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Database: UniProt
Entry: A0A061H6D8_9BASI
LinkDB: A0A061H6D8_9BASI
Original site: A0A061H6D8_9BASI 
ID   A0A061H6D8_9BASI        Unreviewed;      1273 AA.
AC   A0A061H6D8;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Aquaporin {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PFL1_04693 {ECO:0000313|EMBL:EPQ27555.1};
OS   Pseudozyma flocculosa PF-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ27555.1, ECO:0000313|Proteomes:UP000053664};
RN   [1] {ECO:0000313|EMBL:EPQ27555.1, ECO:0000313|Proteomes:UP000053664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF-1 {ECO:0000313|EMBL:EPQ27555.1,
RC   ECO:0000313|Proteomes:UP000053664};
RX   PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA   Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA   Bakkeren G., Belanger R.R.;
RT   "The transition from a phytopathogenic smut ancestor to an anamorphic
RT   biocontrol agent deciphered by comparative whole-genome analysis.";
RL   Plant Cell 25:1946-1959(2013).
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}.
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DR   EMBL; KE361638; EPQ27555.1; -; Genomic_DNA.
DR   RefSeq; XP_007880413.1; XM_007882222.1.
DR   AlphaFoldDB; A0A061H6D8; -.
DR   GeneID; 19318794; -.
DR   KEGG; pfp:PFL1_04693; -.
DR   eggNOG; KOG0224; Eukaryota.
DR   HOGENOM; CLU_263749_0_0_1; -.
DR   OrthoDB; 5490746at2759; -.
DR   Proteomes; UP000053664; 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   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:UP000053664};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        856..875
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        937..957
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        989..1014
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1026..1044
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1136..1273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        93..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..382
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..430
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..478
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..568
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..600
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..634
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..743
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..766
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        780..804
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1189..1203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1273 AA;  135664 MW;  86D8922745BC33A4 CRC64;
     MHHPAPSFDA VRPRRDDSTS GNNDDENHDG LDGHASGSRP LSASSSHPVL AFDPTDFDTR
     IKLPSSSAAA PGHEAYAFSP PEPPTQRQPG PQPEQSDDEE TRSPQASRRT DEDEQLGQLI
     ALDFAEQSAP QHQPPPPPSL DTEQFPTEQD SAPLQTLPEG RRVSGFEAPP DAGDSTSAPR
     KQQQQQQQQP QEQPEQPEQP RYPQRATYFD TAQRSRSIAA LDQTSPRRSV QSPDEEPFGG
     GPAPPPASSA RHLSTGRSPD SYQEPAPYAG PGLVGRQLSE RRAPAAYAQP EDWTYAGPSN
     SASFHSSAPG TSDRHRTPQE LNAKYGSKYV PVTANEPVPE KPVWSLGSTL PRVRRAPKSV
     KTIDRQSRPR VGASQSSENA KRPFSWLGRG KTLEEARSVS KRSASGNEVG CSESEEGHNR
     SHDELRDSGR LPRGQALATL GSAARLTQDV RKGWHDEDRA AGSHGPLEPG KRPDDGAADL
     AEIDVDRSLM ALARHSRPSV PFDENDRREG QHGPPHGDDK AGRRLREARQ RLLQEADEIQ
     ARSAGDARKD ILTDEAVHQD EEGDPVPIKE GSTSRADHVQ RRQSQPGSAQ RRSGSHGQSG
     LGTRGAGGGG GAGNGGDNDS KLPENSSSMD QTRHPGLSGA RPPPRGRTAG GPAVGVGTRH
     ASNVSASAQH HEAPQLQRSA SSHMSARTRR SSHPTSLRRR GHPPASQAGR DLGGRADDQS
     TDPAQGDDQL RKSTSSSQPT TDDGRIGHIE ARQAAGPRKS DEEGGRRSGG GGGGGGEDTR
     TAWMQNSMGR QSASSDVTAT NSDSQYRLHD DDDDDDDDGA GRFQRRASET YDAVDDLQRI
     AFPNLWSKWR FYSREFLAEL VASVLLLVIG TGVNCQVRLS AAMNSTGGSY TSQNTAWGLA
     IMSSIYLSGG RSGAHVNPAI TLTLAVYRGF PWKQVPVYWS AQLLGAFIGA AITYSLYLPA
     LNEYEGGPDV RTLTGDHGSG ELFVTVPQIV TTVASGFGTE LVATTILTVM VLAVGDETNA
     PPGDGMTAVV LGLVLIMGNM ALGWSTGFAV SPSRDLGPRI LLACLGYGRE IWTHNSSWWL
     YGPQAGCFAG AILGGLIYDL TIFTGGESPI NYTREAWQDA TPSRLVRPLQ EAVARSQRQK
     AWRASGQGDD DGDDDGDDGS SFGRGQGNGT SDGRGRARFG GLFSKRVMGG RAAKEEADRL
     ANKVRDGGGG SSRASSAASS LSSGRGGGDP APQRQLDVRP GQGGNDWPTS QHSASMLELQ
     ERGGVDVGGG GRR
//
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