ID A0A2X0M794_9BASI Unreviewed; 462 AA.
AC A0A2X0M794;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=BQ5605_C001g00629 protein {ECO:0000313|EMBL:SGY48213.1};
GN Name=BQ5605_C001g00629 {ECO:0000313|EMBL:SGY48213.1};
GN ORFNames=BQ5605_C001G00629 {ECO:0000313|EMBL:SGY48213.1};
OS Microbotryum silenes-dioicae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=796604 {ECO:0000313|EMBL:SGY48213.1, ECO:0000313|Proteomes:UP000249464};
RN [1] {ECO:0000313|EMBL:SGY48213.1, ECO:0000313|Proteomes:UP000249464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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|ARBA:ARBA00006175, ECO:0000256|RuleBase:RU000477}.
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DR EMBL; FQNC01000043; SGY48213.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X0M794; -.
DR STRING; 796604.A0A2X0M794; -.
DR Proteomes; UP000249464; 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:UP000249464};
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 152..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 313..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 23..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 49703 MW; DC76EA260D5B6F8F CRC64;
MNTSLTSDMN NGQAHRVFNH YQSNTGSHVA GTGDDVHQAP AGSASRRDSG RLAPPVSGAP
VCHDHAGEAE NGDGNVVGVT GQQQNLASKA GRPHSIIDGA GTSVVPASVP SRSYVRRNPF
HRAHIRHHHQ RVQISLDEEH YRNPWFSFRS KYRVYLAEFL GTLILVLWGE GTQAQVIALR
NAPNDYLSIA WGWGVGFMLA ISVSSGISGG HINPAVTISL AVFRKFPWRR VPGYIFSQLL
GAFVAAAILF GVYYGPLNTA EKGYLAAVLT TAPAGKLEGL ISIFFSVFSG AALLMGAIAA
FTDTGNNPAA PGLVPLLLGL VMVGIASSFG YQTGFVLNPA RDVGPRLLSW AVGAPTQSLW
VDNYHYGIWI PTVGTICGAL FGNLIYDLCI YGGRDSPLNY NFSKSGRRAH RLRVQAEKDL
ENGVLPAEDG HHFEERNSDV TLRNEEQEQG GPVGVTTEGK EY
//