ID   PIP2_PEA                Reviewed;         289 AA.
AC   P25794; Q41006;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Probable aquaporin PIP-type 7a;
DE   AltName: Full=Turgor-responsive protein 31;
DE   AltName: Full=Turgor-responsive protein 7a;
GN   Name=TRG-31;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Progress No. 9;
RX   PubMed=1715781; DOI=10.1007/bf00017720;
RA   Guerrero F.D., Jones J.T., Mullet J.E.;
RT   "Turgor-responsive gene transcription and RNA levels increase rapidly when
RT   pea shoots are wilted. Sequence and expression of three inducible genes.";
RL   Plant Mol. Biol. 15:11-26(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8467086; DOI=10.1007/bf00027125;
RA   Guerrero F.D., Crossland L.;
RT   "Tissue-specific expression of a plant turgor-responsive gene with amino
RT   acid sequence homology to transport-facilitating proteins.";
RL   Plant Mol. Biol. 21:929-935(1993).
CC   -!- FUNCTION: Aquaporins facilitate the transport of water and small
CC       neutral solutes across cell membranes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- INDUCTION: By water stress, heat shock and to a small extent by
CC       abscisic acid (ABA). Induced within 30 min after the loss of leaf
CC       turgor.
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; X54357; CAA38241.1; -; mRNA.
DR   EMBL; Z18288; CAA79159.1; -; Genomic_DNA.
DR   PIR; S33617; S33617.
DR   AlphaFoldDB; P25794; -.
DR   SMR; P25794; -.
DR   TCDB; 1.A.8.11.1; the major intrinsic protein (mip) family.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   Cell membrane; Membrane; Repeat; Stress response; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..289
FT                   /note="Probable aquaporin PIP-type 7a"
FT                   /id="PRO_0000064060"
FT   TOPO_DOM        1..57
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..91
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..135
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..178
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        200..212
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        234..260
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        282..289
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           117..119
FT                   /note="NPA 1"
FT   MOTIF           239..241
FT                   /note="NPA 2"
SQ   SEQUENCE   289 AA;  31020 MW;  9E42AF92107761D0 CRC64;
     MEAKEQDVSL GANKFPERQP LGIAAQSQDE PKDYQEPPPA PLFEPSELTS WSFYRAGIAE
     FIATFLFLYI TVLTVMGVVR ESSKCKTVGI QGIAWAFGGM IFALVYCTAG ISGGHINPAV
     TFGLFLARKL SLTRAIFYMV MQVLGAICGA GVVKGFEGKQ RFGDLNGGAN FVAPGYTKGD
     GLGAEIVGTF ILVYTVFSAT DAKRSARDSH VPILAPLPIG FAVFLVHLAT IPITGTGINP
     ARSLGAAIVF NKKIGWNDHW IFWVGPFIGA ALAALYHQVV IRAIPFKSK