CABP8_RAT
ID CABP8_RAT Reviewed; 261 AA.
AC Q06BI3; Q06BI2;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 91.
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;
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] (ISOFORM 2), AND 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 [2] {ECO:0000312|EMBL:ABI94065.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Mikhaylova M., Kreutz M.R.;
RT "Long isoform of Calneuron I, a protein involved in neuronal Ca2+-
RT signaling.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP FUNCTION, INTERACTION WITH PI4KB, AND SUBCELLULAR LOCATION.
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. May play a role in
CC the physiology of neurons and is potentially important in memory and
CC learning. {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|UniProtKB:Q9BXU9}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9BXU9}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q9BXU9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q06BI3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q06BI3-2; Sequence=VSP_060875;
CC -!- TISSUE SPECIFICITY: Brain-specific. High expression in the cerebellum,
CC hippocampus, and cortex. {ECO:0000269|PubMed:17055077}.
CC -!- DOMAIN: The C-terminal transmembrane domain (TMD) is necessary and
CC sufficient for membrane targeting. {ECO:0000250|UniProtKB:Q9BXU9}.
CC -!- MISCELLANEOUS: Calcium binding induces conformational changes in
CC CALN1/CABP8. The calcium binding affinity is not regulated by
CC magnesium.
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DR EMBL; DQ914829; ABI94064.1; -; mRNA.
DR EMBL; DQ914830; ABI94065.1; -; mRNA.
DR EMBL; AABR07035976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07035980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07035978; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07035977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07035979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001070669.1; NM_001077201.1. [Q06BI3-1]
DR RefSeq; XP_006249305.1; XM_006249243.3. [Q06BI3-2]
DR RefSeq; XP_017453898.1; XM_017598409.1. [Q06BI3-2]
DR AlphaFoldDB; Q06BI3; -.
DR SMR; Q06BI3; -.
DR STRING; 10116.ENSRNOP00000001185; -.
DR PaxDb; Q06BI3; -.
DR Ensembl; ENSRNOT00000001185; ENSRNOP00000001185; ENSRNOG00000000886. [Q06BI3-1]
DR GeneID; 363909; -.
DR KEGG; rno:363909; -.
DR CTD; 83698; -.
DR RGD; 1305843; Caln1.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000159212; -.
DR HOGENOM; CLU_106115_0_0_1; -.
DR InParanoid; Q06BI3; -.
DR OMA; EFEVHSQ; -.
DR OrthoDB; 1542616at2759; -.
DR TreeFam; TF331025; -.
DR PRO; PR:Q06BI3; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000000886; Expressed in frontal cortex and 4 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 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_0000383473"
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_060875"
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
