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IQD18_ARATH
ID   IQD18_ARATH             Reviewed;         527 AA.
AC   Q9MAM4; B3H705; Q8LEL3;
DT   02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Protein IQ-DOMAIN 18 {ECO:0000303|PubMed:16368012};
DE            Short=AtIQD18 {ECO:0000303|PubMed:16368012};
GN   Name=IQD18 {ECO:0000303|PubMed:16368012};
GN   OrderedLocusNames=At1g01110 {ECO:0000312|Araport:AT1G01110};
GN   ORFNames=T25K16.10 {ECO:0000312|EMBL:AAF26462.1};
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] (ISOFORM 2).
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   INTERACTION WITH CALMODULIN, GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=16368012; DOI=10.1186/1471-2148-5-72;
RA   Abel S., Savchenko T., Levy M.;
RT   "Genome-wide comparative analysis of the IQD gene families in Arabidopsis
RT   thaliana and Oryza sativa.";
RL   BMC Evol. Biol. 5:72-72(2005).
RN   [5]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=28115582; DOI=10.1104/pp.16.01743;
RA   Buerstenbinder K., Moeller B., Ploetner R., Stamm G., Hause G., Mitra D.,
RA   Abel S.;
RT   "The IQD family of calmodulin-binding proteins links calcium signaling to
RT   microtubules, membrane subdomains, and the nucleus.";
RL   Plant Physiol. 173:1692-1708(2017).
RN   [6]
RP   REVIEW.
RX   PubMed=28534650; DOI=10.1080/15592324.2017.1331198;
RA   Buerstenbinder K., Mitra D., Quegwer J.;
RT   "Functions of IQD proteins as hubs in cellular calcium and auxin signaling:
RT   A toolbox for shape formation and tissue-specification in plants?";
RL   Plant Signal. Behav. 12:E1331198-E1331198(2017).
CC   -!- FUNCTION: May be involved in cooperative interactions with calmodulins
CC       or calmodulin-like proteins (By similarity). Recruits calmodulin
CC       proteins to microtubules, thus being a potential scaffold in cellular
CC       signaling and trafficking (By similarity). May associate with nucleic
CC       acids and regulate gene expression at the transcriptional or post-
CC       transcriptional level (By similarity). {ECO:0000250|UniProtKB:Q9SF32}.
CC   -!- SUBUNIT: Binds to multiple calmodulin (CaM) in the presence of Ca(2+)
CC       and CaM-like proteins. {ECO:0000250|UniProtKB:Q9SF32}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC       ECO:0000269|PubMed:28115582}. Nucleus, nuclear body
CC       {ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:28115582}. Cell membrane
CC       {ECO:0000269|PubMed:28115582}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9MAM4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9MAM4-2; Sequence=VSP_061104;
CC   -!- SIMILARITY: Belongs to the IQD family. {ECO:0000305}.
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DR   EMBL; AC007323; AAF26462.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27238.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27239.1; -; Genomic_DNA.
DR   EMBL; AY085363; AAM62593.1; -; mRNA.
DR   RefSeq; NP_001117204.1; NM_001123732.2. [Q9MAM4-1]
DR   RefSeq; NP_001318900.1; NM_001331250.1. [Q9MAM4-2]
DR   AlphaFoldDB; Q9MAM4; -.
DR   SMR; Q9MAM4; -.
DR   STRING; 3702.AT1G01110.2; -.
DR   PaxDb; Q9MAM4; -.
DR   PRIDE; Q9MAM4; -.
DR   ProteomicsDB; 187905; -.
DR   ProteomicsDB; 201841; -.
DR   EnsemblPlants; AT1G01110.1; AT1G01110.1; AT1G01110. [Q9MAM4-2]
DR   EnsemblPlants; AT1G01110.2; AT1G01110.2; AT1G01110. [Q9MAM4-1]
DR   GeneID; 839394; -.
DR   Gramene; AT1G01110.1; AT1G01110.1; AT1G01110. [Q9MAM4-2]
DR   Gramene; AT1G01110.2; AT1G01110.2; AT1G01110. [Q9MAM4-1]
DR   KEGG; ath:AT1G01110; -.
DR   Araport; AT1G01110; -.
DR   TAIR; locus:2200945; AT1G01110.
DR   eggNOG; ENOG502R300; Eukaryota.
DR   HOGENOM; CLU_024547_1_0_1; -.
DR   InParanoid; Q9MAM4; -.
DR   OMA; HFGLEQQ; -.
DR   OrthoDB; 736229at2759; -.
DR   PhylomeDB; Q9MAM4; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9MAM4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0016604; C:nuclear body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR025064; DUF4005.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF13178; DUF4005; 1.
DR   Pfam; PF00612; IQ; 2.
DR   SMART; SM00015; IQ; 2.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50096; IQ; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calmodulin-binding; Cell membrane; Cytoplasm;
KW   Cytoskeleton; Membrane; Nucleus; Reference proteome; Repeat.
FT   CHAIN           1..527
FT                   /note="Protein IQ-DOMAIN 18"
FT                   /id="PRO_0000453124"
FT   DOMAIN          120..148
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          149..171
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          1..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..161
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000303|PubMed:16368012"
FT   REGION          300..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..480
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           2..9
FT                   /note="Nuclear localization signal 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   MOTIF           22..29
FT                   /note="Nuclear localization signal 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        50..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..460
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..163
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_061104"
SQ   SEQUENCE   527 AA;  59172 MW;  058E9B7B2A2EAE04 CRC64;
     MGKKNGSSSW LTAVKRAFRS PTKKDHSNDV EEDEEKKREK RRWFRKPATQ ESPVKSSGIS
     PPAPQEDSLN VNSKPSPETA PSYATTTPPS NAGKPPSAVV PIATSASKTL APRRIYYARE
     NYAAVVIQTS FRGYLARRAL RALKGLVKLQ ALVRGHNVRK QAKMTLRCMQ ALVRVQSRVL
     DQRKRLSHDG SRKSAFSDSH AVFESRYLQD LSDRQSMSRE GSSAAEDWDD RPHTIDAVKV
     MLQRRRDTAL RHDKTNLSQA FSQKMWRTVG NQSTEGHHEV ELEEERPKWL DRWMATRPWD
     KRASSRASVD QRVSVKTVEI DTSQPYSRTG AGSPSRGQRP SSPSRTSHHY QSRNNFSATP
     SPAKSRPILI RSASPRCQRD PREDRDRAAY SYTSNTPSLR SNYSFTARSG CSISTTMVNN
     ASLLPNYMAS TESAKARIRS HSAPRQRPST PERDRAGLVK KRLSYPVPPP AEYEDNNSLR
     SPSFKSVAGS HFGGMLEQQS NYSSCCTESN GVEISPASTS DFRNWLR
 
 
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