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Aquaporin PIP1-1 (AtPIP1;1) (Plasma membrane aquaporin-1) (Plasma membrane intrinsic protein 1a) (PIP1a)

 PIP11_ARATH             Reviewed;         286 AA.
P61837; P43285; Q0WP60; Q8L9H0; Q9LDT6;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 1.
22-NOV-2017, entry version 124.
RecName: Full=Aquaporin PIP1-1;
Short=AtPIP1;1;
AltName: Full=Plasma membrane aquaporin-1;
AltName: Full=Plasma membrane intrinsic protein 1a;
Short=PIP1a;
Name=PIP1-1; Synonyms=PIP1A; OrderedLocusNames=At3g61430;
ORFNames=F2A19.30;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=cv. Landsberg erecta; TISSUE=Root;
PubMed=7920711; DOI=10.1046/j.1365-313X.1994.6020187.x;
Kammerloher W., Fischer U., Piechottka G.P., Schaeffner A.R.;
"Water channels in the plant plasma membrane cloned by immunoselection
from a mammalian expression system.";
Plant J. 6:187-199(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NOMENCLATURE, AND TISSUE SPECIFICITY.
PubMed=11806824;
Quigley F., Rosenberg J.M., Shachar-Hill Y., Bohnert H.J.;
"From genome to function: the Arabidopsis aquaporins.";
Genome Biol. 3:RESEARCH0001.1-RESEARCH0001.17(2002).
[8]
ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16839310; DOI=10.1042/BJ20060569;
Santoni V., Verdoucq L., Sommerer N., Vinh J., Pflieger D., Maurel C.;
"Methylation of aquaporins in plant plasma membrane.";
Biochem. J. 400:189-197(2006).
-!- FUNCTION: Water channel required to facilitate the transport of
water across cell membrane. Its function is impaired by Hg(2+).
{ECO:0000269|PubMed:7920711}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7920711};
Multi-pass membrane protein {ECO:0000269|PubMed:7920711}.
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in roots, above
ground and in flower buds. {ECO:0000269|PubMed:11806824,
ECO:0000269|PubMed:7920711}.
-!- DOMAIN: Aquaporins contain two tandem repeats each containing
three membrane-spanning domains and a pore-forming loop with the
signature motif Asn-Pro-Ala (NPA).
-!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. PIP
(TC 1.A.8.11) subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Liquid states - Issue
36 of July 2003;
URL="https://web.expasy.org/spotlight/back_issues/036";
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EMBL; X75881; CAA53475.1; -; mRNA.
EMBL; AL132962; CAB71073.1; -; Genomic_DNA.
EMBL; CP002686; AEE80201.1; -; Genomic_DNA.
EMBL; CP002686; AEE80202.1; -; Genomic_DNA.
EMBL; AY097398; AAM19914.1; -; mRNA.
EMBL; AY058113; AAL25530.1; -; mRNA.
EMBL; AK229222; BAF01089.1; -; mRNA.
EMBL; AY088439; AAM65975.1; -; mRNA.
PIR; T47935; T47935.
RefSeq; NP_001078323.1; NM_001084854.2.
RefSeq; NP_191702.1; NM_116008.4.
UniGene; At.23835; -.
ProteinModelPortal; P61837; -.
SMR; P61837; -.
BioGrid; 10630; 7.
IntAct; P61837; 5.
STRING; 3702.AT3G61430.1; -.
TCDB; 1.A.8.11.3; the major intrinsic protein (mip) family.
iPTMnet; P61837; -.
PaxDb; P61837; -.
PRIDE; P61837; -.
EnsemblPlants; AT3G61430.1; AT3G61430.1; AT3G61430.
EnsemblPlants; AT3G61430.2; AT3G61430.2; AT3G61430.
GeneID; 825316; -.
Gramene; AT3G61430.1; AT3G61430.1; AT3G61430.
Gramene; AT3G61430.2; AT3G61430.2; AT3G61430.
KEGG; ath:AT3G61430; -.
Araport; AT3G61430; -.
TAIR; locus:2082822; AT3G61430.
eggNOG; KOG0223; Eukaryota.
eggNOG; COG0580; LUCA.
HOGENOM; HOG000288286; -.
InParanoid; P61837; -.
KO; K09872; -.
OMA; EHETISH; -.
OrthoDB; EOG09360H22; -.
PhylomeDB; P61837; -.
PRO; PR:P61837; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; P61837; baseline and differential.
Genevisible; P61837; AT.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0015250; F:water channel activity; IDA:TAIR.
GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
GO; GO:0006833; P:water transport; IDA:TAIR.
CDD; cd00333; MIP; 1.
Gene3D; 1.20.1080.10; -; 1.
InterPro; IPR023271; Aquaporin-like.
InterPro; IPR034294; Aquaporin_transptr.
InterPro; IPR000425; MIP.
InterPro; IPR022357; MIP_CS.
PANTHER; PTHR19139; PTHR19139; 1.
Pfam; PF00230; MIP; 1.
PRINTS; PR00783; MINTRINSICP.
SUPFAM; SSF81338; SSF81338; 1.
TIGRFAMs; TIGR00861; MIP; 1.
PROSITE; PS00221; MIP; 1.
1: Evidence at protein level;
Acetylation; Cell membrane; Complete proteome; Membrane;
Phosphoprotein; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 286 Aquaporin PIP1-1.
/FTId=PRO_0000064045.
TOPO_DOM 1 54 Cytoplasmic. {ECO:0000255}.
TRANSMEM 55 75 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 76 91 Extracellular. {ECO:0000255}.
TRANSMEM 92 112 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 113 132 Cytoplasmic. {ECO:0000255}.
TRANSMEM 133 153 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 154 174 Extracellular. {ECO:0000255}.
TRANSMEM 175 195 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 196 208 Cytoplasmic. {ECO:0000255}.
TRANSMEM 209 229 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 230 256 Extracellular. {ECO:0000255}.
TRANSMEM 257 277 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 278 286 Cytoplasmic. {ECO:0000255}.
MOTIF 114 116 NPA 1.
MOTIF 235 237 NPA 2.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:16839310}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000250|UniProtKB:P43286}.
CONFLICT 15 15 F -> L (in Ref. 5; AAM65975).
{ECO:0000305}.
CONFLICT 231 231 G -> A (in Ref. 1; CAA53475).
{ECO:0000305}.
SEQUENCE 286 AA; 30689 MW; 5C0284F6BB5EA7B7 CRC64;
MEGKEEDVRV GANKFPERQP IGTSAQSDKD YKEPPPAPFF EPGELSSWSF WRAGIAEFIA
TFLFLYITVL TVMGVKRSPN MCASVGIQGI AWAFGGMIFA LVYCTAGISG GHINPAVTFG
LFLARKLSLT RALYYIVMQC LGAICGAGVV KGFQPKQYQA LGGGANTVAH GYTKGSGLGA
EIIGTFVLVY TVFSATDAKR NARDSHVPIL APLPIGFAVF LVHLATIPIT GTGINPARSL
GAAIIYNKDH SWDDHWVFWV GPFIGAALAA LYHVVVIRAI PFKSRS


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