ID SIP11_ARATH Reviewed; 240 AA.
AC Q9M8W5; Q0WWC3;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 140.
DE RecName: Full=Aquaporin SIP1-1;
DE AltName: Full=Small basic intrinsic protein 1-1;
DE Short=AtSIP1;1;
GN Name=SIP1-1; OrderedLocusNames=At3g04090; ORFNames=T6K12.29;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16223486; DOI=10.1016/j.febslet.2005.09.076;
RA Ishikawa F., Suga S., Uemura T., Sato M.H., Maeshima M.;
RT "Novel type aquaporin SIPs are mainly localized to the ER membrane and show
RT cell-specific expression in Arabidopsis thaliana.";
RL FEBS Lett. 579:5814-5820(2005).
CC -!- FUNCTION: Water channel required to facilitate the transport of water
CC across cell membrane. {ECO:0000269|PubMed:16223486}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16223486}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16223486}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and above ground. Expressed in
CC elongating regions of the root tips, trichome cells of the rosette
CC leaves, vascular tissues of the flower petals, stigma, stamens (anthers
CC and filaments), pollen and the top and bottom (receptacle) of siliques.
CC {ECO:0000269|PubMed:11806824, ECO:0000269|PubMed:16223486}.
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/Thr (NPA).
CC -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. SIP (TC
CC 1.A.8.10) subfamily. {ECO:0000305}.
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DR EMBL; AC016829; AAF26804.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74036.1; -; Genomic_DNA.
DR EMBL; AK226432; BAE98575.1; -; mRNA.
DR RefSeq; NP_187059.1; NM_111280.5.
DR AlphaFoldDB; Q9M8W5; -.
DR SMR; Q9M8W5; -.
DR STRING; 3702.Q9M8W5; -.
DR TCDB; 1.A.8.10.5; the major intrinsic protein (mip) family.
DR PaxDb; 3702-AT3G04090-1; -.
DR ProteomicsDB; 234463; -.
DR EnsemblPlants; AT3G04090.1; AT3G04090.1; AT3G04090.
DR GeneID; 819564; -.
DR Gramene; AT3G04090.1; AT3G04090.1; AT3G04090.
DR KEGG; ath:AT3G04090; -.
DR Araport; AT3G04090; -.
DR TAIR; AT3G04090; SIP1A.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_100006_0_0_1; -.
DR InParanoid; Q9M8W5; -.
DR OMA; LMPASYK; -.
DR OrthoDB; 315019at2759; -.
DR PhylomeDB; Q9M8W5; -.
DR PRO; PR:Q9M8W5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M8W5; baseline and differential.
DR Genevisible; Q9M8W5; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015250; F:water channel activity; IDA:TAIR.
DR Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR044222; SIP1-1/2-like.
DR PANTHER; PTHR46739; AQUAPORIN SIP1-1; 1.
DR PANTHER; PTHR46739:SF3; AQUAPORIN SIP1-1; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; Aquaporin-like; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..240
FT /note="Aquaporin SIP1-1"
FT /id="PRO_0000064073"
FT TRANSMEM 13..33
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT MOTIF 70..72
FT /note="NPA 1"
FT MOTIF 185..187
FT /note="NPA 2"
SQ SEQUENCE 240 AA; 25706 MW; CC0D694AB1DC163A CRC64;
MMGVLKSAIG DMLMTFSWVV LSATFGIQTA AIISAGDFQA ITWAPLVILT SLIFVYVSIF
TVIFGSASFN PTGSAAFYVA GVPGDTLFSL AIRLPAQAIG AAGGALAIME FIPEKYKHMI
GGPSLQVDVH TGAIAETILS FGITFAVLLI ILRGPRRLLA KTFLLALATI SFVVAGSKYT
GPAMNPAIAF GWAYMYSSHN TWDHIYVYWI SSFVGALSAA LLFRSIFPPP RPQKKKQKKA
//
