ID A0A183LMG0_9TREM Unreviewed; 292 AA.
AC A0A183LMG0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aquaporin {ECO:0008006|Google:ProtNLM};
GN ORFNames=SMRZ_LOCUS4985 {ECO:0000313|EMBL:VDO64013.1};
OS Schistosoma margrebowiei.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=48269 {ECO:0000313|WBParaSite:SMRZ_0000498601-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SMRZ_0000498601-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO64013.1, ECO:0000313|Proteomes:UP000277204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zambia {ECO:0000313|EMBL:VDO64013.1,
RC ECO:0000313|Proteomes:UP000277204};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Aquaglyceroporin that may modulate the water content and
CC osmolytes during anhydrobiosis (PubMed:23761966).
CC {ECO:0000256|ARBA:ARBA00037632}.
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; UZAI01001645; VDO64013.1; -; Genomic_DNA.
DR STRING; 48269.A0A183LMG0; -.
DR WBParaSite; SMRZ_0000498601-mRNA-1; SMRZ_0000498601-mRNA-1; SMRZ_0000498601.
DR Proteomes; UP000277204; 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 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:SF9; AQUAPORIN OR AQUAGLYCEROPORIN RELATED; 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:UP000277204};
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 28..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 105..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 292 AA; 33991 MW; DD785CD95E487B8B CRC64;
MYKLNLHDNY IYFLYKIKHK FSLIHNKHLL NICISEFIGT FILITIGLSS MLHNTLKYNL
YYMNISIGWS IALFLSQIIT QPLGYNSLMN PSITLSLALI NKLSFYYVIP LTMIQLISSF
LSSLLIYYIY YYNYISNHDN IKLIILNQFI ITPNGSHLIC FIDRLLLTIM TTIFILLIRD
ERNDKIQKNY RLIFIILFTS GRITSLSMNA GTSINPIRDL GPRITIALCG KNLFFSFFFN
LSNHYYFWIP IVAPYIGSII GAILYELLIG AYLNRKTVVA DNVWPTDPKY FV
//
