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CDPK1_PLAFK
ID   CDPK1_PLAFK             Reviewed;         524 AA.
AC   P62343; Q27731;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Calcium-dependent protein kinase 1;
DE            EC=2.7.11.1 {ECO:0000269|PubMed:8142371, ECO:0000269|PubMed:8440720};
DE   AltName: Full=PfCDPK1;
DE            Short=PfCPK;
GN   Name=CDPK1 {ECO:0000250|UniProtKB:P62344}; Synonyms=CPK1;
OS   Plasmodium falciparum (isolate K1 / Thailand).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5839;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=8440720; DOI=10.1016/s0021-9258(18)53616-4;
RA   Zhao Y., Kappes B., Franklin R.M.;
RT   "Gene structure and expression of an unusual protein kinase from Plasmodium
RT   falciparum homologous at its carboxyl terminus with the EF hand calcium-
RT   binding proteins.";
RL   J. Biol. Chem. 268:4347-4354(1993).
RN   [2]
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, CALCIUM-BINDING, AND MUTAGENESIS
RP   OF GLU-396; GLU-440; GLU-476 AND GLU-510.
RX   PubMed=8142371; DOI=10.1021/bi00178a031;
RA   Zhao Y., Pokutta S., Maurer P., Lindt M., Franklin R.M., Kappes B.;
RT   "Calcium-binding properties of a calcium-dependent protein kinase from
RT   Plasmodium falciparum and the significance of individual calcium-binding
RT   sites for kinase activation.";
RL   Biochemistry 33:3714-3721(1994).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBCELLULAR
RP   LOCATION, DEVELOPMENTAL STAGE, AND AUTOPHOSPHORYLATION.
RX   PubMed=7808482; DOI=10.1016/0166-6851(94)90159-7;
RA   Zhao Y., Franklin R.M., Kappes B.;
RT   "Plasmodium falciparum calcium-dependent protein kinase phosphorylates
RT   proteins of the host erythrocytic membrane.";
RL   Mol. Biochem. Parasitol. 66:329-343(1994).
CC   -!- FUNCTION: Calcium-dependent protein kinase which acts as a sensor and
CC       effector of intracellular Ca(2+) levels probably in part downstream of
CC       cGMP-activated PKG kinase (PubMed:7808482). By phosphorylating various
CC       proteins, required for microneme secretion and thus merozoite egress
CC       from and invasion of host erythrocytes (By similarity). During
CC       gametogenesis, essential for the development of both male and female
CC       gametes (By similarity). Phosphorylates SERA5 p50 which enhances SERA5
CC       p50 protease activity; however, SERA5 p50 protease activity has been
CC       shown in other studies to be controversial. Probably by phosphorylating
CC       SERA5 p50, plays a role in merozoite egress from host erythrocytes.
CC       Probably prior or during merozoite invasion of host erythrocytes,
CC       phosphorylates rhoptry protein RhopH3 which is required for RhopH3
CC       localization to rhoptries and for its secretion. Probably in late
CC       schizonts, phosphorylates myosin A tail domain-interacting protein MTIP
CC       and glideosome-associated protein 45 GAP45, both of which are
CC       components of the motor complex that generates the force required by
CC       the parasite to invade host cells. In late schizonts, phosphorylates
CC       inner membrane complex protein IMC1g. In late schizonts, phosphorylates
CC       PKA regulatory subunit PKAr in a calcium-dependent manner, which may
CC       contribute to the dissociation of regulatory PKAr and catalytic PKAc
CC       subunits and promote the activation of PKAc. May phosphorylate raf
CC       kinase inhibitory protein RKIP which in turn may regulate CDPK1
CC       catalytic activity (By similarity). May phosphorylate proteins of the
CC       host erythrocyte membranes (PubMed:7808482).
CC       {ECO:0000250|UniProtKB:A0A2I0BVG8, ECO:0000250|UniProtKB:P62344,
CC       ECO:0000269|PubMed:7808482}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000269|PubMed:8142371, ECO:0000269|PubMed:8440720};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000269|PubMed:8142371,
CC         ECO:0000269|PubMed:8440720};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:7808482};
CC       Note=Can use both Mg(2+) and Mn(2+) in vitro and shows higher activity
CC       with Mn(2+) but Mg(2+) is likely to be the in vivo cofactor.
CC       {ECO:0000269|PubMed:7808482};
CC   -!- ACTIVITY REGULATION: Activated by calcium (PubMed:8440720,
CC       PubMed:8142371, PubMed:7808482). Upon calcium binding to the EF-hand
CC       domains, the C-terminus of the junction domain (J domain) undergoes a
CC       conformational change which results in the dissociation of the pseudo-
CC       substrate inhibitory motif from the catalytic domain (By similarity).
CC       This, in turn may facilitate the autophosphorylation of the activation
CC       loop at Thr-231, which leads to the kinase activation (By similarity).
CC       Inhibited by calmodulin antagonists such as calmidazolium,
CC       trifluoperazine, N-[6-aminohexyl]-5-chloro-1-naphthalene-sulfonamide,
CC       and ophiobolin A (PubMed:7808482). {ECO:0000250|UniProtKB:P62344,
CC       ECO:0000269|PubMed:7808482, ECO:0000269|PubMed:8142371,
CC       ECO:0000269|PubMed:8440720}.
CC   -!- SUBUNIT: Monomer. Forms a high molecular weight (250 and 400 kDa)
CC       complex. Forms a complex composed of CDPK1, PKA regulatory subunit PKAr
CC       and 14-3-3I; the complex is formed in merozoites in response to low
CC       extracellular level of K(+) and may play a role in microneme secretion.
CC       Interacts (when phosphorylated) with 14-3-3I in a Ca(2+)-independent
CC       manner; the interaction does not regulate CDPK1 catalytic activity but
CC       is required for merozoite invasion of host erythrocytes. Interacts with
CC       PKA regulatory subunit PKAr; in a Ca(2+)-dependent manner. Interacts
CC       with SERA5 p50 in the late schizont stage. Interacts with inner
CC       membrane complex protein IMC1g in late schizonts. Interacts with
CC       rhoptry protein RhopH3 in merozoites. {ECO:0000250|UniProtKB:P62344}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:7808482}; Lipid-
CC       anchor {ECO:0000269|PubMed:7808482}. Cell membrane
CC       {ECO:0000250|UniProtKB:P62344}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P62344}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P62344}. Parasitophorous vacuole membrane
CC       {ECO:0000250|UniProtKB:P62344}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P62344}. Cytoplasm
CC       {ECO:0000250|UniProtKB:A0A2I0BVG8}. Cell projection, cilium, flagellum
CC       {ECO:0000250|UniProtKB:A0A2I0BVG8}. Host cell membrane
CC       {ECO:0000250|UniProtKB:P62344}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P62344}. Note=Localizes to the host erythrocytic
CC       membrane at low level (PubMed:7808482). Localizes to the cell membrane
CC       in the nascent merozoites contained within the late-stage schizonts and
CC       in free merozoites. Colocalizes with MTIP around developing merozoites
CC       in segmented schizonts, also localizes in membranes around the mature
CC       food vacuole/residual body of the schizonts. Ser-64 phosphorylated form
CC       localizes at the apical pole in punctate structures in merozoites
CC       within late schizonts in free merozoites. In trophozoites and
CC       schizonts, localizes to the parasitophorous vacuole (PV) and in
CC       membranous systems derived from the PV including intraparasitic
CC       vacuoles and the tubovesicular system, an extension of the
CC       parasitophorous vacuole membrane into the host cell cytoplasm.
CC       Localization to the cytoplasm in trophozoite or schizonts is minimal
CC       (By similarity). In female stage V gametocytes and gametes, localizes
CC       to the cell membrane. In stage V male gametocytes, localizes to the
CC       cell membrane and in the cytoplasm. In male gametes, localizes to the
CC       residual body, cell membrane and in the flagella (By similarity).
CC       Calcium and/or autophosphorylation does not affect membrane
CC       localization (By similarity). {ECO:0000250|UniProtKB:A0A2I0BVG8,
CC       ECO:0000250|UniProtKB:P62344, ECO:0000269|PubMed:7808482}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in ring and schizont stages and to a
CC       lesser extent in early and late trophozoite stages.
CC       {ECO:0000269|PubMed:7808482}.
CC   -!- DOMAIN: The junction domain (J domain) is composed of 2 motifs that
CC       maintain the kinase inactive. The N-terminal autoinhibitory motif acts
CC       as a pseudosubstrate inhibiting the catalytic domain while the C-
CC       terminal motif binds the EF-hand domains.
CC       {ECO:0000250|UniProtKB:P62344}.
CC   -!- PTM: Myristoylated. Myristoylation, palmitoylation and the basic
CC       cluster motif are required for the localization to the parasitophorous
CC       vacuole membrane. {ECO:0000250|UniProtKB:P62344}.
CC   -!- PTM: Palmitoylated. Palmitoylation increases in merozoites in response
CC       to low level of extracellular K(+) in the host blood. Myristoylation,
CC       palmitoylation and the basic cluster motif are required for the
CC       localization to the parasitophorous vacuole membrane.
CC       {ECO:0000250|UniProtKB:P62344}.
CC   -!- PTM: Phosphorylation at Ser-64 occurs at late schizont stage and
CC       regulates CDPK1 protein-protein interaction. Phosphorylated at Ser-28,
CC       Ser-34 and Ser-64 in merozoites in response to low extracellular level
CC       of K(+). Phosphorylation at Thr-231 may regulate CDPK1 kinase activity.
CC       Phosphorylation increases in response to an increase in intracellular
CC       Ca(2+) levels (By similarity). Autophosphorylated in vitro
CC       (PubMed:7808482). Autophosphorylation does not affect membrane
CC       localization in vitro (By similarity). {ECO:0000250|UniProtKB:P62344,
CC       ECO:0000269|PubMed:7808482}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. CDPK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; X67288; CAA47704.1; -; mRNA.
DR   AlphaFoldDB; P62343; -.
DR   SMR; P62343; -.
DR   BindingDB; P62343; -.
DR   PRIDE; P62343; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020005; C:symbiont-containing vacuole membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IEA:UniProt.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   CDD; cd00051; EFh; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF13499; EF-hand_7; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00054; EFh; 4.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 4.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Cell membrane; Cell projection; Cilium; Cytoplasm;
KW   Flagellum; Host cell membrane; Host membrane; Kinase; Lipoprotein;
KW   Membrane; Metal-binding; Myristate; Nucleotide-binding; Palmitate;
KW   Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   CHAIN           2..524
FT                   /note="Calcium-dependent protein kinase 1"
FT                   /id="PRO_0000085835"
FT   DOMAIN          56..325
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          372..407
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          416..451
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          452..487
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          488..521
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          346..364
FT                   /note="J domain"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   MOTIF           10..20
FT                   /note="J domain basic cluster involved in membrane binding"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   MOTIF           346..353
FT                   /note="J domain autoinhibitory motif"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   MOTIF           354..364
FT                   /note="Interacts with the EF-hand domains"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   COMPBIAS        18..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        191
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         62..70
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         385
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         387
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         389
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         391
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         396
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         429
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         431
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         433
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         435
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         440
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         465
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         467
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         469
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         471
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         476
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         499
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         501
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         503
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         505
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         510
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   MOD_RES         17
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   MOD_RES         28
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   MOD_RES         64
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   MOD_RES         100
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   MOD_RES         118
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   MOD_RES         217
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   MOD_RES         220
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   MOD_RES         231
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   MOD_RES         335
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P62344"
FT   MUTAGEN         396
FT                   /note="E->K,Q: Induces a strong decrease in calcium-
FT                   binding. Strongly affects kinase activity."
FT                   /evidence="ECO:0000269|PubMed:8142371"
FT   MUTAGEN         440
FT                   /note="E->K,Q: Almost abolishes in calcium-binding.
FT                   Abolishes kinase activity."
FT                   /evidence="ECO:0000269|PubMed:8142371"
FT   MUTAGEN         476
FT                   /note="E->K,Q: Induces a slight decrease in calcium-binding
FT                   and kinase activity."
FT                   /evidence="ECO:0000269|PubMed:8142371"
FT   MUTAGEN         510
FT                   /note="E->K,Q: Induces a slight decrease in calcium-binding
FT                   and kinase activity."
FT                   /evidence="ECO:0000269|PubMed:8142371"
SQ   SEQUENCE   524 AA;  60800 MW;  D2A45E1579D2C951 CRC64;
     MGCSQSSNVK DFKTRRSKFT NGNNYGKSGN NKNSEDLAIN PGMYVRKKEG KIGESYFKVR
     KLGSGAYGEV LLCREKHGHG EKAIKVIKKS QFDKMKYSIT NKIECDDKIH EEIYNEISLL
     KSLDHPNIIK LFDVFEDKKY FYLVTEFYEG GELFEQIINR HKFDECDAAN IMKQILSGIC
     YLHKHNIVHR DIKPENILLE NKHSLLNIKI VDFGLSSFFS KDNKLRDRLG TAYYIAPEVL
     RKKYNEKCDV WSCGVILYIL LCGYPPFGGQ NDQDIIKKVE KGKYYFDFND WKNISEEAKE
     LIKLMLTYDY NKRITAKEAL NSKWIKKYAN NINKSDQKTL CGALSNMRKF EGSQKLAQAA
     ILFIGSKLTT LEERKELTDI FKKLDKNGDG QLDKKELIEG YNILRSFKNE LGELKNVEEE
     VDNILKEVDF DKNGYIEYSE FISVCMDKQI LFSEERLRDA FNLFDTDKSG KITKEELANL
     FGLTSISEQM WNEVLGEADK NKDNMIDFDE FVNMMHKICD NKSS
 
 
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