AQP8_MILTA
ID AQP8_MILTA Reviewed; 342 AA.
AC G5CTG5;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Aquaporin-8 {ECO:0000303|PubMed:23761966};
DE Short=AQP-8 {ECO:0000303|PubMed:23761966};
GN Name=AQP8 {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: Aquaglyceroporin that may modulate the water content and
CC 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 but expression is slightly up-
CC regulated in the inactive stage (during anhydrobiois)
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; JN378743; AEP14562.1; -; mRNA.
DR AlphaFoldDB; G5CTG5; -.
DR SMR; G5CTG5; -.
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:0015267; F:channel activity; IEA:InterPro.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR000425; MIP.
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..342
FT /note="Aquaporin-8"
FT /id="PRO_0000440209"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 302..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 108..110
FT /note="NPA 1"
FT MOTIF 240..242
FT /note="NPA 2"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 342 AA; 37279 MW; F684F08AF524A57F CRC64;
MSTAESRNHY KEVPTIEHYS EAIGITNRKK MDWRGWLRKS TLVRSQLIRG CMAEFLAVFV
LMVFIEGSAA TAIFTNRRQD ILFGSISSGL GVAMAVYVAG GVSGAFLNPA VALAFAVLGK
LSWKNCIFYM ISQYLAAFVA SCTMFAYLYE ALNNFDGGER QMFGPNGTAH IWSTYPQPFL
SPHTAFADQV FCTAILLIVV LAMCDSKNWK PHNGFLPIAI GLLIITISCT LSYNAGAAMN
PSRDLAPRFF SYLAGYGTEP FGVKGYTWFF VPVLGSHCGA IIGGAIYQLF IGGQWPDDTS
DTNSVSSMSY NEDNSTLTKR KQVSNIVHDS KGAKGSSTAP VN
