PIP13_ARATH
ID PIP13_ARATH Reviewed; 286 AA.
AC Q08733; Q8W4E5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 168.
DE RecName: Full=Aquaporin PIP1-3;
DE Short=AtPIP1;3;
DE AltName: Full=Plasma membrane intrinsic protein 1c;
DE Short=PIP1c;
DE AltName: Full=Transmembrane protein B;
DE Short=TMP-B;
GN Name=PIP1-3; Synonyms=PIP1C, TMPB; OrderedLocusNames=At1g01620;
GN ORFNames=F22L4.16;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Etiolated seedling;
RX PubMed=8108519; DOI=10.1104/pp.102.2.689;
RA Shagan T., Meraro D., Bar-Zvi D.;
RT "Nucleotide sequence of an Arabidopsis thaliana turgor-responsive TMP-B
RT cDNA clone encoding transmembrane protein with a major intrinsic protein
RT motif.";
RL Plant Physiol. 102:689-690(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Landsberg erecta; TISSUE=Root;
RX PubMed=7920711; DOI=10.1046/j.1365-313x.1994.6020187.x;
RA Kammerloher W., Fischer U., Piechottka G.P., Schaeffner A.R.;
RT "Water channels in the plant plasma membrane cloned by immunoselection from
RT a mammalian expression system.";
RL Plant J. 6:187-199(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NOMENCLATURE, AND TISSUE SPECIFICITY.
RX PubMed=11806824; DOI=10.1186/gb-2001-3-1-research0001;
RA Quigley F., Rosenberg J.M., Shachar-Hill Y., Bohnert H.J.;
RT "From genome to function: the Arabidopsis aquaporins.";
RL Genome Biol. 3:RESEARCH0001.1-RESEARCH0001.17(2002).
RN [7]
RP ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16839310; DOI=10.1042/bj20060569;
RA Santoni V., Verdoucq L., Sommerer N., Vinh J., Pflieger D., Maurel C.;
RT "Methylation of aquaporins in plant plasma membrane.";
RL Biochem. J. 400:189-197(2006).
CC -!- FUNCTION: Water channel required to facilitate the transport of water
CC across cell membrane. Its function is impaired by Hg(2+).
CC {ECO:0000269|PubMed:7920711}.
CC -!- INTERACTION:
CC Q08733; P30302: PIP2-3; NbExp=2; IntAct=EBI-4431134, EBI-4431139;
CC Q08733; Q9SV31: PIP2-5; NbExp=5; IntAct=EBI-4431134, EBI-4425112;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7920711};
CC Multi-pass membrane protein {ECO:0000269|PubMed:7920711}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q08733-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots, above ground, ripening fruit,
CC flower buds, green siliques and senescing leaves.
CC {ECO:0000269|PubMed:11806824, ECO:0000269|PubMed:7920711}.
CC -!- DOMAIN: The Asn-Pro-Ala (NPA) motifs may contribute to the formation of
CC two hemipores that could generate a narrow channel. {ECO:0000250}.
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; X69294; CAA49155.1; -; mRNA.
DR EMBL; X75882; CAA53476.1; -; mRNA.
DR EMBL; AC061957; AAF81320.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27312.1; -; Genomic_DNA.
DR EMBL; AF348574; AAK15545.1; -; mRNA.
DR EMBL; AY062610; AAL32688.1; -; mRNA.
DR EMBL; BT002101; AAN72112.1; -; mRNA.
DR PIR; A86147; A86147.
DR RefSeq; NP_171668.1; NM_100044.5. [Q08733-1]
DR AlphaFoldDB; Q08733; -.
DR SMR; Q08733; -.
DR BioGRID; 24471; 66.
DR IntAct; Q08733; 61.
DR STRING; 3702.AT1G01620.1; -.
DR iPTMnet; Q08733; -.
DR MetOSite; Q08733; -.
DR PaxDb; Q08733; -.
DR PRIDE; Q08733; -.
DR ProteomicsDB; 234668; -. [Q08733-1]
DR EnsemblPlants; AT1G01620.1; AT1G01620.1; AT1G01620. [Q08733-1]
DR GeneID; 839235; -.
DR Gramene; AT1G01620.1; AT1G01620.1; AT1G01620. [Q08733-1]
DR KEGG; ath:AT1G01620; -.
DR Araport; AT1G01620; -.
DR TAIR; locus:2025391; AT1G01620.
DR eggNOG; KOG0223; Eukaryota.
DR InParanoid; Q08733; -.
DR OMA; PHELISW; -.
DR PhylomeDB; Q08733; -.
DR PRO; PR:Q08733; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q08733; baseline and differential.
DR Genevisible; Q08733; AT.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0015250; F:water channel activity; IDA:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR GO; GO:0006833; P:water transport; IDA:TAIR.
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 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..286
FT /note="Aquaporin PIP1-3"
FT /id="PRO_0000064048"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..81
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 103..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..208
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..256
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 114..116
FT /note="NPA 1"
FT MOTIF 235..237
FT /note="NPA 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:16839310"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
FT CONFLICT 141
FT /note="L -> F (in Ref. 2; CAA53476)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="V -> I (in Ref. 2; CAA53476)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="T -> S (in Ref. 2; CAA53476)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="I -> F (in Ref. 5; AAN72112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 30633 MW; 4E2F8444232030B2 CRC64;
MEGKEEDVRV GANKFPERQP IGTSAQTDKD YKEPPPAPFF EPGELSSWSF YRAGIAEFIA
TFLFLYITVL TVMGVKRAPN MCASVGIQGI AWAFGGMIFA LVYCTAGISG GHINPAVTFG
LFLARKLSLT RAVFYIVMQC LGAICGAGVV KGFQPNPYQT LGGGANTVAH GYTKGSGLGA
EIIGTFVLVY TVFSATDAKR SARDSHVPIL APLPIGFAVF LVHLATIPIT GTGINPARSL
GAAIIYNKDH AWDDHWIFWV GPFIGAALAA LYHQLVIRAI PFKSRS
