ID A0A2G5TID5_9PELO Unreviewed; 289 AA.
AC A0A2G5TID5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=Aquaporin {ECO:0008006|Google:ProtNLM};
GN Name=Cni-aqp-6 {ECO:0000313|EMBL:PIC27017.1};
GN Synonyms=Cnig_chr_V.g19403 {ECO:0000313|EMBL:PIC27017.1};
GN ORFNames=B9Z55_019403 {ECO:0000313|EMBL:PIC27017.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC27017.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIC27017.1}.
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DR EMBL; PDUG01000005; PIC27017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5TID5; -.
DR STRING; 1611254.A0A2G5TID5; -.
DR Proteomes; UP000230233; Chromosome v.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR CDD; cd00333; MIP; 1.
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 InterPro; IPR022357; MIP_CS.
DR PANTHER; PTHR45665; AQUAPORIN-8; 1.
DR PANTHER; PTHR45665:SF9; AQUAPORIN-8; 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:UP000230233};
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 55..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..107
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 204..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 289 AA; 30972 MW; 3547D02FB5FCBDD3 CRC64;
MESCPVYLDP EKLPSPMVRS ASDVILNVDP FNQTTEKLKS GSDIVSKMIE DEKDYSIYSK
CAAEFIAVLL FVYIGSMQAA GGGDGVLHAA FAHGVAIFVL AATFGGVSGA HINPAVTFGI
ALCGRISPIH AVCYIASQLL GSVFGALLVR ISLHYKAYFA IGAGATLCGR GVGWQEGLTA
EIVTTYILVQ TVLLCAVDTD KNRLAPLAIG FSLIIEILAA GAISGASMNP ARSFGPNIMG
QFFLKPENLD SLYMFWNYHW IYYVGPVIGA FIAAGVYRLF FARDYRVLA
//