AQPB_DICDI
ID AQPB_DICDI Reviewed; 294 AA.
AC Q54WT8;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Aquaporin-B;
GN Name=aqpB {ECO:0000303|PubMed:22262860}; ORFNames=DDB_G0279443;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), ALTERNATIVE INITIATION,
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION,
RP GLYCOSYLATION, AND MUTAGENESIS OF SER-120; 208-SER--ASN-212;
RP 208-SER--SER-219 AND ASP-275.
RC STRAIN=AX2 {ECO:0000269|PubMed:22262860};
RX PubMed=22262860; DOI=10.1074/jbc.m111.329102;
RA von Buelow J., Mueller-Lucks A., Kai L., Bernhard F., Beitz E.;
RT "Functional characterization of a novel aquaporin from Dictyostelium
RT discoideum amoebae implies a unique gating mechanism.";
RL J. Biol. Chem. 287:7487-7494(2012).
RN [2] {ECO:0000312|EMBL:EAL67660.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Putatively gated water-specific channel, requiring a cysteine
CC residue within the channel. Impermeable to water, glycerol and urea
CC when expressed in Xenopus oocytes. Not regulated by pH; channels remain
CC impermeable to water at pH 7.4 and 5.2. {ECO:0000269|PubMed:22262860}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22262860};
CC Multi-pass membrane protein {ECO:0000269|PubMed:22262860}. Cytoplasmic
CC vesicle {ECO:0000269|PubMed:22262860}. Note=Expressed in lamellipodia-
CC like protrusions of the plasma membrane and intracellular vacuolar
CC structures. {ECO:0000255, ECO:0000269|PubMed:22262860}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long {ECO:0000269|PubMed:22262860};
CC IsoId=Q54WT8-1; Sequence=Displayed;
CC Name=Short {ECO:0000269|PubMed:22262860};
CC IsoId=Q54WT8-2; Sequence=VSP_043004;
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development from amoebae
CC through to the formation of spores at 24 hours. Highest expression is
CC at 12 and 24 hours. {ECO:0000269|PubMed:22262860}.
CC -!- INDUCTION: Inhibited by mercuric chloride.
CC {ECO:0000269|PubMed:22262860}.
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:Q9U8P7}.
CC -!- PTM: Glycosylated and non-glycosylated forms exist throughout all
CC developmental stages. {ECO:0000269|PubMed:22262860}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000255}.
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DR EMBL; AAFI02000031; EAL67660.1; -; Genomic_DNA.
DR RefSeq; XP_641629.1; XM_636537.1.
DR AlphaFoldDB; Q54WT8; -.
DR SMR; Q54WT8; -.
DR STRING; 44689.DDB0205768; -.
DR TCDB; 1.A.8.10.8; the major intrinsic protein (mip) family.
DR iPTMnet; Q54WT8; -.
DR PaxDb; Q54WT8; -.
DR EnsemblProtists; EAL67660; EAL67660; DDB_G0279443.
DR GeneID; 8622035; -.
DR KEGG; ddi:DDB_G0279443; -.
DR dictyBase; DDB_G0279443; aqpB.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_4_1; -.
DR InParanoid; Q54WT8; -.
DR OMA; MAIQVTW; -.
DR PhylomeDB; Q54WT8; -.
DR Reactome; R-DDI-432047; Passive transport by Aquaporins.
DR PRO; PR:Q54WT8; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:dictyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
DR GO; GO:0015250; F:water channel activity; IBA:GO_Central.
DR GO; GO:0048870; P:cell motility; IMP:dictyBase.
DR GO; GO:0006971; P:hypotonic response; IMP:dictyBase.
DR GO; GO:0006833; P:water transport; IBA:GO_Central.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR45665; PTHR45665; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR PROSITE; PS00221; MIP; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Cell membrane; Cytoplasmic vesicle; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..294
FT /note="Aquaporin-B"
FT /id="PRO_0000416937"
FT TOPO_DOM 1..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..79
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..172
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..219
FT /note="Required for water permeability"
FT /evidence="ECO:0000269|PubMed:22262860"
FT MOTIF 106..108
FT /note="NPA 1"
FT /evidence="ECO:0000250|UniProtKB:Q9U8P7"
FT MOTIF 251..253
FT /note="NPA 2"
FT /evidence="ECO:0000250|UniProtKB:Q9U8P7"
FT SITE 239
FT /note="Selectivity filter"
FT /evidence="ECO:0000269|PubMed:22262860"
FT CARBOHYD 75
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000269|PubMed:22262860"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:22262860"
FT /id="VSP_043004"
FT MUTAGEN 120
FT /note="S->A: Permanently unphosphorylated state,
FT impermeable to water in Xenopus oocytes."
FT /evidence="ECO:0000269|PubMed:22262860"
FT MUTAGEN 120
FT /note="S->D: Permanently phosphorylated, impermeable to
FT water in Xenopus oocytes."
FT /evidence="ECO:0000269|PubMed:22262860"
FT MUTAGEN 208..219
FT /note="Missing: Permeable to water in Xenopus oocytes and
FT liposomes, impermeable to glycerol and urea."
FT /evidence="ECO:0000269|PubMed:22262860"
FT MUTAGEN 208..212
FT /note="Missing: Impermeable to water in Xenopus oocytes."
FT /evidence="ECO:0000269|PubMed:22262860"
FT MUTAGEN 275
FT /note="D->A: Impermeable to water in Xenopus oocytes."
FT /evidence="ECO:0000269|PubMed:22262860"
FT MUTAGEN 275
FT /note="D->P: Impermeable to water in Xenopus oocytes."
FT /evidence="ECO:0000269|PubMed:22262860"
SQ SEQUENCE 294 AA; 31243 MW; DA7DBA7431177033 CRC64;
MSLKRSDDYQ DLEEGIAMED GGNIKDEEEK PLDPIEEQNK KRWVLIRAVL GELLCTFLFV
YVLCATSANF IRLGSPPNPV VGGLSTGFAA VALIYSFADV SGAHFNPAVT FATCVTRKTS
ITKGLMYVGA QLVGSVLASL ILLATFPGNF PGDKNAASAV AIAPSTDANI GNAFLTELVL
TFILVYVIFA VAFDTVDNSV KTKVVGKSSS NNLTIYTTSG QTKAGFAPIA IGFTLGFLCF
LGGSVSGGAF NPARVFGTAL VGNNWTRHWM YWIADFLGAG LAGFAQKFFS STHK
