ID   TIPA_PHAVU              Reviewed;         256 AA.
AC   P23958;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Probable aquaporin TIP-type alpha;
DE   AltName: Full=Alpha TIP;
DE   AltName: Full=Tonoplast intrinsic protein alpha;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
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; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 11-21.
RC   STRAIN=cv. Greensleeves; TISSUE=Seed;
RX   PubMed=2152174; DOI=10.2307/3869114;
RA   Johnson K.D., Hoefte H.R., Chrispeels M.J.;
RT   "An intrinsic tonoplast protein of protein storage vacuoles in seeds is
RT   structurally related to a bacterial solute transporter (GlpF).";
RL   Plant Cell 2:525-532(1990).
RN   [2]
RP   PHOSPHORYLATION AT SER-7 BY CPK.
RX   PubMed=16653198; DOI=10.1104/pp.100.4.1787;
RA   Johnson K.D., Chrispeels M.J.;
RT   "Tonoplast-bound protein kinase phosphorylates tonoplast intrinsic
RT   protein.";
RL   Plant Physiol. 100:1787-1795(1992).
CC   -!- FUNCTION: Channel protein in tonoplast. These proteins may allow the
CC       diffusion of amino acids and/or peptides from the vacuolar compartment
CC       to the cytoplasm.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane; Multi-pass membrane protein.
CC       Note=Tonoplast.
CC   -!- TISSUE SPECIFICITY: Found in all seed tissues that are alive at seed
CC       maturity, but not in tissues that lose viability during seed
CC       maturation.
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   -!- PTM: Phosphorylated by a tonoplast-bound calcium-dependent protein
CC       kinase. {ECO:0000269|PubMed:16653198}.
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. TIP (TC
CC       1.A.8.10) subfamily. {ECO:0000305}.
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DR   EMBL; X62873; CAA44669.1; -; mRNA.
DR   PIR; JQ1106; JQ1106.
DR   PIR; S26742; S26742.
DR   AlphaFoldDB; P23958; -.
DR   SMR; P23958; -.
DR   STRING; 3885.XP_007152506.1; -.
DR   TCDB; 1.A.8.10.11; the major intrinsic protein (mip) family.
DR   iPTMnet; P23958; -.
DR   eggNOG; KOG0223; Eukaryota.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015267; F:channel activity; IEA:InterPro.
DR   GO; GO:0010431; P:seed maturation; TAS:AgBase.
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; PTHR45665; PTHR45665; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; Phosphoprotein; Repeat; Transmembrane;
KW   Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..256
FT                   /note="Probable aquaporin TIP-type alpha"
FT                   /id="PRO_0000064042"
FT   TOPO_DOM        1..24
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..57
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..102
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        122..143
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..169
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        190..216
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        240..256
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOTIF           85..87
FT                   /note="NPA 1"
FT   MOTIF           199..201
FT                   /note="NPA 2"
FT   MOD_RES         7
FT                   /note="Phosphoserine; by CPK"
FT                   /evidence="ECO:0000305|PubMed:16653198"
SQ   SEQUENCE   256 AA;  27196 MW;  7862A0AC8EB46810 CRC64;
     MATRRYSFGR TDEATHPDSM RASLAEFAST FIFVFAGEGS GLALVKIYQD SAFSAGELLA
     LALAHAFALF AAVSASMHVS GGHVNPAVSF GALIGGRISV IRAVYYWIAQ LLGSIVAALV
     LRLVTNNMRP SGFHVSPGVG VGHMFILEVV MTFGLMYTVY GTAIDPKRGA VSYIAPLAIG
     LIVGANILVG GPFDGACMNP ALAFGPSLVG WQWHQHWIFW VGPLLGAALA ALVYEYAVIP
     IEPPPHHHQP LATEDY