CABP8_MOUSE
ID CABP8_MOUSE Reviewed; 261 AA.
AC Q9JJG7; F8WHE1;
DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Calcium-binding protein 8;
DE Short=CaBP8;
DE AltName: Full=Calneuron I;
DE AltName: Full=Calneuron-1;
GN Name=Caln1; Synonyms=Cabp8; ORFNames=MNCb-0849;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=11286509; DOI=10.1006/mgme.2001.3160;
RA Wu Y.-Q., Lin X., Liu C.-M., Jamrich M., Shaffer L.G.;
RT "Identification of a human brain-specific gene, calneuron 1, a new member
RT of the calmodulin superfamily.";
RL Mol. Genet. Metab. 72:343-350(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Negatively regulates Golgi-to-plasma membrane trafficking by
CC interacting with PI4KB and inhibiting its activity. May play a role in
CC the physiology of neurons and is potentially important in memory and
CC learning. {ECO:0000250|UniProtKB:Q06BI3}.
CC -!- SUBUNIT: Interacts with PI4KB. This binding competes with FREQ/NCS1
CC binding in a calcium-dependent manner. {ECO:0000250|UniProtKB:Q06BI3}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000250|UniProtKB:Q9BXU9}; Single-pass type IV membrane protein
CC {ECO:0000255}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q9BXU9}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9BXU9}; Single-pass type IV membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JJG7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JJG7-2; Sequence=VSP_060874;
CC -!- TISSUE SPECIFICITY: Brain-specific. High expression in the cerebellum,
CC hippocampus, and cortex.
CC -!- DEVELOPMENTAL STAGE: Shows little prenatal expression, with highest
CC expression at postnatal day 21.
CC -!- DOMAIN: The C-terminal transmembrane domain (TMD) is necessary and
CC sufficient for membrane targeting. {ECO:0000250|UniProtKB:Q9BXU9}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK15156.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF282251; AAK15156.1; ALT_INIT; mRNA.
DR EMBL; AB041539; BAA95024.1; -; mRNA.
DR EMBL; AC169670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC120437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC142405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC156620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057129; AAH57129.1; -; mRNA.
DR EMBL; BC058963; AAH58963.1; -; mRNA.
DR CCDS; CCDS19714.1; -. [Q9JJG7-2]
DR CCDS; CCDS51656.1; -. [Q9JJG7-1]
DR RefSeq; NP_067346.1; NM_021371.2. [Q9JJG7-2]
DR RefSeq; NP_851388.1; NM_181045.1. [Q9JJG7-1]
DR RefSeq; XP_006504435.1; XM_006504372.3. [Q9JJG7-1]
DR RefSeq; XP_006504436.1; XM_006504373.2. [Q9JJG7-2]
DR RefSeq; XP_006504437.1; XM_006504374.2. [Q9JJG7-2]
DR AlphaFoldDB; Q9JJG7; -.
DR SMR; Q9JJG7; -.
DR IntAct; Q9JJG7; 1.
DR STRING; 10090.ENSMUSP00000083193; -.
DR iPTMnet; Q9JJG7; -.
DR PhosphoSitePlus; Q9JJG7; -.
DR PaxDb; Q9JJG7; -.
DR PRIDE; Q9JJG7; -.
DR ProteomicsDB; 273820; -. [Q9JJG7-1]
DR ProteomicsDB; 318093; -.
DR Antibodypedia; 28332; 170 antibodies from 28 providers.
DR DNASU; 140904; -.
DR Ensembl; ENSMUST00000086029; ENSMUSP00000083193; ENSMUSG00000060371. [Q9JJG7-1]
DR Ensembl; ENSMUST00000111287; ENSMUSP00000106918; ENSMUSG00000060371. [Q9JJG7-2]
DR Ensembl; ENSMUST00000111288; ENSMUSP00000106919; ENSMUSG00000060371. [Q9JJG7-2]
DR GeneID; 140904; -.
DR KEGG; mmu:140904; -.
DR UCSC; uc008zum.2; mouse.
DR UCSC; uc008zuo.2; mouse. [Q9JJG7-1]
DR CTD; 83698; -.
DR MGI; MGI:2155987; Caln1.
DR VEuPathDB; HostDB:ENSMUSG00000060371; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000159212; -.
DR HOGENOM; CLU_106115_0_0_1; -.
DR InParanoid; Q9JJG7; -.
DR OMA; EFEVHSQ; -.
DR OrthoDB; 1542616at2759; -.
DR PhylomeDB; Q9JJG7; -.
DR TreeFam; TF331025; -.
DR BioGRID-ORCS; 140904; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Caln1; mouse.
DR PRO; PR:Q9JJG7; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9JJG7; protein.
DR Bgee; ENSMUSG00000060371; Expressed in nucleus accumbens and 103 other tissues.
DR ExpressionAtlas; Q9JJG7; baseline and differential.
DR Genevisible; Q9JJG7; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0032588; C:trans-Golgi network membrane; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; 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; IPR001751; S100/CaBP7/8-like_CS.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell membrane; Cytoplasm; Golgi apparatus;
KW Membrane; Metal-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..261
FT /note="Calcium-binding protein 8"
FT /id="PRO_0000073530"
FT TOPO_DOM 1..234
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 78..113
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 114..149
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_060874"
SQ SEQUENCE 261 AA; 29625 MW; D38AE0DFBBAE38D9 CRC64;
MRLPEQPGDG KPENETKGDQ ETPERGEEPR RSPAPDFPTW EKMPFHHVTA GLLYKGNYLN
RSLSAGSDSE QLANISVEEL DEIREAFRVL DRDGNGFISK QELGMAMRSL GYMPSEVELA
IIMQRLDMDG DGQVDFDEFM TILGPKLVSS EGRDGFLGNT IDSIFWQFDM QRVTLEELKH
ILYHAFRDHL TMKDIENIII NEEESLNETS GNCQTEFEGV HSQKQNRQTC VRKSLICAFA
MAFIISVMLI AANQILRSGM E
