ID A0A166K3F2_9AGAM Unreviewed; 459 AA.
AC A0A166K3F2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Aquaporin {ECO:0000313|EMBL:KZV75256.1};
GN ORFNames=PENSPDRAFT_600272 {ECO:0000313|EMBL:KZV75256.1};
OS Peniophora sp. CONT.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Russulales; Peniophoraceae; Peniophora.
OX NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV75256.1, ECO:0000313|Proteomes:UP000077086};
RN [1] {ECO:0000313|EMBL:KZV75256.1, ECO:0000313|Proteomes:UP000077086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CONT {ECO:0000313|EMBL:KZV75256.1,
RC ECO:0000313|Proteomes:UP000077086};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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|ARBA:ARBA00006175, ECO:0000256|RuleBase:RU000477}.
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DR EMBL; KV424473; KZV75256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166K3F2; -.
DR STRING; 1314672.A0A166K3F2; -.
DR InParanoid; A0A166K3F2; -.
DR OrthoDB; 5490746at2759; -.
DR Proteomes; UP000077086; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR GO; GO:0015791; P:polyol transmembrane transport; IEA:UniProt.
DR CDD; cd00333; MIP; 1.
DR Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR022357; MIP_CS.
DR NCBIfam; TIGR00861; MIP; 1.
DR PANTHER; PTHR43829; AQUAPORIN OR AQUAGLYCEROPORIN RELATED; 1.
DR PANTHER; PTHR43829:SF9; AQUAPORIN OR AQUAGLYCEROPORIN RELATED; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; Aquaporin-like; 1.
DR PROSITE; PS00221; MIP; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077086};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000477};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000477}.
FT TRANSMEM 176..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 316..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 399..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 35..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 48910 MW; 5D2AA20A75AB4DA5 CRC64;
MNELNSASLA THFERPTFTA LASIFAPMSS GKTTIVDKSD GGSVGRSQDG HEGGMMDTRS
EGGEDSTMAS MAGGTMNGRM GSSSMATTAA PSTMMTTAPS AMTTQNAGMQ SAGMTSTMQN
TGGMMDMMAP IGKSEPGPGQ PAIADEALAL EYNRLVDYHA RYPNVWSSIR EPFRECAAEA
LGTFILCLAG IGTNLQVGLS ARSDIAPAPR GDWNSISWGW SLGVAIAVWV AGGVSGGHVN
PAVTISFAVF RRFPWRKVPF YIAAQVFGAF LAGLVCYFNY SHALTIYEGS PTIRTVPGTA
AFLTCYALDY VSNTNAFFDA FIGPFILMVV LFAVTDRTNG GGVRRELVPL VAFATLFVIS
SGFGYQTLWA LNPARDFGPR LATYLVGYGT AVWTYRGQYW LWCNICSPIL GAVCGSLVYE
LFINVGPDSI INTPSRAARQ YLRATVPGAD EKMKAAEMV
//
