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CI111_ARATH
ID   CI111_ARATH             Reviewed;        1022 AA.
AC   Q9LET7; Q9LD58;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Calmodulin-interacting protein 111;
DE            Short=CaM-interacting protein 111;
DE   AltName: Full=ATPase family AAA domain-containing protein CIP111;
GN   Name=CIP111; OrderedLocusNames=At3g56690; ORFNames=T8M16_200;
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 [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP   INTERACTION WITH CAM2.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=11346951; DOI=10.1007/s004250000440;
RA   Buaboocha T., Liao B., Zielinski R.E.;
RT   "Isolation of cDNA and genomic DNA clones encoding a calmodulin-binding
RT   protein related to a family of ATPases involved in cell division and
RT   vesicle fusion.";
RL   Planta 212:774-781(2001).
RN   [2]
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   [3]
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).
CC   -!- SUBUNIT: Interacts with CAM2. {ECO:0000269|PubMed:11346951}.
CC   -!- INTERACTION:
CC       Q9LET7; P25069: CAM5; NbExp=2; IntAct=EBI-2112024, EBI-1397259;
CC   -!- TISSUE SPECIFICITY: Expressed in the whole plant.
CC       {ECO:0000269|PubMed:11346951}.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR   EMBL; AF217546; AAF28347.1; -; mRNA.
DR   EMBL; AF217547; AAF28348.1; -; Genomic_DNA.
DR   EMBL; AL390921; CAC00732.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79552.1; -; Genomic_DNA.
DR   PIR; T50927; T50928.
DR   PIR; T51257; T51257.
DR   RefSeq; NP_191228.1; NM_115528.3.
DR   AlphaFoldDB; Q9LET7; -.
DR   SMR; Q9LET7; -.
DR   BioGRID; 10152; 1.
DR   IntAct; Q9LET7; 2.
DR   STRING; 3702.AT3G56690.1; -.
DR   iPTMnet; Q9LET7; -.
DR   SwissPalm; Q9LET7; -.
DR   PaxDb; Q9LET7; -.
DR   PRIDE; Q9LET7; -.
DR   ProteomicsDB; 246922; -.
DR   EnsemblPlants; AT3G56690.1; AT3G56690.1; AT3G56690.
DR   GeneID; 824836; -.
DR   Gramene; AT3G56690.1; AT3G56690.1; AT3G56690.
DR   KEGG; ath:AT3G56690; -.
DR   Araport; AT3G56690; -.
DR   TAIR; locus:2103555; AT3G56690.
DR   eggNOG; KOG0733; Eukaryota.
DR   HOGENOM; CLU_000688_4_0_1; -.
DR   InParanoid; Q9LET7; -.
DR   OMA; SWLYSRS; -.
DR   OrthoDB; 194195at2759; -.
DR   PhylomeDB; Q9LET7; -.
DR   PRO; PR:Q9LET7; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LET7; baseline and differential.
DR   Genevisible; Q9LET7; AT.
DR   GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; ISS:TAIR.
DR   GO; GO:0005516; F:calmodulin binding; IDA:TAIR.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calmodulin-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..1022
FT                   /note="Calmodulin-interacting protein 111"
FT                   /id="PRO_0000415736"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1005..1022
FT                   /note="Calmodulin-binding"
FT   COMPBIAS        1..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         425..432
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         765..772
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        412
FT                   /note="S -> G (in Ref. 1; AAF28348/AAF28347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        480
FT                   /note="V -> A (in Ref. 1; AAF28348/AAF28347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        551
FT                   /note="V -> A (in Ref. 1; AAF28348/AAF28347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        563
FT                   /note="I -> V (in Ref. 1; AAF28348/AAF28347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        566
FT                   /note="R -> C (in Ref. 1; AAF28348/AAF28347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        612
FT                   /note="S -> Y (in Ref. 1; AAF28348/AAF28347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        630
FT                   /note="N -> S (in Ref. 1; AAF28348/AAF28347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        672
FT                   /note="I -> N (in Ref. 1; AAF28348/AAF28347)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1010
FT                   /note="R -> K (in Ref. 1; AAF28348/AAF28347)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1022 AA;  111519 MW;  F53B67B928686BF6 CRC64;
     MPSKKKQSRT PSRLSNSEPP ASPRTPASST TSRDTDSINE EELRRSIEEA SAAFPCLLGK
     SAIIARVADV ASESIRGSKI WLSETSMVAA SLSPGSTVSV SLASPESRFS RSFPLSSIKA
     EYGDDSESII ADEPGNYFVL TTVFSSSKVF KDAVRISLNL CYGLGCPVSG RTVFVYPVSG
     PSLSDQFNGN GRSRYDDVNH LSLLACKELC LELTPFRNML QAKNAFESSY EQNGNGNSTP
     KTPANLQKFS SPRPKSPVSP IIEDSVFSCK QRFSSESSID LREVLSNESS KKLLQICASS
     WLYPCSLLYG NFVSVPILSE ICIFCVKRAD KRPSDTSNRN HAFMINQETK VYLHHTLDLA
     SEIQGRTFVQ GLQFDEGENV GCEISKLGGL SKEYAILRDI IDSSSIKNSL SSLGLRPTKG
     VLIHGPPGTG KTSLARTFAR HSGVNFFSVN GPEIISQYLG ESEKALDEVF RSASNATPAV
     VFIDDLDAIA PARKEGGEEL SQRMVATLLN LMDGISRTDG VVVIAATNRP DSIEPALRRP
     GRLDREIEIG VPSSTQRSDI LHIILRGMRH SLSNIQVEQL AMATHGFVGA DLSALCCEAA
     FVCLRRHLDQ SSSSSNLPLE EAPIAESSSN MSDISSDSSD SASSCITISA TTSGAQRSFS
     LDETVSLVAD DIQNNGNSCS EQMLRKQGEH TLSVGFEDFE NAKTKIRPSA MREVILEVPK
     VNWEDVGGQN EVKNQLMEAV EWPQKHQDAF KRIGTRPPSG ILMFGPPGCS KTLMARAVAS
     EAKLNFLAVK GPELFSKWVG ESEKAVRSLF AKARANAPSI IFFDEIDSLA SIRGKENDGV
     SVSDRVMSQL LVELDGLHQR VGVTVIAATN RPDKIDSALL RPGRFDRLLY VGPPNETDRE
     AILKIHLRKI PCSSDICLKE LASITKGYTG ADISLICREA AIAALEESLE MEEISMRHLK
     AAISQIEPTE ILSYKALSEK FQRLVHTDPQ REEEVTQPGN KSRSLWTPLR SVAMFLRRHI
     AS
 
 
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