:cerebrospinal fluid secretion; IEA:Ensembl.
DR GO; GO:0019934; P:cGMP-mediated signaling; ISS:UniProtKB.
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:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; ISS:UniProtKB.
DR GO; GO:0010761; P:fibroblast migration; IMP:MGI.
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:0042538; P:hyperosmotic salinity response; IEA:Ensembl.
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:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
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:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; ISO:MGI.
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:MGI.
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:0030104; P:water homeostasis; IMP:MGI.
DR GO; GO:0006833; P:water transport; IDA:MGI.
DR GO; GO:0042060; P:wound healing; IMP:MGI.
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 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..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 8..36
FT /note="Helical; Name=Helix 1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 37..48
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 49..66
FT /note="Helical; Name=Helix 2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 67..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT INTRAMEM 71..76
FT /evidence="ECO:0000250"
FT INTRAMEM 77..84
FT /note="Helical; Name=Helix B"
FT /evidence="ECO:0000250"
FT TOPO_DOM 85..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 95..115
FT /note="Helical; Name=Helix 3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 116..136
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 137..155
FT /note="Helical; Name=Helix 4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 156..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 167..183
FT /note="Helical; Name=Helix 5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 184..186
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT INTRAMEM 187..192
FT /evidence="ECO:0000250"
FT INTRAMEM 193..200
FT /note="Helical; Name=Helix E"
FT /evidence="ECO:0000250"
FT TOPO_DOM 201..207
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 208..228
FT /note="Helical; Name=Helix 6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 229..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 76..78
FT /note="NPA 1"
FT MOTIF 192..194
FT /note="NPA 2"
FT SITE 56
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250"
FT SITE 180
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250"
FT SITE 189
FT /note="Hg(2+)-sensitive residue"
FT /evidence="ECO:0000250"
FT SITE 195
FT /note="Substrate discrimination"
FT /evidence="ECO:0000250"
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
