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   25-MAY-2022, entry version 85.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U18403; AAA86991.1; -; mRNA.
DR   AlphaFoldDB; P42767; -.
DR   SMR; P42767; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015267; F:channel activity; IEA:InterPro.
DR   CDD; cd00333; MIP; 1.
DR   Gene3D; 1.20.1080.10; -; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR034294; Aquaporin_transptr.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   PANTHER; PTHR45687; PTHR45687; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; SSF81338; 1.
DR   TIGRFAMs; TIGR00861; MIP; 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