ID   AQPA_PELLE              Reviewed;         272 AA.
AC   P50501;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Aquaporin FA-CHIP;
GN   Name=AQPA;
OS   Pelophylax lessonae (Pool frog) (Rana lessonae).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Pelophylax.
OX   NCBI_TaxID=45623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Urinary bladder urothelium;
RX   PubMed=7515688; DOI=10.1016/0005-2736(94)90155-4;
RA   Abrami L., Simon M., Rousselet G., Berthonaud V., Buhler J.M.;
RT   "Sequence and functional expression of an amphibian water channel, FA-CHIP:
RT   a new member of the MIP family.";
RL   Biochim. Biophys. Acta 1192:147-151(1994).
CC   -!- FUNCTION: Forms a 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.
CC       {ECO:0000305}.
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DR   EMBL; L24754; AAC38016.1; -; mRNA.
DR   PIR; I51164; I51164.
DR   AlphaFoldDB; P50501; -.
DR   SMR; P50501; -.
DR   PRIDE; P50501; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0015267; F:channel activity; IEA:InterPro.
DR   GO; GO:0015168; F:glycerol transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015793; P:glycerol transmembrane transport; IDA:UniProtKB.
DR   CDD; cd00333; MIP; 1.
DR   Gene3D; 1.20.1080.10; -; 1.
DR   InterPro; IPR023271; Aquaporin-like.
DR   InterPro; IPR023274; Aquaporin_1.
DR   InterPro; IPR034294; Aquaporin_transptr.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   PANTHER; PTHR19139; PTHR19139; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR02013; AQUAPORIN1.
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   Glycoprotein; Membrane; Repeat; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..272
FT                   /note="Aquaporin FA-CHIP"
FT                   /id="PRO_0000063973"
FT   TOPO_DOM        1..17
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        18..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..52
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        72..97
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..139
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..168
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        189..214
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        237..272
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOTIF           80..82
FT                   /note="NPA 1"
FT   MOTIF           196..198
FT                   /note="NPA 2"
FT   SITE            193
FT                   /note="Hg(2+)-sensitive residue"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        209
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   272 AA;  28881 MW;  9E79B4BD4E168BD2 CRC64;
     MASEFKKKAF WRAVIAEFLA MILFVFISIG AALGFNFPIE EKANQTVGRS QDIVKVSLAF
     GISIATMAQS VGHVSGAHLN PAVTLGCLLS CQISILKAVM YIIAQCLGAV VATAILSGIT
     SGLENNSLGL NGLSPGVSAG QGLGVEILVT FQLVLCVVAV TDRRRHDVSG SVPLAIGLSV
     ALGHLIAIDY TGCGMNPARS FGSAVLTKNF TYHWIFWVGP MIGGAAAAII YDFILAPRTS
     DLTDRMKVWT NGQVEEYELD GDDNTRVEMK PK