ID M7WL99_RHOT1 Unreviewed; 416 AA.
AC M7WL99;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Aquaporin {ECO:0000313|EMBL:EMS18630.1};
GN ORFNames=RHTO_05733 {ECO:0000313|EMBL:EMS18630.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS18630.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS18630.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS18630.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
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; KB722677; EMS18630.1; -; Genomic_DNA.
DR RefSeq; XP_016269749.1; XM_016419394.1.
DR AlphaFoldDB; M7WL99; -.
DR GeneID; 27369746; -.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_1_0_1; -.
DR OrthoDB; 3236018at2759; -.
DR Proteomes; UP000016926; 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; IPR034294; Aquaporin_transptr.
DR InterPro; IPR000425; MIP.
DR PANTHER; PTHR19139:SF199; AQUAPORIN; 1.
DR PANTHER; PTHR19139; AQUAPORIN TRANSPORTER; 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..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 416 AA; 43411 MW; A82779492D967853 CRC64;
MSGLPTAGAP TELPSQEHRR HRGPLNWHIR PASRGPLRLA VKNTFVAMVG DVANIPTTSV
TGATTAGQDG TAASAPNTSN LLYIALSFGF SLAVNAWIFF RVSGGLFNPA VSLGMAIAGA
LTPLRAIFLT ISQILGGIVG AAIIQALLPG TLNVATKLSP GTSVARGLFL EMFLTALLML
AILLLAAEKH KATFLAPIGI GLALFVAELV GVYYTGGSLN PARSFGPAVV LRSFDGYHWI
YWVGPFLGTL LAAGFYKFIK YLEYETVLGP EEPDTPSPSS SNNQNEKTDK AALGRNLVAP
SATLLGSTAA GASGSTRATP TAATTSMGEK EVHPADQKGT VAVQGPGLPD LLTTGPAGGV
FDLPQPPYDY RTRLERIESL LETLIAGAGA HGRKVSTEGT VVETGREWHK VNDSPV
//