CABP7_RAT
ID CABP7_RAT Reviewed; 215 AA.
AC Q66H96;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Calcium-binding protein 7;
DE Short=CaBP7;
DE AltName: Full=Calneuron II;
DE AltName: Full=Calneuron-2;
GN Name=Cabp7; Synonyms=Caln2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Kim H., Hong S.;
RT "Rat calcium binding protein 7.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=17055077; DOI=10.1016/j.bbamcr.2006.08.047;
RA Mikhaylova M., Sharma Y., Reissner C., Nagel F., Aravind P., Rajini B.,
RA Smalla K.-H., Gundelfinger E.D., Kreutz M.R.;
RT "Neuronal Ca2+ signaling via caldendrin and calneurons.";
RL Biochim. Biophys. Acta 1763:1229-1237(2006).
RN [4]
RP SUBCELLULAR LOCATION, INTERACTION WITH PI4KB, AND FUNCTION.
RX PubMed=19458041; DOI=10.1073/pnas.0903001106;
RA Mikhaylova M., Reddy P.P., Munsch T., Landgraf P., Suman S.K.,
RA Smalla K.-H., Gundelfinger E.D., Sharma Y., Kreutz M.R.;
RT "Calneurons provide a calcium threshold for trans-Golgi network to plasma
RT membrane trafficking.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:9093-9098(2009).
CC -!- FUNCTION: Negatively regulates Golgi-to-plasma membrane trafficking by
CC interacting with PI4KB and inhibiting its activity.
CC {ECO:0000269|PubMed:19458041}.
CC -!- SUBUNIT: Interacts with PI4KB. This binding competes with FREQ/NCS1
CC binding in a calcium-dependent manner. {ECO:0000269|PubMed:19458041}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000305|PubMed:19458041}; Single-pass type IV membrane protein
CC {ECO:0000305|PubMed:19458041}. Cytoplasm, perinuclear region
CC {ECO:0000250}. Cell membrane {ECO:0000250}; Single-pass type IV
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Brain-specific. Restricted to the CA3 region of the
CC hippocampus, entorhinal cortex, the antero-dorsal and antero-ventral
CC thalamus and the inferior and superior colliculus.
CC {ECO:0000269|PubMed:17055077}.
CC -!- DOMAIN: The C-terminal transmembrane domain (TMD) is necessary and
CC sufficient for membrane targeting. {ECO:0000250}.
CC -!- MISCELLANEOUS: The calcium-binding affinity is not regulated by
CC magnesium.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY841152; AAW21810.1; -; mRNA.
DR EMBL; BC081959; AAH81959.1; -; mRNA.
DR RefSeq; NP_001007731.1; NM_001007730.2.
DR AlphaFoldDB; Q66H96; -.
DR BMRB; Q66H96; -.
DR SMR; Q66H96; -.
DR STRING; 10116.ENSRNOP00000010439; -.
DR PaxDb; Q66H96; -.
DR Ensembl; ENSRNOT00000078179; ENSRNOP00000074795; ENSRNOG00000057703.
DR GeneID; 360970; -.
DR KEGG; rno:360970; -.
DR UCSC; RGD:1359269; rat.
DR CTD; 164633; -.
DR RGD; 1359269; Cabp7.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000159368; -.
DR HOGENOM; CLU_106115_0_0_1; -.
DR InParanoid; Q66H96; -.
DR OMA; CPVEVET; -.
DR OrthoDB; 1542616at2759; -.
DR PhylomeDB; Q66H96; -.
DR TreeFam; TF331025; -.
DR PRO; PR:Q66H96; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000057703; Expressed in cerebellum and 3 other tissues.
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; ISO:RGD.
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 1: Evidence at protein level;
KW Calcium; Cell membrane; Cytoplasm; Golgi apparatus; Membrane;
KW Metal-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..215
FT /note="Calcium-binding protein 7"
FT /id="PRO_0000383472"
FT TOPO_DOM 1..188
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 210..215
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 33..68
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 69..104
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 46
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 48
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 50
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="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 84
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 86
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 88
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 215 AA; 24453 MW; 9C254C955F7AFFA8 CRC64;
MPFHPVTAAL MYRGIYTVPN LLSEQRPVDI PEDELEEIRE AFKVFDRDGN GFISKQELGT
AMRSLGYMPN EVELEVIIQR LDMDGDGQVD FEEFVTLLGP KLSTSGIPEK FHGTDFDTVF
WKCDMQKLTV DELKRLLYDT FCEHLSMKDI ENIIMTEEES HLGTAEECPV DVETCSNQQI
RQTCVRKSLI CAFAIAFIIS VMLIAANQVL RSGMK
