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NCS1_XENLA
ID   NCS1_XENLA              Reviewed;         190 AA.
AC   Q91614; Q6GQJ0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Neuronal calcium sensor 1;
DE            Short=NCS-1;
DE   AltName: Full=Frequenin;
GN   Name=ncs1; Synonyms=freq;
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 [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7644528; DOI=10.1073/pnas.92.17.8001;
RA   Olafsson P., Wang T., Lu B.;
RT   "Molecular cloning and functional characterization of the Xenopus Ca(2+)-
RT   binding protein frequenin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:8001-8005(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Neuronal calcium sensor, regulator of G protein-coupled
CC       receptor phosphorylation in a calcium dependent manner. Directly
CC       regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for
CC       calmodulin (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250|UniProtKB:P62166}.
CC       Postsynaptic density {ECO:0000250|UniProtKB:P62166}. Cytoplasm,
CC       perinuclear region {ECO:0000250|UniProtKB:P62166}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P62168}. Cell membrane
CC       {ECO:0000250|UniProtKB:P62166}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P62166}. Membrane
CC       {ECO:0000250|UniProtKB:P62168}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:P62166}.
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- DEVELOPMENTAL STAGE: Is not detectable until stage 21, when spinal
CC       neurons begin to establish synaptic contacts with muscle cells, levels
CC       increase dramatically around stage 40.
CC   -!- MISCELLANEOUS: Binds 3 calcium ions via the second, third and fourth
CC       EF-hand. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR   EMBL; U27274; AAC59690.1; -; mRNA.
DR   EMBL; BC072752; AAH72752.1; -; mRNA.
DR   PIR; I51686; I51686.
DR   RefSeq; NP_001084088.1; NM_001090619.1.
DR   AlphaFoldDB; Q91614; -.
DR   SMR; Q91614; -.
DR   DNASU; 399297; -.
DR   GeneID; 399297; -.
DR   KEGG; xla:399297; -.
DR   CTD; 399297; -.
DR   Xenbase; XB-GENE-953746; ncs1.L.
DR   OrthoDB; 1369072at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 399297; Expressed in brain and 17 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0010975; P:regulation of neuron projection development; ISS:UniProtKB.
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   InterPro; IPR028846; Recoverin.
DR   PANTHER; PTHR23055; PTHR23055; 1.
DR   Pfam; PF00036; EF-hand_1; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   PROSITE; PS00018; EF_HAND_1; 3.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   2: Evidence at transcript level;
KW   Calcium; Cell membrane; Cytoplasm; Golgi apparatus; Lipoprotein; Membrane;
KW   Metal-binding; Myristate; Reference proteome; Repeat; Synapse.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..190
FT                   /note="Neuronal calcium sensor 1"
FT                   /id="PRO_0000073792"
FT   DOMAIN          24..59
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          60..95
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          96..131
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          144..179
FT                   /note="EF-hand 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         73
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         75
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         77
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         79
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         84
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         109
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         111
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         113
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         115
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         120
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         157
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         159
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT   BINDING         161
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         163
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         168
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   190 AA;  21925 MW;  4EC80C6B93F8056F CRC64;
     MGKSNSKLKP EVVEELTRKT YFTEKEVQQW YKGFIKDCPS GQLDATGFQK IYKQFFPFGD
     PTKFATFVFN VFDENKDGRI EFSEFIQALS VTSRGTLDEK LRWAFKLYDL DNDGYITRNE
     MLDIVDAIYQ MVGNTVELPE EENTPEKRVD RIFAMMDKNS DGKLTLQEFQ EGSKADPSIV
     QALSLYDGLV
 
 
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