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Aquaporin-B

 AQPB_DICDI              Reviewed;         294 AA.
Q54WT8;
18-APR-2012, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
23-MAY-2018, entry version 97.
RecName: Full=Aquaporin-B;
Name=aqpB {ECO:0000303|PubMed:22262860}; ORFNames=DDB_G0279443;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyostelids; Dictyosteliales;
Dictyosteliaceae; Dictyostelium.
NCBI_TaxID=44689;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), ALTERNATIVE INITIATION,
FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION,
GLYCOSYLATION, AND MUTAGENESIS OF SER-120; 208-SER--ASN-212;
208-SER--SER-219 AND ASP-275.
STRAIN=AX2 {ECO:0000269|PubMed:22262860};
PubMed=22262860; DOI=10.1074/jbc.M111.329102;
von Buelow J., Mueller-Lucks A., Kai L., Bernhard F., Beitz E.;
"Functional characterization of a novel aquaporin from Dictyostelium
discoideum amoebae implies a unique gating mechanism.";
J. Biol. Chem. 287:7487-7494(2012).
[2] {ECO:0000312|EMBL:EAL67660.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
-!- FUNCTION: Putatively gated water-specific channel, requiring a
cysteine residue within the channel. Impermeable to water,
glycerol and urea when expressed in Xenopus oocytes. Not regulated
by pH; channels remain impermeable to water at pH 7.4 and 5.2.
{ECO:0000269|PubMed:22262860}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22262860};
Multi-pass membrane protein {ECO:0000269|PubMed:22262860}.
Cytoplasmic vesicle {ECO:0000269|PubMed:22262860}. Note=Expressed
in lamellipodia-like protrusions of the plasma membrane and
intracellular vacuolar structures. {ECO:0000255,
ECO:0000269|PubMed:22262860}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Long {ECO:0000269|PubMed:22262860};
IsoId=Q54WT8-1; Sequence=Displayed;
Name=Short {ECO:0000269|PubMed:22262860};
IsoId=Q54WT8-2; Sequence=VSP_043004;
-!- DEVELOPMENTAL STAGE: Expressed throughout development from amoebae
through to the formation of spores at 24 hours. Highest expression
is at 12 and 24 hours. {ECO:0000269|PubMed:22262860}.
-!- INDUCTION: Inhibited by mercuric chloride.
{ECO:0000269|PubMed:22262860}.
-!- DOMAIN: Aquaporins contain two tandem repeats each containing
three membrane-spanning domains and a pore-forming loop with the
signature motif Asn-Pro-Ala (NPA). {ECO:0000250|UniProtKB:Q9U8P7}.
-!- PTM: Glycosylated and non-glycosylated forms exist throughout all
developmental stages. {ECO:0000269|PubMed:22262860}.
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
{ECO:0000255}.
-----------------------------------------------------------------------
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EMBL; AAFI02000031; EAL67660.1; -; Genomic_DNA.
RefSeq; XP_641629.1; XM_636537.1.
ProteinModelPortal; Q54WT8; -.
STRING; 44689.DDB0205768; -.
TCDB; 1.A.8.10.8; the major intrinsic protein (mip) family.
iPTMnet; Q54WT8; -.
PaxDb; Q54WT8; -.
EnsemblProtists; EAL67660; EAL67660; DDB_G0279443.
GeneID; 8622035; -.
KEGG; ddi:DDB_G0279443; -.
dictyBase; DDB_G0279443; aqpB.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
InParanoid; Q54WT8; -.
KO; K09885; -.
OMA; ELFGTFW; -.
PhylomeDB; Q54WT8; -.
PRO; PR:Q54WT8; -.
Proteomes; UP000002195; Chromosome 3.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:dictyBase.
GO; GO:0005773; C:vacuole; IDA:dictyBase.
GO; GO:0015250; F:water channel activity; IBA:GO_Central.
GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
CDD; cd00333; MIP; 1.
Gene3D; 1.20.1080.10; -; 2.
InterPro; IPR023271; Aquaporin-like.
InterPro; IPR034294; Aquaporin_transptr.
InterPro; IPR000425; MIP.
InterPro; IPR022357; MIP_CS.
PANTHER; PTHR19139; PTHR19139; 1.
Pfam; PF00230; MIP; 1.
PRINTS; PR00783; MINTRINSICP.
SUPFAM; SSF81338; SSF81338; 1.
PROSITE; PS00221; MIP; 1.
1: Evidence at protein level;
Alternative initiation; Cell membrane; Complete proteome;
Cytoplasmic vesicle; Glycoprotein; Membrane; Phosphoprotein;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 294 Aquaporin-B.
/FTId=PRO_0000416937.
TOPO_DOM 1 42 Cytoplasmic. {ECO:0000255}.
TRANSMEM 43 63 Helical. {ECO:0000255}.
TOPO_DOM 64 79 Extracellular. {ECO:0000255}.
TRANSMEM 80 100 Helical. {ECO:0000255}.
TOPO_DOM 101 123 Cytoplasmic. {ECO:0000255}.
TRANSMEM 124 144 Helical. {ECO:0000255}.
TOPO_DOM 145 172 Extracellular. {ECO:0000255}.
TRANSMEM 173 193 Helical. {ECO:0000255}.
TOPO_DOM 194 224 Cytoplasmic. {ECO:0000255}.
TRANSMEM 225 245 Helical. {ECO:0000255}.
TOPO_DOM 246 268 Extracellular. {ECO:0000255}.
TRANSMEM 269 289 Helical. {ECO:0000255}.
TOPO_DOM 290 294 Cytoplasmic. {ECO:0000255}.
REGION 208 219 Required for water permeability.
{ECO:0000269|PubMed:22262860}.
MOTIF 106 108 NPA 1. {ECO:0000250|UniProtKB:Q9U8P7}.
MOTIF 251 253 NPA 2. {ECO:0000250|UniProtKB:Q9U8P7}.
SITE 239 239 Selectivity filter.
{ECO:0000269|PubMed:22262860}.
CARBOHYD 75 75 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:22262860}.
VAR_SEQ 1 17 Missing (in isoform Short).
{ECO:0000303|PubMed:22262860}.
/FTId=VSP_043004.
MUTAGEN 120 120 S->A: Permanently unphosphorylated state,
impermeable to water in Xenopus oocytes.
{ECO:0000269|PubMed:22262860}.
MUTAGEN 120 120 S->D: Permanently phosphorylated,
impermeable to water in Xenopus oocytes.
{ECO:0000269|PubMed:22262860}.
MUTAGEN 208 219 Missing: Permeable to water in Xenopus
oocytes and liposomes, impermeable to
glycerol and urea.
{ECO:0000269|PubMed:22262860}.
MUTAGEN 208 212 Missing: Impermeable to water in Xenopus
oocytes. {ECO:0000269|PubMed:22262860}.
MUTAGEN 275 275 D->A: Impermeable to water in Xenopus
oocytes. {ECO:0000269|PubMed:22262860}.
MUTAGEN 275 275 D->P: Impermeable to water in Xenopus
oocytes. {ECO:0000269|PubMed:22262860}.
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


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