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CNG16_ARATH
ID   CNG16_ARATH             Reviewed;         705 AA.
AC   Q9SU64; Q1PEH4;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Probable cyclic nucleotide-gated ion channel 16;
DE   AltName: Full=Cyclic nucleotide- and calmodulin-regulated ion channel 16;
GN   Name=CNGC16; OrderedLocusNames=At3g48010; ORFNames=T17F15.120;
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] OF 86-705.
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [4]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=11500563; DOI=10.1104/pp.126.4.1646;
RA   Maeser P., Thomine S., Schroeder J.I., Ward J.M., Hirschi K., Sze H.,
RA   Talke I.N., Amtmann A., Maathuis F.J.M., Sanders D., Harper J.F.,
RA   Tchieu J., Gribskov M., Persans M.W., Salt D.E., Kim S.A., Guerinot M.L.;
RT   "Phylogenetic relationships within cation transporter families of
RT   Arabidopsis.";
RL   Plant Physiol. 126:1646-1667(2001).
CC   -!- FUNCTION: Putative cyclic nucleotide-gated ion channel.
CC   -!- SUBUNIT: Homotetramer or heterotetramer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: The binding of calmodulin to the C-terminus might interfere
CC       with cyclic nucleotide binding and thus channel activation.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide-gated cation channel (TC
CC       1.A.1.5) family. {ECO:0000305}.
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DR   EMBL; AL049658; CAB41138.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE78356.1; -; Genomic_DNA.
DR   EMBL; DQ446744; ABE65999.1; -; mRNA.
DR   PIR; T06682; T06682.
DR   RefSeq; NP_190384.1; NM_114670.2.
DR   AlphaFoldDB; Q9SU64; -.
DR   BioGRID; 9275; 1.
DR   STRING; 3702.AT3G48010.1; -.
DR   PaxDb; Q9SU64; -.
DR   PRIDE; Q9SU64; -.
DR   ProteomicsDB; 220290; -.
DR   EnsemblPlants; AT3G48010.1; AT3G48010.1; AT3G48010.
DR   GeneID; 823956; -.
DR   Gramene; AT3G48010.1; AT3G48010.1; AT3G48010.
DR   KEGG; ath:AT3G48010; -.
DR   Araport; AT3G48010; -.
DR   TAIR; locus:2097860; AT3G48010.
DR   eggNOG; KOG0498; Eukaryota.
DR   HOGENOM; CLU_013069_3_0_1; -.
DR   InParanoid; Q9SU64; -.
DR   OMA; MIWFVIP; -.
DR   OrthoDB; 281394at2759; -.
DR   PhylomeDB; Q9SU64; -.
DR   PRO; PR:Q9SU64; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SU64; baseline and differential.
DR   Genevisible; Q9SU64; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005216; F:ion channel activity; IEA:InterPro.
DR   CDD; cd00038; CAP_ED; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   2: Evidence at transcript level;
KW   Calmodulin-binding; cAMP; cAMP-binding; Cell membrane; cGMP; cGMP-binding;
KW   Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW   Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..705
FT                   /note="Probable cyclic nucleotide-gated ion channel 16"
FT                   /id="PRO_0000219344"
FT   TOPO_DOM        1..57
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical; Name=H1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..91
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical; Name=H2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..147
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical; Name=H3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..180
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        181..201
FT                   /note="Helical; Name=H4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..222
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        223..243
FT                   /note="Helical; Name=H5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        244..353
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..374
FT                   /note="Helical; Name=H6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        375..705
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          593..622
FT                   /note="IQ"
FT   REGION          573..588
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          636..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          672..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         457..580
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT   BINDING         528
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   705 AA;  81955 MW;  F5696626418AE93F CRC64;
     MSNLHLYTSA RFRNFPTTFS LRHHHNDPNN QRRRSIFSKL RDKTLDPGGD LITRWNHIFL
     ITCLLALFLD PLYFYLPIVQ AGTACMSIDV RFGIFVTCFR NLADLSFLIH ILLKFKTAFV
     SKSSRVFGRG ELVMDRREIA IRYLKSEFVI DLAATLPLPQ IMIWFVIPNA GEFRYAAHQN
     HTLSLIVLIQ YVPRFLVMLP LNRRIIKATG VAAKTAWSGA AYNLILYLLV SHVLGSVWYV
     LSIQRQHECW RRECIKEMNA THSPSCSLLF LDCGSLHDPG RQAWMRITRV LSNCDARNDD
     DQHFQFGMFG DAFTNDVTSS PFFDKYFYCL WWGLRNLSSY GQSLAASTLS SETIFSCFIC
     VAGLVFFSHL IGNVQNYLQS TTARLDEWRV RRRDTEEWMR HRQLPDELQE RVRRFVQYKW
     LTTRGVDEEA ILRALPLDLR RQIQRHLCLA LVRRVPFFAQ MDDQLLDAIC ERLVPSLNTK
     DTYVIREGDP VNEMLFIIRG QMESSTTDGG RSGFFNSITL RPGDFCGEEL LTWALVPNIN
     HNLPLSTRTV RTLSEVEAFA LRAEDLKFVA NQFRRLHSKK LQHAFRYYSH QWRAWGTCFI
     QAAWRRYMKR KLAMELARQE EEDDYFYDDD GDYQFEEDMP ESNNNNGDEN SSNNQNLSAT
     ILASKFAANT KRGVLGNQRG STRIDPDHPT LKMPKMFKPE DPGFF
 
 
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