AQP6_MILTA
ID AQP6_MILTA Reviewed; 285 AA.
AC G5CTG3;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2013, sequence version 2.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Aquaporin-6 {ECO:0000303|PubMed:23761966};
DE Short=AQP-6 {ECO:0000303|PubMed:23761966};
GN Name=AQP6 {ECO:0000303|PubMed:23761966};
OS Milnesium tardigradum (Water bear) (Tardigrade).
OC Eukaryota; Metazoa; Ecdysozoa; Tardigrada; Eutardigrada; Apochela;
OC Milnesiidae; Milnesium.
OX NCBI_TaxID=46460;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DOMAIN, AND INDUCTION.
RX PubMed=23761966; DOI=10.4137/bbi.s11497;
RA Grohme M.A., Mali B., Welnicz W., Michel S., Schill R.O., Frohme M.;
RT "The aquaporin channel repertoire of the tardigrade Milnesium
RT tardigradum.";
RL Bioinf. Biol. Insights 7:153-165(2013).
CC -!- FUNCTION: Probable water-specific aquaporin that may modulate the water
CC content and osmolytes during anhydrobiosis (PubMed:23761966).
CC {ECO:0000305|PubMed:23761966}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Transcript abundance is low and expression levels are not
CC significantly affected by desiccation or rehydratation
CC (PubMed:23761966). {ECO:0000269|PubMed:23761966}.
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:0000305|PubMed:23761966}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000305}.
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DR EMBL; JN378741; AEP14560.2; -; mRNA.
DR AlphaFoldDB; G5CTG3; -.
DR SMR; G5CTG3; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015250; F:water channel activity; ISS:UniProtKB.
DR GO; GO:0003097; P:renal water transport; ISS:UniProtKB.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR PANTHER; PTHR19139; PTHR19139; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Repeat; Stress response;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..285
FT /note="Aquaporin-6"
FT /id="PRO_0000440207"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 86..88
FT /note="NPA 1"
FT MOTIF 206..208
FT /note="NPA 2"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 285 AA; 31694 MW; BDE0AED1D3DF4BDD CRC64;
MAFMDKSEVR QRLQKVLQQC AKAPTWSPKE EVRQSIFWKS IRAELIGSLV LMVFSCSRDS
IYGPVSYGCT YAILSYCFKS ISAHFNPVIT IAALLLRSIT PFRCISLVLA QTLGTLSGAS
VCYYGLSNET ETGSAPISPV LNVSPAKGFG YEFFGTFVII LTMSSYLDCN DYVSESGDSN
LLPLIFGLSV GLSSGMARQA TGGFLNPMRA FSLALFELNH WSNHYIYWIG PIFGCLLAVF
TFDYTRPIIP NRDSNNRINF PTFNKNNKYE VEMQPETEIT LATLA
