SIP12_ARATH
ID SIP12_ARATH Reviewed; 243 AA.
AC Q9FK43;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable aquaporin SIP1-2;
DE AltName: Full=Small basic intrinsic protein 1-2;
DE Short=AtSIP1;2;
GN Name=SIP1-2; OrderedLocusNames=At5g18290; ORFNames=F20L16_10, MRG7.25;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
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 [6]
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 {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and above ground. Expressed in
CC elongating regions of the root tips, cotyledons, minor veins and
CC hydathode cells of the rosette leaves. Weakly expressed in vascular
CC tissues of the flower petals, filaments of stamens, upper part of the
CC styles and receptacles of the siliques. {ECO:0000269|PubMed:11806824,
CC 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/Cys (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; AB012246; BAB09487.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92534.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92535.1; -; Genomic_DNA.
DR EMBL; AK117849; BAC42490.1; -; mRNA.
DR EMBL; BT005263; AAO63327.1; -; mRNA.
DR RefSeq; NP_001190329.1; NM_001203400.1.
DR RefSeq; NP_197330.1; NM_121834.2.
DR AlphaFoldDB; Q9FK43; -.
DR SMR; Q9FK43; -.
DR BioGRID; 17223; 2.
DR IntAct; Q9FK43; 2.
DR STRING; 3702.AT5G18290.1; -.
DR PaxDb; Q9FK43; -.
DR PRIDE; Q9FK43; -.
DR ProteomicsDB; 234549; -.
DR EnsemblPlants; AT5G18290.1; AT5G18290.1; AT5G18290.
DR EnsemblPlants; AT5G18290.2; AT5G18290.2; AT5G18290.
DR GeneID; 831947; -.
DR Gramene; AT5G18290.1; AT5G18290.1; AT5G18290.
DR Gramene; AT5G18290.2; AT5G18290.2; AT5G18290.
DR KEGG; ath:AT5G18290; -.
DR Araport; AT5G18290; -.
DR TAIR; locus:2146268; AT5G18290.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_100006_0_0_1; -.
DR InParanoid; Q9FK43; -.
DR OMA; YKSHNTW; -.
DR OrthoDB; 1487748at2759; -.
DR PhylomeDB; Q9FK43; -.
DR PRO; PR:Q9FK43; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FK43; baseline and differential.
DR Genevisible; Q9FK43; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015250; F:water channel activity; IDA:TAIR.
DR Gene3D; 1.20.1080.10; -; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR044222; SIP1-1/2-like.
DR PANTHER; PTHR46739; PTHR46739; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SUPFAM; SSF81338; SSF81338; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Membrane; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..243
FT /note="Probable aquaporin SIP1-2"
FT /id="PRO_0000064074"
FT TRANSMEM 12..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT MOTIF 72..74
FT /note="NPA 1"
FT MOTIF 188..190
FT /note="NPA 2"
SQ SEQUENCE 243 AA; 26036 MW; 903096FD5D017B96 CRC64;
MSAVKSALGD MVITFLWVIL SATFGIQTAA IVSAVGFHGI TWAPLVISTL VVFVSISIFT
VIGNVLGGAS FNPCGNAAFY TAGVSSDSLF SLAIRSPAQA IGAAGGAITI MEMIPEKYKT
RIGGKPSLQF GAHNGAISEV VLSFSVTFLV LLIILRGPRK LLAKTFLLAL ATVSVFVVGS
KFTRPFMNPA IAFGWAYIYK SHNTWDHFYV YWISSYTGAI LSAMLFRIIF PAPPLVQKKQ
KKA
