ID AQP11_RAT Reviewed; 271 AA.
AC Q8CHM1; Q6AZ79;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 24-JAN-2024, entry version 123.
DE RecName: Full=Aquaporin-11 {ECO:0000305|Ref.1};
DE Short=AQP-11 {ECO:0000305|Ref.1};
GN Name=Aqp11 {ECO:0000312|RGD:628763};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Ishibashi K., Imai M.;
RT "Cloning of a new superfamily of aquaporin.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=19812234; DOI=10.1530/rep-09-0298;
RA Yeung C.H., Cooper T.G.;
RT "Aquaporin AQP11 in the testis: molecular identity and association with the
RT processing of residual cytoplasm of elongated spermatids.";
RL Reproduction 139:209-216(2010).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=27107718; DOI=10.1186/s12974-016-0554-2;
RA Deeg C.A., Amann B., Lutz K., Hirmer S., Lutterberg K., Kremmer E.,
RA Hauck S.M.;
RT "Aquaporin 11, a regulator of water efflux at retinal Mueller glial cell
RT surface decreases concomitant with immune-mediated gliosis.";
RL J. Neuroinflamm. 13:89-89(2016).
CC -!- FUNCTION: Channel protein that facilitates the transport of water,
CC glycerol and hydrogen peroxide across membrane of cell or organelles
CC guaranteeing intracellular homeostasis in several organes like liver,
CC kidney and brain. In situation of stress, participates in endoplasmic
CC reticulum (ER) homeostasis by regulating redox homeostasis through the
CC transport of hydrogen peroxide across the endoplasmic reticulum
CC membrane thereby regulating the oxidative stress through the NADPH
CC oxidase 2 pathway (By similarity). Plays a role by maintaining an
CC environment suitable for translation or protein foldings in the ER
CC lumen namely by participating in the PKD1 glycosylation processing
CC resulting in regulation of PKD1 membrane trafficking thereby preventing
CC the accumulation of unfolding protein in ER. Plays a role in the
CC proximal tubule function by regulating its endosomal acidification. May
CC play a role in postnatal kidney development (By similarity).
CC {ECO:0000250|UniProtKB:Q8BHH1, ECO:0000250|UniProtKB:Q8NBQ7}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Homotrimer (By similarity). Can
CC also form homomultimer (By similarity). {ECO:0000250|UniProtKB:Q8BHH1,
CC ECO:0000250|UniProtKB:Q8NBQ7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8NBQ7}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8NBQ7}. Cell membrane
CC {ECO:0000250|UniProtKB:Q8NBQ7}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8NBQ7}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8BHH1}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8BHH1}. Note=Localizes mainly to the periphery
CC of lipid droplets. it accumulates partly in mitochondrial-associated
CC endoplasmic reticulum membranes. {ECO:0000250|UniProtKB:Q8NBQ7}.
CC -!- TISSUE SPECIFICITY: Expressed in retina specifically at retinal Mueller
CC glial cells (PubMed:27107718). Expressed in adult testis, in the
CC elongated spermatids (ES) and in residual bodies inside Sertoli cells
CC (PubMed:19812234). {ECO:0000269|PubMed:19812234,
CC ECO:0000269|PubMed:27107718}.
CC -!- DOMAIN: The NPC motif is essential for oligomerization and water
CC permeability function. {ECO:0000250|UniProtKB:Q8BHH1}.
CC -!- PTM: Not glycosylated. {ECO:0000250|UniProtKB:Q8NBQ7}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. AQP11/AQP12
CC subfamily. {ECO:0000305}.
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DR EMBL; AB023644; BAC45003.1; -; mRNA.
DR EMBL; BC078694; AAH78694.1; -; mRNA.
DR RefSeq; NP_775128.1; NM_173105.1.
DR AlphaFoldDB; Q8CHM1; -.
DR SMR; Q8CHM1; -.
DR STRING; 10116.ENSRNOP00000018091; -.
DR PaxDb; 10116-ENSRNOP00000018091; -.
DR Ensembl; ENSRNOT00055051857; ENSRNOP00055042794; ENSRNOG00055029934.
DR Ensembl; ENSRNOT00060003947; ENSRNOP00060002788; ENSRNOG00060002461.
DR Ensembl; ENSRNOT00065036759; ENSRNOP00065029597; ENSRNOG00065021617.
DR GeneID; 286758; -.
DR KEGG; rno:286758; -.
DR UCSC; RGD:628763; rat.
DR AGR; RGD:628763; -.
DR CTD; 282679; -.
DR RGD; 628763; Aqp11.
DR VEuPathDB; HostDB:ENSRNOG00000013358; -.
DR eggNOG; ENOG502S15B; Eukaryota.
DR HOGENOM; CLU_074449_0_0_1; -.
DR InParanoid; Q8CHM1; -.
DR OrthoDB; 2875321at2759; -.
DR PhylomeDB; Q8CHM1; -.
DR TreeFam; TF320251; -.
DR Reactome; R-RNO-432047; Passive transport by Aquaporins.
DR PRO; PR:Q8CHM1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000013358; Expressed in testis and 16 other cell types or tissues.
DR Genevisible; Q8CHM1; RN.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0015267; F:channel activity; IBA:GO_Central.
DR GO; GO:0015254; F:glycerol channel activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR GO; GO:0048388; P:endosomal lumen acidification; ISO:RGD.
DR GO; GO:0015793; P:glycerol transmembrane transport; ISS:UniProtKB.
DR GO; GO:0080170; P:hydrogen peroxide transmembrane transport; ISS:UniProtKB.
DR GO; GO:0032364; P:intracellular oxygen homeostasis; ISO:RGD.
DR GO; GO:0009992; P:intracellular water homeostasis; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:1904293; P:negative regulation of ERAD pathway; ISS:UniProtKB.
DR GO; GO:1903573; P:negative regulation of response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0072014; P:proximal tubule development; ISS:UniProtKB.
DR GO; GO:0006833; P:water transport; ISS:UniProtKB.
DR Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR023266; Aquaporin_11.
DR InterPro; IPR016697; Aquaporin_11/12.
DR InterPro; IPR000425; MIP.
DR PANTHER; PTHR21191; AQUAPORIN; 1.
DR PANTHER; PTHR21191:SF7; AQUAPORIN-11; 1.
DR Pfam; PF00230; MIP; 1.
DR PIRSF; PIRSF017529; Aquaporin_11/12; 1.
DR PRINTS; PR02024; AQUAPORIN11.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; Aquaporin-like; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cytoplasm; Cytoplasmic vesicle; Disulfide bond;
KW Endoplasmic reticulum; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..271
FT /note="Aquaporin-11"
FT /id="PRO_0000063970"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..41
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..166
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..234
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..271
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q8NBQ7"
FT MOTIF 99..101
FT /note="NPC"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT MOTIF 216..218
FT /note="NPA"
FT /evidence="ECO:0000250|UniProtKB:Q96PS8"
FT CONFLICT 150
FT /note="E -> K (in Ref. 1; BAC45003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 30369 MW; C309985D82B1E748 CRC64;
MSALLGLPPE VQDTCISLGL MLLVVLFMGL ARVIARQQLH RPMVHAFVLE FLATFQLCYC
THELQLLSEQ DSGHPTWTLT LIYFFSLVHG LTLVGTASNP CGVMMQMILG GMSPEMGAVR
LMAQLVSALC SRYCISALWS LSLTKYHFDE RILACRNPIN TDISKAIIIE AICSFIFHSA
LLHFQEVRTK LRIHVLAALI TFLAYAGGSL TGALFNPALA LSLHFPCFDE SFYKFFVVYW
VAPSLGVLLM ILMFSFFLPW LHNNQLSNKK E
//
