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CALM1_XENLA
ID   CALM1_XENLA             Reviewed;         149 AA.
AC   P0DP33; P02593; P0DP40; P62155; P70667; P99014; Q61379; Q61380; Q6INP3;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Calmodulin-1 {ECO:0000250|UniProtKB:P0DP23};
GN   Name=calm1 {ECO:0000250|UniProtKB:P0DP23};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Kidney;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   STRUCTURE BY NMR.
RX   PubMed=7552748; DOI=10.1038/nsb0995-768;
RA   Kuboniwa H., Tjandra N., Grzesiek S., Ren H., Klee C.B., Bax A.;
RT   "Solution structure of calcium-free calmodulin.";
RL   Nat. Struct. Biol. 2:768-776(1995).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=7552747; DOI=10.1038/nsb0995-758;
RA   Zhang M., Tanaka T., Ikura M.;
RT   "Calcium-induced conformational transition revealed by the solution
RT   structure of apo calmodulin.";
RL   Nat. Struct. Biol. 2:758-767(1995).
RN   [4]
RP   STRUCTURE BY NMR.
RX   PubMed=9514729; DOI=10.1006/jmbi.1997.1524;
RA   Osawa M., Swindells M.B., Tanikawa J., Tanaka T., Mase T., Furuya T.,
RA   Ikura M.;
RT   "Solution structure of calmodulin-W-7 complex: the basis of diversity in
RT   molecular recognition.";
RL   J. Mol. Biol. 276:165-176(1998).
RN   [5]
RP   STRUCTURE BY NMR.
RX   PubMed=10493800; DOI=10.1021/bi9908235;
RA   Elshorst B., Hennig M., Foersterling H., Diener A., Maurer M., Schulte P.,
RA   Schwalbe H., Griesinger C., Krebs J., Schmid H., Vorherr T.E., Carafoli E.;
RT   "NMR solution structure of a complex of calmodulin with a binding peptide
RT   of the Ca(2+) pump.";
RL   Biochemistry 38:12320-12332(1999).
RN   [6]
RP   STRUCTURE BY NMR.
RX   PubMed=10467092; DOI=10.1038/12271;
RA   Osawa M., Tokumitsu H., Swindells M.B., Kurihara H., Orita M.,
RA   Shibanuma T., Furuya T., Ikura M.;
RT   "A novel target recognition revealed by calmodulin in complex with Ca2+-
RT   calmodulin-dependent kinase kinase.";
RL   Nat. Struct. Biol. 6:819-824(1999).
RN   [7]
RP   STRUCTURE BY NMR OF 1-77 AND 83-149.
RX   PubMed=11142512; DOI=10.1023/a:1026563923774;
RA   Chou J.J., Li S., Bax A.;
RT   "Study of conformational rearrangement and refinement of structural
RT   homology models by the use of heteronuclear dipolar couplings.";
RL   J. Biomol. NMR 18:217-227(2000).
RN   [8]
RP   STRUCTURE BY NMR.
RX   PubMed=12684008; DOI=10.1016/s0022-2836(03)00271-7;
RA   Yap K.L., Yuan T., Mal T.K., Vogel H.J., Ikura M.;
RT   "Structural basis for simultaneous binding of two carboxy-terminal peptides
RT   of plant glutamate decarboxylase to calmodulin.";
RL   J. Mol. Biol. 328:193-204(2003).
RN   [9]
RP   STRUCTURE BY NMR OF 79-149.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of magnesium-bound form of calmodulin C-domain
RT   E104D/E140D Mutant.";
RL   Submitted (APR-2008) to the PDB data bank.
CC   -!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
CC       ion channels and other proteins by Ca(2+). Among the enzymes to be
CC       stimulated by the calmodulin-Ca(2+) complex are a number of protein
CC       kinases and phosphatases.
CC   -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC   -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR   EMBL; BC094079; AAH94079.1; -; mRNA.
DR   PIR; I51402; I51402.
DR   RefSeq; NP_001080864.1; NM_001087395.1.
DR   RefSeq; NP_001084025.1; NM_001090556.1.
DR   RefSeq; NP_001089059.1; NM_001095590.1.
DR   RefSeq; XP_018085904.1; XM_018230415.1.
DR   PDB; 1CFC; NMR; -; A=2-149.
DR   PDB; 1CFD; NMR; -; A=2-149.
DR   PDB; 1CFF; NMR; -; A=2-149.
DR   PDB; 1CKK; NMR; -; A=2-149.
DR   PDB; 1DMO; NMR; -; A=2-149.
DR   PDB; 1F70; NMR; -; A=2-77.
DR   PDB; 1F71; NMR; -; A=83-149.
DR   PDB; 1IQ5; X-ray; 1.80 A; A=1-149.
DR   PDB; 1MUX; NMR; -; A=2-149.
DR   PDB; 1NWD; NMR; -; A=2-149.
DR   PDB; 1SY9; NMR; -; A=2-149.
DR   PDB; 1X02; NMR; -; A=2-149.
DR   PDB; 1Y0V; X-ray; 3.60 A; H/I/J/K/L/M=6-149.
DR   PDB; 2COL; X-ray; 2.20 A; B=80-146.
DR   PDB; 2K3S; NMR; -; B=83-149.
DR   PDB; 2KDU; NMR; -; A=2-149.
DR   PDB; 2LLO; NMR; -; A=2-81.
DR   PDB; 2LLQ; NMR; -; A=83-149.
DR   PDB; 2MES; NMR; -; A=2-149.
DR   PDB; 2RRT; NMR; -; A=79-149.
DR   PDB; 4R8G; X-ray; 3.50 A; A/B/H=2-149.
DR   PDB; 5J7J; NMR; -; A=2-149.
DR   PDB; 5T0X; NMR; -; A=2-149.
DR   PDB; 6CTB; NMR; -; A=3-149.
DR   PDBsum; 1CFC; -.
DR   PDBsum; 1CFD; -.
DR   PDBsum; 1CFF; -.
DR   PDBsum; 1CKK; -.
DR   PDBsum; 1DMO; -.
DR   PDBsum; 1F70; -.
DR   PDBsum; 1F71; -.
DR   PDBsum; 1IQ5; -.
DR   PDBsum; 1MUX; -.
DR   PDBsum; 1NWD; -.
DR   PDBsum; 1SY9; -.
DR   PDBsum; 1X02; -.
DR   PDBsum; 1Y0V; -.
DR   PDBsum; 2COL; -.
DR   PDBsum; 2K3S; -.
DR   PDBsum; 2KDU; -.
DR   PDBsum; 2LLO; -.
DR   PDBsum; 2LLQ; -.
DR   PDBsum; 2MES; -.
DR   PDBsum; 2RRT; -.
DR   PDBsum; 4R8G; -.
DR   PDBsum; 5J7J; -.
DR   PDBsum; 5T0X; -.
DR   PDBsum; 6CTB; -.
DR   AlphaFoldDB; P0DP33; -.
DR   SASBDB; P0DP33; -.
DR   SMR; P0DP33; -.
DR   DNASU; 108698710; -.
DR   DNASU; 380558; -.
DR   DNASU; 399259; -.
DR   DNASU; 606721; -.
DR   GeneID; 108698710; -.
DR   GeneID; 380558; -.
DR   GeneID; 399259; -.
DR   GeneID; 606721; -.
DR   KEGG; xla:108698710; -.
DR   KEGG; xla:380558; -.
DR   KEGG; xla:399259; -.
DR   KEGG; xla:606721; -.
DR   CTD; 380558; -.
DR   CTD; 399259; -.
DR   CTD; 606721; -.
DR   Xenbase; XB-GENE-976648; calm1.S.
DR   Xenbase; XB-GENE-17331898; calm2.L.
DR   Xenbase; XB-GENE-1014645; calm2.S.
DR   OMA; HPEATHA; -.
DR   OrthoDB; 1386217at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 108698710; Expressed in brain and 19 other tissues.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:BHF-UCL.
DR   CDD; cd00051; EFh; 2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   Pfam; PF13499; EF-hand_7; 2.
DR   SMART; SM00054; EFh; 4.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Calcium; Metal-binding; Methylation;
KW   Reference proteome; Repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..149
FT                   /note="Calmodulin-1"
FT                   /id="PRO_0000439944"
FT   DOMAIN          8..43
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          44..79
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          81..116
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          117..149
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         21
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         23
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         25
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         27
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         32
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         57
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         59
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         61
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         63
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         94
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         96
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         98
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         100
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         105
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         130
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         132
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         134
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         136
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         141
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         116
FT                   /note="N6,N6,N6-trimethyllysine"
FT                   /evidence="ECO:0000250"
FT   HELIX           7..20
FT                   /evidence="ECO:0007829|PDB:1IQ5"
FT   STRAND          22..24
FT                   /evidence="ECO:0007829|PDB:2LLO"
FT   STRAND          25..28
FT                   /evidence="ECO:0007829|PDB:1IQ5"
FT   HELIX           30..39
FT                   /evidence="ECO:0007829|PDB:1IQ5"
FT   HELIX           46..56
FT                   /evidence="ECO:0007829|PDB:1IQ5"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:1F70"
FT   STRAND          61..65
FT                   /evidence="ECO:0007829|PDB:1IQ5"
FT   HELIX           66..76
FT                   /evidence="ECO:0007829|PDB:1IQ5"
FT   STRAND          77..81
FT                   /evidence="ECO:0007829|PDB:1NWD"
FT   HELIX           84..93
FT                   /evidence="ECO:0007829|PDB:1IQ5"
FT   TURN            95..97
FT                   /evidence="ECO:0007829|PDB:1CFF"
FT   STRAND          98..101
FT                   /evidence="ECO:0007829|PDB:1IQ5"
FT   HELIX           103..112
FT                   /evidence="ECO:0007829|PDB:1IQ5"
FT   STRAND          113..115
FT                   /evidence="ECO:0007829|PDB:5T0X"
FT   HELIX           119..129
FT                   /evidence="ECO:0007829|PDB:1IQ5"
FT   STRAND          134..138
FT                   /evidence="ECO:0007829|PDB:1IQ5"
FT   HELIX           139..146
FT                   /evidence="ECO:0007829|PDB:1IQ5"
SQ   SEQUENCE   149 AA;  16838 MW;  6B4BC3FCDE10727B CRC64;
     MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
     NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
     EVDEMIREAD IDGDGQVNYE EFVQMMTAK
 
 
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