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NIP61_ARATH
ID   NIP61_ARATH             Reviewed;         305 AA.
AC   Q9SAI4; Q5PP68;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Aquaporin NIP6-1;
DE   AltName: Full=NOD26-like intrinsic protein 6-1;
DE            Short=AtNIP6;1;
GN   Name=NIP6-1; OrderedLocusNames=At1g80760; ORFNames=F23A5.11;
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=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   [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   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2005) 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, AND MUTAGENESIS OF ALA-119 AND VAL-252.
RX   PubMed=16363796; DOI=10.1021/bi0511888;
RA   Wallace I.S., Roberts D.M.;
RT   "Distinct transport selectivity of two structural subclasses of the
RT   nodulin-like intrinsic protein family of plant aquaglyceroporin channels.";
RL   Biochemistry 44:16826-16834(2005).
CC   -!- FUNCTION: Transports glycerol, urea and formamide, in Xenopus laevis
CC       oocytes. Very low water transport activity.
CC       {ECO:0000269|PubMed:16363796}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots. {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/Val (NPA).
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family. NIP (TC
CC       1.A.8.12) subfamily. {ECO:0000305}.
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DR   EMBL; AC011713; AAF14664.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE36445.1; -; Genomic_DNA.
DR   EMBL; BT020229; AAV74223.1; -; mRNA.
DR   EMBL; BT021924; AAX49373.1; -; mRNA.
DR   PIR; B96840; B96840.
DR   RefSeq; NP_178191.1; NM_106724.3.
DR   AlphaFoldDB; Q9SAI4; -.
DR   SMR; Q9SAI4; -.
DR   BioGRID; 29633; 1.
DR   IntAct; Q9SAI4; 1.
DR   STRING; 3702.AT1G80760.1; -.
DR   TCDB; 1.A.8.12.9; the major intrinsic protein (mip) family.
DR   PaxDb; Q9SAI4; -.
DR   PRIDE; Q9SAI4; -.
DR   ProteomicsDB; 249436; -.
DR   EnsemblPlants; AT1G80760.1; AT1G80760.1; AT1G80760.
DR   GeneID; 844415; -.
DR   Gramene; AT1G80760.1; AT1G80760.1; AT1G80760.
DR   KEGG; ath:AT1G80760; -.
DR   Araport; AT1G80760; -.
DR   TAIR; locus:2025822; AT1G80760.
DR   eggNOG; KOG0223; Eukaryota.
DR   HOGENOM; CLU_020019_3_1_1; -.
DR   InParanoid; Q9SAI4; -.
DR   OMA; RRLIMYV; -.
DR   OrthoDB; 1246320at2759; -.
DR   PhylomeDB; Q9SAI4; -.
DR   PRO; PR:Q9SAI4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9SAI4; baseline and differential.
DR   Genevisible; Q9SAI4; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0046715; F:active borate transmembrane transporter activity; IDA:TAIR.
DR   GO; GO:0015267; F:channel activity; IEA:InterPro.
DR   GO; GO:0015168; F:glycerol transmembrane transporter activity; IDA:TAIR.
DR   GO; GO:0015204; F:urea transmembrane transporter activity; IDA:TAIR.
DR   GO; GO:0046713; P:borate transport; IMP:TAIR.
DR   GO; GO:0080029; P:cellular response to boron-containing substance levels; IEP: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; PTHR45724; PTHR45724; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; SSF81338; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..305
FT                   /note="Aquaporin NIP6-1"
FT                   /id="PRO_0000064069"
FT   TRANSMEM        82..102
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           139..141
FT                   /note="NPA 1"
FT   MOTIF           250..252
FT                   /note="NPA 2"
FT   MOD_RES         302
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P43286"
FT   MUTAGEN         119
FT                   /note="A->W: 6-fold increase in water transport activity,
FT                   but impaired in urea transport."
FT                   /evidence="ECO:0000269|PubMed:16363796"
FT   MUTAGEN         252
FT                   /note="V->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:16363796"
SQ   SEQUENCE   305 AA;  31845 MW;  C6D6622660E5CDC8 CRC64;
     MDHEEIPSTP STPATTPGTP GAPLFGGFEG KRNGHNGRYT PKSLLKSCKC FSVDNEWALE
     DGRLPPVTCS LPPPNVSLYR KLGAEFVGTL ILIFAGTATA IVNQKTDGAE TLIGCAASAG
     LAVMIVILST GHISGAHLNP AVTIAFAALK HFPWKHVPVY IGAQVMASVS AAFALKAVFE
     PTMSGGVTVP TVGLSQAFAL EFIISFNLMF VVTAVATDTR AVGELAGIAV GATVMLNILI
     AGPATSASMN PVRTLGPAIA ANNYRAIWVY LTAPILGALI GAGTYTIVKL PEEDEAPKER
     RSFRR
 
 
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