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Database: UniProt
Entry: A0A2T2P520_CORCC
LinkDB: A0A2T2P520_CORCC
Original site: A0A2T2P520_CORCC 
ID   A0A2T2P520_CORCC        Unreviewed;       628 AA.
AC   A0A2T2P520;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Aquaporin-like protein {ECO:0000313|EMBL:PSN72772.1};
GN   ORFNames=BS50DRAFT_168436 {ECO:0000313|EMBL:PSN72772.1};
OS   Corynespora cassiicola Philippines.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Corynesporascaceae; Corynespora.
OX   NCBI_TaxID=1448308 {ECO:0000313|EMBL:PSN72772.1, ECO:0000313|Proteomes:UP000240883};
RN   [1] {ECO:0000313|EMBL:PSN72772.1, ECO:0000313|Proteomes:UP000240883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philippines {ECO:0000313|EMBL:PSN72772.1,
RC   ECO:0000313|Proteomes:UP000240883};
RX   PubMed=29551995; DOI=10.3389/fmicb.2018.00276;
RA   Lopez D., Ribeiro S., Label P., Fumanal B., Venisse J.S., Kohler A.,
RA   de Oliveira R.R., Labutti K., Lipzen A., Lail K., Bauer D., Ohm R.A.,
RA   Barry K.W., Spatafora J., Grigoriev I.V., Martin F.M., Pujade-Renaud V.;
RT   "Genome-Wide Analysis of Corynespora cassiicola Leaf Fall Disease Putative
RT   Effectors.";
RL   Front. Microbiol. 9:276-276(2018).
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; KZ678129; PSN72772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T2P520; -.
DR   STRING; 1448308.A0A2T2P520; -.
DR   Proteomes; UP000240883; 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   PANTHER; PTHR43829; AQUAPORIN OR AQUAGLYCEROPORIN RELATED; 1.
DR   PANTHER; PTHR43829:SF24; MIP AQUAPORIN (EUROFUNG); 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   Reference proteome {ECO:0000313|Proteomes:UP000240883};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        356..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        391..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        431..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        486..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        516..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..264
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..113
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..171
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..198
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..233
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..331
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   628 AA;  69694 MW;  E1632E415581572F CRC64;
     MSTEGDYFGS RAEDYSGQPA RPNLRAVSGS GRPEGRQQTS YAGSAPLERY PTSHLEPIDD
     PRGAHSRTNT APTTISRFQT AHDDERVPDR DPTHAEDLNR QRIERKQEQK VPVDDEYYSL
     NPWYGQQPDK PLFGLSNPFP RTVRPGMRRP RRTLKESEFQ ATGQQASAAE REGIQTGDAA
     QVRQPQSRGT GVDRMSSNFD EDYLSNQHAR EGLENPSTFQ DVERSQQPPL PRTETGGHHQ
     PRRQASSGTN TVVPGRSHDH QIGDRGIDEH NLQIPESRPH PHTFGLQQGL PPLQEVQSHK
     SVDTAQTTGT QETMDKSYTQ TEKEEIQERE RQDRQDFYNT YRNPLARFRA KHPQALAEWL
     STFVYIFMGI TGSLSILTSN SENGGYATQC SAWGLAVMTA IYVGGGVSGA HLNPWISVSL
     WFYRGFPKRM CLTFIVAQML GGFCAGALAY LIYREAILNM DPGLDPNTTG KAFFTAPQPF
     VSPTTAFFND YVSMCIWIIV VFALGDDQNA PPGAGLNALI IGLFTYLLSI SMGYQTGLGV
     NPARDLGPRL VALWAGYGTE IFTTGWWAYG PIGAGLAGSL TGGFIYDAFV FVGGESPVNY
     RWPHPTEVKW FAKVKKDQAK DKLSDSLV
//
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