PIP14_ARATH
ID PIP14_ARATH Reviewed; 287 AA.
AC Q39196; O23059; O23829;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 163.
DE RecName: Full=Probable aquaporin PIP1-4;
DE AltName: Full=Plasma membrane intrinsic protein 1-4;
DE Short=AtPIP1;4;
DE AltName: Full=Transmembrane protein C;
DE Short=TMP-C;
GN Name=PIP1.4; Synonyms=TMPC; OrderedLocusNames=At4g00430;
GN ORFNames=A_IG005I10.2, F5I10.2;
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=Flower bud;
RX PubMed=7972502; DOI=10.1104/pp.105.4.1441;
RA Kinoshita T., Hara-Nishimura I., Shiraishi H., Okada K., Shimura Y.,
RA Nishimura M.;
RT "Nucleotide sequence of a transmembrane protein (TMP-C) cDNA in Arabidopsis
RT thaliana.";
RL Plant Physiol. 105:1441-1442(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Flower bud;
RX PubMed=8980528; DOI=10.1007/bf00020217;
RA Utsugi S., Sakamoto W., Ogura Y., Murata M., Motoyoshi F.;
RT "Isolation and characterization of cDNA clones corresponding to the genes
RT expressed preferentially in floral organs of Arabidopsis thaliana.";
RL Plant Mol. Biol. 32:759-765(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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: Aquaporins facilitate the transport of water and small
CC neutral solutes across cell membranes. {ECO:0000250}.
CC -!- INTERACTION:
CC Q39196; Q9SV31: PIP2-5; NbExp=4; IntAct=EBI-4427223, EBI-4425112;
CC Q39196; P93004: PIP2-7; NbExp=3; IntAct=EBI-4427223, EBI-4434233;
CC Q39196; Q9ZVX8: PIP2-8; NbExp=5; IntAct=EBI-4427223, EBI-4425116;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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=Q39196-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots and green
CC siliques. Also expressed above ground and in flower buds.
CC {ECO:0000269|PubMed:11806824}.
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 -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. PIP (TC
CC 1.A.8.11) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB62824.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF02782.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80801.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D26609; BAA05654.1; -; mRNA.
DR EMBL; D85192; BAA22097.1; -; mRNA.
DR EMBL; AF013293; AAB62824.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF195115; AAF02782.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161471; CAB80801.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE81879.1; -; Genomic_DNA.
DR EMBL; AY099825; AAM20676.1; -; mRNA.
DR EMBL; AY120785; AAM53343.1; -; mRNA.
DR EMBL; BT000330; AAN15649.1; -; mRNA.
DR EMBL; BT006313; AAP13421.1; -; mRNA.
DR PIR; T01528; T01528.
DR RefSeq; NP_567178.1; NM_116268.4. [Q39196-1]
DR AlphaFoldDB; Q39196; -.
DR SMR; Q39196; -.
DR BioGRID; 13247; 16.
DR IntAct; Q39196; 11.
DR STRING; 3702.AT4G00430.1; -.
DR iPTMnet; Q39196; -.
DR SwissPalm; Q39196; -.
DR PaxDb; Q39196; -.
DR PRIDE; Q39196; -.
DR ProteomicsDB; 234959; -. [Q39196-1]
DR EnsemblPlants; AT4G00430.1; AT4G00430.1; AT4G00430. [Q39196-1]
DR GeneID; 827956; -.
DR Gramene; AT4G00430.1; AT4G00430.1; AT4G00430. [Q39196-1]
DR KEGG; ath:AT4G00430; -.
DR Araport; AT4G00430; -.
DR TAIR; locus:2126026; AT4G00430.
DR eggNOG; KOG0223; Eukaryota.
DR HOGENOM; CLU_020019_3_0_1; -.
DR InParanoid; Q39196; -.
DR OMA; KKEVCSA; -.
DR PhylomeDB; Q39196; -.
DR PRO; PR:Q39196; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q39196; baseline and differential.
DR Genevisible; Q39196; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0015250; F:water channel activity; ISS:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR GO; GO:0006833; P:water transport; IMP: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..287
FT /note="Probable aquaporin PIP1-4"
FT /id="PRO_0000064049"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 77..92
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 115..117
FT /note="NPA 1"
FT MOTIF 236..238
FT /note="NPA 2"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:16839310"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43286"
FT CONFLICT 25
FT /note="A -> V (in Ref. 2; BAA22097)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="P -> S (in Ref. 2; BAA22097)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="V -> G (in Ref. 2; BAA22097)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="A -> D (in Ref. 2; BAA22097)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="A -> V (in Ref. 2; BAA22097)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 287 AA; 30693 MW; 8CE76043F389B3B8 CRC64;
MEGKEEDVRV GANKFPERQP IGTSAQSTDK DYKEPPPAPL FEPGELSSWS FYRAGIAEFI
ATFLFLYITV LTVMGVKRAP NMCASVGIQG IAWAFGGMIF ALVYCTAGIS GGHINPAVTF
GLFLARKLSL TRAVFYMIMQ CLGAICGAGV VKGFQPTPYQ TLGGGANTVA HGYTKGSGLG
AEIIGTFVLV YTVFSATDAK RSARDSHVPI LAPLPIGFAV FLVHLATIPI TGTGINPARS
LGAAIIYNKD HSWDDHWIFW VGPFIGAALA ALYHQIVIRA IPFKSKS
