ID PIP1_ATRCA Reviewed; 282 AA.
AC P42767;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 13-SEP-2023, entry version 88.
DE RecName: Full=Aquaporin PIP-type;
OS Atriplex canescens (Fourwing saltbush) (Calligonum canescens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Atripliceae; Atriplex.
OX NCBI_TaxID=35922;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7543207; DOI=10.1104/pp.108.3.1291;
RA Cairney J., Newton R.J., Funkhouser E.A., Chang S., Hayes D.;
RT "Nucleotide sequence of a cDNA for a water channel protein (aquaporin)
RT homolog from Atriplex canescens (Pursh.) Nutt.";
RL Plant Physiol. 108:1291-1292(1995).
CC -!- FUNCTION: Water-specific channel.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- DOMAIN: Aquaporins contain two tandem repeats each containing three
CC membrane-spanning domains and a pore-forming loop with the signature
CC motif Asn-Pro-Ala (NPA).
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. PIP (TC
CC 1.A.8.11) subfamily. {ECO:0000305}.
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DR EMBL; U18403; AAA86991.1; -; mRNA.
DR AlphaFoldDB; P42767; -.
DR SMR; P42767; -.
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 NCBIfam; TIGR00861; MIP; 1.
DR PANTHER; PTHR45687; AQUAPORIN OR AQUAGLYCEROPORIN RELATED; 1.
DR PANTHER; PTHR45687:SF19; AQUAPORIN PIP2-7-RELATED; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; Aquaporin-like; 1.
DR PROSITE; PS00221; MIP; 1.
PE 2: Evidence at transcript level;
KW Membrane; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..282
FT /note="Aquaporin PIP-type"
FT /id="PRO_0000064061"
FT TRANSMEM 39..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..265
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT MOTIF 102..104
FT /note="NPA 1"
FT MOTIF 223..225
FT /note="NPA 2"
SQ SEQUENCE 282 AA; 30260 MW; 42AA96F0EB0F1444 CRC64;
MSKEVISEEG QVHQHGKDYV DPPPAPFFDM GELKLWSFWR AAIAEFIATL LFLYITVATV
IGYKKETDPC ASVGLLGIAW SFGGMIFVLV YCTAGISGGH INPAVTFGLF LARKVSLLRA
LVYMIAQCAG AICGVGLVKA FMKGPYNQFG GGANSVALGY NKGTAFGAEL IGTFVLVYTV
FSATDPKRSA RDSHVPILAP LPIGFAVFMV HLATIPITGT GINPARSFGA AVIYNKKRVW
DDHWIFWVGP FVGALAAAAY HQYVLRAAAI KALGSFRSNP TN
//
