ID A0A2V5I629_9EURO Unreviewed; 260 AA.
AC A0A2V5I629;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 03-MAY-2023, entry version 13.
DE SubName: Full=Aquaporin-like protein {ECO:0000313|EMBL:PYI32235.1};
GN ORFNames=BP00DRAFT_425011 {ECO:0000313|EMBL:PYI32235.1};
OS Aspergillus indologenus CBS 114.80.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450541 {ECO:0000313|EMBL:PYI32235.1, ECO:0000313|Proteomes:UP000248817};
RN [1] {ECO:0000313|EMBL:PYI32235.1, ECO:0000313|Proteomes:UP000248817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114.80 {ECO:0000313|EMBL:PYI32235.1,
RC ECO:0000313|Proteomes:UP000248817};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O(in) = H2O(out); Xref=Rhea:RHEA:29667, ChEBI:CHEBI:15377;
CC Evidence={ECO:0000256|ARBA:ARBA00034651};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC {ECO:0000256|RuleBase:RU000477}.
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DR EMBL; KZ825494; PYI32235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V5I629; -.
DR Proteomes; UP000248817; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR000425; MIP.
DR PANTHER; PTHR47002; AQUAPORIN-LIKE; 1.
DR PANTHER; PTHR47002:SF2; AQUAPORIN-LIKE; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; Aquaporin-like; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000477};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|RuleBase:RU000477}.
FT TRANSMEM 81..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 260 AA; 27925 MW; 819503E55A8FC5D8 CRC64;
MLNTFISAWV TTHPYAAMTA STAASGVYGT VTFFSPTFGG LTNLLLTPLL IYTFSPSSGG
HINPLITLAT FFARIISFPR AVLYILGQTL GGALAGLALH AAFGDRRITV GGCYIDTAQV
PVTSGLVIEF FACLIVVWLC FGVALDPRQA RVFGPAVGPW LVGVVVGVVT WGTSFTRTGY
IGASRFSVPR GCWWRERGFG VMVEANAMIG VNPARCFGAY VASEFPGYHW IHWVGPLAAS
VAHGFVYFVD PLWKDPRSKS
//