AQP8_RAT
ID AQP8_RAT Reviewed; 263 AA.
AC P56405;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Aquaporin-8;
DE Short=AQP-8;
GN Name=Aqp8;
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 STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=9299432; DOI=10.1006/bbrc.1997.7219;
RA Ishibashi K., Kuwahara M., Kageyama Y., Tohsaka A., Marumo F., Sasaki S.;
RT "Cloning and functional expression of a second new aquaporin abundantly
RT expressed in testis.";
RL Biochem. Biophys. Res. Commun. 237:714-718(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver, and Pancreas;
RX PubMed=9374520; DOI=10.1074/jbc.272.48.30329;
RA Koyama Y., Yamamoto T., Kondo D., Funaki H., Yaoita E., Kawasaki K.,
RA Sato N., Hatakeyama K., Kihara I.;
RT "Molecular cloning of a new aquaporin from rat pancreas and liver.";
RL J. Biol. Chem. 272:30329-30333(1997).
RN [3]
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).
CC -!- FUNCTION: Forms a water-specific channel; mercury-sensitive. It may
CC have an important role in spermatogenesis, in fertilization, and in the
CC secretion of pancreatic juice and saliva.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in sperm, pancreas and liver. Some
CC expression has been found in salivary gland and absorptive colonic
CC epithelial cells.
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 -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; AB005547; BAA21918.1; -; mRNA.
DR EMBL; AF007775; AAC53463.1; -; mRNA.
DR EMBL; BC081812; AAH81812.1; -; mRNA.
DR PIR; JC5622; JC5622.
DR RefSeq; NP_062031.1; NM_019158.2.
DR AlphaFoldDB; P56405; -.
DR SMR; P56405; -.
DR STRING; 10116.ENSRNOP00000019939; -.
DR GlyGen; P56405; 1 site.
DR PaxDb; P56405; -.
DR GeneID; 29172; -.
DR KEGG; rno:29172; -.
DR UCSC; RGD:2146; rat.
DR CTD; 343; -.
DR RGD; 2146; Aqp8.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_5_1; -.
DR InParanoid; P56405; -.
DR OrthoDB; 1152704at2759; -.
DR PhylomeDB; P56405; -.
DR TreeFam; TF312940; -.
DR Reactome; R-RNO-432047; Passive transport by Aquaporins.
DR PRO; PR:P56405; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P56405; RN.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046691; C:intracellular canaliculus; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0015250; F:water channel activity; IDA:RGD.
DR GO; GO:0015722; P:canalicular bile acid transport; IDA:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:RGD.
DR GO; GO:0006833; P:water transport; IDA:RGD.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR023277; Aquaporin_8.
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; PR02020; AQUAPORIN8.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
DR PROSITE; PS00221; MIP; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..263
FT /note="Aquaporin-8"
FT /id="PRO_0000063963"
FT TOPO_DOM 1..38
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..86
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 131..158
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..185
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 207..230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 94..96
FT /note="NPA 1"
FT MOTIF 212..214
FT /note="NPA 2"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 263 AA; 28055 MW; B34AC8ACFA596BD2 CRC64;
MSGEQTPMCS MDLREIKGKE TNMADSYHGM SWYEQYIQPC VVELLGSALF IFIGCLSVIE
NSPNTGLLQP ALAHGLALGL IIATLGNISG GHFNPAVSLA VTLVGGLKTM LLIPYWVSQL
FGGMIGAALA KVVSPEERFW NASGAAFAIV QEQEQVAEAL GVEIVMTMLL VLAVCMGAVN
EKTMGPLAPF SIGFSVIVDI LAGGGISGAC MNPARAFGPA VMAGYWDFHW IYWLGPLLAG
LFVGLLIRLF IGDEKTRLIL KSR
