CABP1_HUMAN
ID CABP1_HUMAN Reviewed; 370 AA.
AC Q9NZU7; O95663; Q8N6H5; Q9NZU8;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 5.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Calcium-binding protein 1;
DE Short=CaBP1;
DE AltName: Full=Calbrain;
DE AltName: Full=Caldendrin;
GN Name=CABP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CALBRAIN).
RC TISSUE=Cerebellum;
RX PubMed=9920909; DOI=10.1074/jbc.274.6.3610;
RA Yamaguchi K., Yamaguchi F., Miyamoto O., Sugimoto K., Konishi R.,
RA Hatase O.;
RT "Calbrain, a novel two EF-hand calcium-binding protein that suppresses
RT Ca2+/calmodulin-dependent protein kinase II activity in the brain.";
RL J. Biol. Chem. 274:3610-3616(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS L-CABP1 AND S-CABP1), MYRISTOYLATION
RP AT GLY-2 (ISOFORMS L-CABP1 AND S-CABP1), PALMITOYLATION AT CYS-4 (ISOFORMS
RP L-CABP1 AND S-CABP1), AND SUBCELLULAR LOCATION.
RC TISSUE=Retina;
RX PubMed=10625670; DOI=10.1074/jbc.275.2.1247;
RA Haeseleer F., Sokal I., Verlinde C.L.M.J., Erdjument-Bromage H., Tempst P.,
RA Pronin A.N., Benovic J.L., Fariss R.N., Palczewski K.;
RT "Five members of a novel Ca(2+)-binding protein (CABP) subfamily with
RT similarity to calmodulin.";
RL J. Biol. Chem. 275:1247-1260(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CALDENDRIN).
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 [5]
RP ALTERNATIVE SPLICING (ISOFORM CALDENDRIN).
RX PubMed=9694893; DOI=10.1074/jbc.273.33.21324;
RA Seidenbecher C.I., Langnaese K., Sanmarti-Vila L., Boeckers T.M.,
RA Smalla K.-H., Sabel B.A., Garner C.C., Gundelfinger E.D., Kreutz M.R.;
RT "Caldendrin, a novel neuronal calcium-binding protein confined to the
RT somato-dendritic compartment.";
RL J. Biol. Chem. 273:21324-21331(1998).
RN [6]
RP INTERACTION WITH ITPR1; ITPR2 AND ITPR3, AND MUTAGENESIS OF ASP-238;
RP ASP-240; ASP-315; ASN-317; ASP-352 AND ASN-354.
RX PubMed=12032348; DOI=10.1073/pnas.102006299;
RA Yang J., McBride S., Mak D.-O.D., Vardi N., Palczewski K., Haeseleer F.,
RA Foskett J.K.;
RT "Identification of a family of calcium sensors as protein ligands of
RT inositol trisphosphate receptor Ca(2+) release channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7711-7716(2002).
RN [7]
RP FUNCTION, AND INTERACTION WITH CACNA1A.
RX PubMed=11865310; DOI=10.1038/nn805;
RA Lee A., Westenbroek R.E., Haeseleer F., Palczewski K., Scheuer T.,
RA Catterall W.A.;
RT "Differential modulation of Ca(v)2.1 channels by calmodulin and Ca2+-
RT binding protein 1.";
RL Nat. Neurosci. 5:210-217(2002).
RN [8]
RP PHOSPHORYLATION AT SER-323, MUTAGENESIS OF SER-323, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH ITPR1.
RX PubMed=14685260; DOI=10.1038/sj.emboj.7600037;
RA Kasri N.N., Holmes A.M., Bultynck G., Parys J.B., Bootman M.D.,
RA Rietdorf K., Missiaen L., McDonald F., De Smedt H., Conway S.J.,
RA Holmes A.B., Berridge M.J., Roderick H.L.;
RT "Regulation of InsP3 receptor activity by neuronal Ca2+-binding proteins.";
RL EMBO J. 23:312-321(2004).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14570872; DOI=10.1074/jbc.m309617200;
RA Haynes L.P., Tepikin A.V., Burgoyne R.D.;
RT "Calcium-binding protein 1 is an inhibitor of agonist-evoked, inositol
RT 1,4,5-trisphosphate-mediated calcium signaling.";
RL J. Biol. Chem. 279:547-555(2004).
RN [10]
RP INTERACTION WITH MAP1LC3B.
RX PubMed=15095872; DOI=10.1016/j.jmb.2003.12.054;
RA Seidenbecher C.I., Landwehr M., Smalla K.H., Kreutz M., Dieterich D.C.,
RA Zuschratter W., Reissner C., Hammarback J.A., Bockers T.M.,
RA Gundelfinger E.D., Kreutz M.R.;
RT "Caldendrin but not calmodulin binds to light chain 3 of MAP1A/B: an
RT association with the microtubule cytoskeleton highlighting exclusive
RT binding partners for neuronal Ca(2+)-sensor proteins.";
RL J. Mol. Biol. 336:957-970(2004).
RN [11]
RP FUNCTION, AND INTERACTION WITH CACNA1C.
RX PubMed=15140941; DOI=10.1523/jneurosci.5523-03.2004;
RA Zhou H., Kim S.-A., Kirk E.A., Tippens A.L., Sun H., Haeseleer F., Lee A.;
RT "Ca2+-binding protein-1 facilitates and forms a postsynaptic complex with
RT Cav1.2 (L-type) Ca2+ channels.";
RL J. Neurosci. 24:4698-4708(2004).
RN [12]
RP FUNCTION, AND INTERACTION WITH CACNA1C.
RX PubMed=15980432; DOI=10.1074/jbc.m504167200;
RA Zhou H., Yu K., McCoy K.L., Lee A.;
RT "Molecular mechanism for divergent regulation of Cav1.2 Ca2+ channels by
RT calmodulin and Ca2+-binding protein-1.";
RL J. Biol. Chem. 280:29612-29619(2005).
RN [13]
RP FUNCTION, AND INTERACTION WITH TRPC5.
RX PubMed=15895247; DOI=10.1007/s00424-005-1419-1;
RA Kinoshita-Kawada M., Tang J., Xiao R., Kaneko S., Foskett J.K., Zhu M.X.;
RT "Inhibition of TRPC5 channels by Ca2+-binding protein 1 in Xenopus
RT oocytes.";
RL Pflugers Arch. 450:345-354(2005).
RN [14]
RP SUBUNIT, CALCIUM-BINDING, AND MAGNESIUM-BINDING.
RX PubMed=16147998; DOI=10.1074/jbc.m508541200;
RA Wingard J.N., Chan J., Bosanac I., Haeseleer F., Palczewski K., Ikura M.,
RA Ames J.B.;
RT "Structural analysis of Mg2+ and Ca2+ binding to CaBP1, a neuron-specific
RT regulator of calcium channels.";
RL J. Biol. Chem. 280:37461-37470(2005).
RN [15]
RP STRUCTURE BY NMR OF 219-294 AND 299-370 IN COMPLEX WITH MAGNESIUM AND
RP CALCIUM, AND MUTAGENESIS OF ASP-238; ASP-240; ASP-242 AND ASP-249.
RX PubMed=19008222; DOI=10.1074/jbc.m806513200;
RA Li C., Chan J., Haeseleer F., Mikoshiba K., Palczewski K., Ikura M.,
RA Ames J.B.;
RT "Structural insights into Ca2+-dependent regulation of inositol 1,4,5-
RT trisphosphate receptors by CaBP1.";
RL J. Biol. Chem. 284:2472-2481(2009).
CC -!- FUNCTION: Modulates calcium-dependent activity of inositol 1,4,5-
CC triphosphate receptors (ITPRs)(PubMed:14570872). Inhibits agonist-
CC induced intracellular calcium signaling (PubMed:15980432). Enhances
CC inactivation and does not support calcium-dependent facilitation of
CC voltage-dependent P/Q-type calcium channels (PubMed:11865310). Causes
CC calcium-dependent facilitation and inhibits inactivation of L-type
CC calcium channels by binding to the same sites as calmodulin in the C-
CC terminal domain of CACNA1C, but has an opposite effect on channel
CC function (PubMed:15140941). Suppresses the calcium-dependent
CC inactivation of CACNA1D (By similarity). Inhibits TRPC5 channels
CC (PubMed:15895247). Prevents NMDA receptor-induced cellular
CC degeneration. Required for the normal transfer of light signals through
CC the retina (By similarity). {ECO:0000250|UniProtKB:O88751,
CC ECO:0000250|UniProtKB:Q9JLK7, ECO:0000269|PubMed:11865310,
CC ECO:0000269|PubMed:14570872, ECO:0000269|PubMed:15140941,
CC ECO:0000269|PubMed:15895247, ECO:0000269|PubMed:15980432}.
CC -!- SUBUNIT: Homodimer; when bound to calcium or magnesium. Interacts (via
CC C-terminus) with ITPR1, ITPR2 and ITPR3. This binding is calcium
CC dependent and the interaction correlates with calcium concentration. An
CC additional calcium-independent interaction with the N-terminus of ITPR1
CC results in a decreased InsP(3) binding to the receptor. Interacts with
CC CACNA1A (via C-terminal CDB motif) in the pre- and postsynaptic
CC membranes. Interacts with CACNA1C (via C-terminal C and IQ motifs). The
CC binding to the C motif is calcium independent whereas the binding to IQ
CC requires the presence of calcium and is mutually exclusive with
CC calmodulin binding. Interacts with CACNA1D (By similarity). Interacts
CC with TRPC5 (via C-terminus). Interacts (via EF-hands 1 and 2) at
CC microtubules with MAP1LC3B. Interacts with MYO1C (By similarity).
CC Interacts (via EF-hands 1 and 2) with NSMF (via the central NLS-
CC containing motif region), the interaction occurs in a calcium dependent
CC manner after synaptic NMDA receptor stimulation and prevents nuclear
CC import of NSMF. Interacts with SPACA9 (By similarity).
CC {ECO:0000250|UniProtKB:O88751, ECO:0000250|UniProtKB:Q9JLK7,
CC ECO:0000269|PubMed:11865310, ECO:0000269|PubMed:12032348,
CC ECO:0000269|PubMed:15095872, ECO:0000269|PubMed:15140941,
CC ECO:0000269|PubMed:15895247, ECO:0000269|PubMed:15980432}.
CC -!- INTERACTION:
CC Q9NZU7; Q13936: CACNA1C; NbExp=4; IntAct=EBI-907894, EBI-1038838;
CC Q9NZU7-2; Q13936-20: CACNA1C; NbExp=2; IntAct=EBI-15896740, EBI-15896749;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10625670}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:14685260}. Cell membrane
CC {ECO:0000269|PubMed:10625670, ECO:0000269|PubMed:14570872,
CC ECO:0000269|PubMed:14685260}; Lipid-anchor; Cytoplasmic side. Golgi
CC apparatus {ECO:0000269|PubMed:14570872, ECO:0000269|PubMed:14685260}.
CC Postsynaptic density {ECO:0000305}. Note=L-CaBP1 is associated most
CC likely with the cytoskeletal structures, whereas S-CaBP1 is localized
CC at or near the plasma membrane. {ECO:0000269|PubMed:10625670}.
CC -!- SUBCELLULAR LOCATION: [Isoform L-CaBP1]: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10625670}. Note=L-CaBP1 is associated most likely
CC with the cytoskeletal structures. {ECO:0000269|PubMed:10625670}.
CC -!- SUBCELLULAR LOCATION: [Isoform S-CaBP1]: Cytoplasm, cell cortex. Cell
CC membrane {ECO:0000305|PubMed:10625670}; Lipid-anchor {ECO:0000305}.
CC Note=S-CaBP1 is localized at or near the plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=Caldendrin;
CC IsoId=Q9NZU7-4; Sequence=Displayed;
CC Name=L-CaBP1; Synonyms=Caldendrin-S2;
CC IsoId=Q9NZU7-1; Sequence=VSP_037938, VSP_037939;
CC Name=S-CaBP1; Synonyms=Caldendrin-S1;
CC IsoId=Q9NZU7-2; Sequence=VSP_037937, VSP_037940;
CC Name=Calbrain;
CC IsoId=Q9NZU7-3; Sequence=VSP_037936;
CC -!- TISSUE SPECIFICITY: Retina and brain. Somatodendritic compartment of
CC neurons. Calbrain was found exclusively in brain where it is abundant
CC in the hippocampus, habenular area in the epithalamus and in the
CC cerebellum.
CC -!- DOMAIN: EF-1 binds magnesium constitutively under physiological
CC conditions, EF-3 and EF-4 bind calcium cooperatively and EF-2 binds
CC neither calcium nor magnesium.
CC -!- PTM: Phosphorylated. The phosphorylation regulates the activity.
CC {ECO:0000269|PubMed:14685260}.
CC -!- MISCELLANEOUS: [Isoform Calbrain]: It is currently uncertain whether
CC calbrain represent a spliced isoform. {ECO:0000305}.
CC -!- CAUTION: The interaction with CACNA1A is described as calcium
CC independent in PubMed:11865310 while it is shown to be acutely calcium
CC dependent in PubMed:14570872. PubMed:12032348 describes a stimulatory
CC effect of CABP1 during agonist-induced intracellular calcium signaling
CC while PubMed:14570872 and PubMed:11865310 show an inhibitory effect.
CC {ECO:0000305}.
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DR EMBL; X94700; CAA64361.1; -; mRNA.
DR EMBL; AF169148; AAF25782.1; -; mRNA.
DR EMBL; AF169149; AAF25783.1; -; mRNA.
DR EMBL; AC069234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030201; AAH30201.2; -; mRNA.
DR CCDS; CCDS31913.1; -. [Q9NZU7-4]
DR CCDS; CCDS9204.1; -. [Q9NZU7-2]
DR CCDS; CCDS9205.1; -. [Q9NZU7-1]
DR RefSeq; NP_001028849.1; NM_001033677.1. [Q9NZU7-4]
DR RefSeq; NP_004267.2; NM_004276.4. [Q9NZU7-2]
DR RefSeq; NP_112482.1; NM_031205.3. [Q9NZU7-1]
DR PDB; 2K7B; NMR; -; A=219-294.
DR PDB; 2K7C; NMR; -; A=299-370.
DR PDB; 2K7D; NMR; -; A=299-370.
DR PDB; 2LAN; NMR; -; A=219-370.
DR PDB; 2LAP; NMR; -; A=219-370.
DR PDB; 3OX5; X-ray; 2.90 A; A/B/C/D/E/F=219-370.
DR PDB; 3OX6; X-ray; 2.40 A; A/B/C/D/E/F=219-370.
DR PDBsum; 2K7B; -.
DR PDBsum; 2K7C; -.
DR PDBsum; 2K7D; -.
DR PDBsum; 2LAN; -.
DR PDBsum; 2LAP; -.
DR PDBsum; 3OX5; -.
DR PDBsum; 3OX6; -.
DR AlphaFoldDB; Q9NZU7; -.
DR BMRB; Q9NZU7; -.
DR SMR; Q9NZU7; -.
DR BioGRID; 114863; 11.
DR DIP; DIP-35477N; -.
DR IntAct; Q9NZU7; 5.
DR STRING; 9606.ENSP00000317310; -.
DR TCDB; 8.A.82.1.11; the calmodulin calcium binding protein (calmodulin) family.
DR iPTMnet; Q9NZU7; -.
DR PhosphoSitePlus; Q9NZU7; -.
DR BioMuta; CABP1; -.
DR DMDM; 334302962; -.
DR jPOST; Q9NZU7; -.
DR MassIVE; Q9NZU7; -.
DR PaxDb; Q9NZU7; -.
DR PeptideAtlas; Q9NZU7; -.
DR PRIDE; Q9NZU7; -.
DR ProteomicsDB; 83512; -. [Q9NZU7-4]
DR ProteomicsDB; 83513; -. [Q9NZU7-1]
DR ProteomicsDB; 83514; -. [Q9NZU7-2]
DR ProteomicsDB; 83515; -. [Q9NZU7-3]
DR Antibodypedia; 31502; 125 antibodies from 30 providers.
DR DNASU; 9478; -.
DR Ensembl; ENST00000288616.7; ENSP00000288616.3; ENSG00000157782.10. [Q9NZU7-1]
DR Ensembl; ENST00000316803.8; ENSP00000317310.3; ENSG00000157782.10. [Q9NZU7-4]
DR Ensembl; ENST00000351200.6; ENSP00000288615.2; ENSG00000157782.10. [Q9NZU7-2]
DR GeneID; 9478; -.
DR KEGG; hsa:9478; -.
DR MANE-Select; ENST00000316803.8; ENSP00000317310.3; NM_001033677.2; NP_001028849.1.
DR UCSC; uc001tyu.4; human. [Q9NZU7-4]
DR CTD; 9478; -.
DR DisGeNET; 9478; -.
DR GeneCards; CABP1; -.
DR HGNC; HGNC:1384; CABP1.
DR HPA; ENSG00000157782; Group enriched (brain, choroid plexus).
DR MIM; 605563; gene.
DR neXtProt; NX_Q9NZU7; -.
DR OpenTargets; ENSG00000157782; -.
DR PharmGKB; PA26000; -.
DR VEuPathDB; HostDB:ENSG00000157782; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00940000158555; -.
DR HOGENOM; CLU_061288_8_0_1; -.
DR InParanoid; Q9NZU7; -.
DR OMA; KKMCQEE; -.
DR OrthoDB; 1424914at2759; -.
DR PhylomeDB; Q9NZU7; -.
DR TreeFam; TF334804; -.
DR PathwayCommons; Q9NZU7; -.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR SignaLink; Q9NZU7; -.
DR BioGRID-ORCS; 9478; 10 hits in 1078 CRISPR screens.
DR ChiTaRS; CABP1; human.
DR EvolutionaryTrace; Q9NZU7; -.
DR GenomeRNAi; 9478; -.
DR Pharos; Q9NZU7; Tbio.
DR PRO; PR:Q9NZU7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NZU7; protein.
DR Bgee; ENSG00000157782; Expressed in right frontal lobe and 134 other tissues.
DR ExpressionAtlas; Q9NZU7; baseline and differential.
DR Genevisible; Q9NZU7; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0005246; F:calcium channel regulator activity; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc.
DR GO; GO:0008139; F:nuclear localization sequence binding; ISS:UniProtKB.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; ISS:UniProtKB.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR043582; CaBP1/2/4/5.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR45917; PTHR45917; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW Cytoskeleton; Golgi apparatus; Lipoprotein; Magnesium; Membrane;
KW Metal-binding; Myristate; Phosphoprotein; Reference proteome; Repeat;
KW Sensory transduction; Synapse; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..370
FT /note="Calcium-binding protein 1"
FT /id="PRO_0000073513"
FT DOMAIN 225..260
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 279..296
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 302..337
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 339..370
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 238
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19008222"
FT BINDING 240
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19008222"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19008222"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19008222"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 315
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142,
FT ECO:0000269|PubMed:19008222"
FT BINDING 317
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142,
FT ECO:0000269|PubMed:19008222"
FT BINDING 319
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142,
FT ECO:0000269|PubMed:19008222"
FT BINDING 321
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142,
FT ECO:0000269|PubMed:19008222"
FT BINDING 326
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142,
FT ECO:0000269|PubMed:19008222"
FT BINDING 352
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142,
FT ECO:0000269|PubMed:19008222"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19008222"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142,
FT ECO:0000269|PubMed:19008222"
FT BINDING 356
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142,
FT ECO:0000269|PubMed:19008222"
FT BINDING 357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19008222"
FT BINDING 358
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142,
FT ECO:0000269|PubMed:19008222"
FT BINDING 360
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19008222"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142,
FT ECO:0000269|PubMed:19008222"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14685260"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..300
FT /note="Missing (in isoform Calbrain)"
FT /evidence="ECO:0000303|PubMed:9920909"
FT /id="VSP_037936"
FT VAR_SEQ 1..203
FT /note="Missing (in isoform S-CaBP1)"
FT /evidence="ECO:0000303|PubMed:10625670"
FT /id="VSP_037937"
FT VAR_SEQ 1..143
FT /note="Missing (in isoform L-CaBP1)"
FT /evidence="ECO:0000303|PubMed:10625670"
FT /id="VSP_037938"
FT VAR_SEQ 144..218
FT /note="RPREALPAAASRPSPSSPLPPARGRDGEERGLSPALGLRGSLRARGRGDSVP
FT AAASEADPFLHRLRPMLSSAFGQ -> MGNCVKYPLRNLSRKMCQEEQTSYMVVQTSEE
FT GLAADAELPGPLLMLAQNCAVMHNLLGPACIFLRKGFAENRQP (in isoform L-
FT CaBP1)"
FT /evidence="ECO:0000303|PubMed:10625670"
FT /id="VSP_037939"
FT VAR_SEQ 204..218
FT /note="FLHRLRPMLSSAFGQ -> MGNCVKYPLRNLSRK (in isoform S-
FT CaBP1)"
FT /evidence="ECO:0000303|PubMed:10625670"
FT /id="VSP_037940"
FT MUTAGEN 238
FT /note="D->A: Loss of magnesium-binding. Loss of binding to
FT ITPRs; when associated with A-240; A-315; A-317; A-352 and
FT A-354."
FT /evidence="ECO:0000269|PubMed:12032348,
FT ECO:0000269|PubMed:19008222"
FT MUTAGEN 240
FT /note="D->A: Loss of magnesium-binding. Loss of binding to
FT ITPRs; when associated with A-238; A-315; A-317; A-352 and
FT A-354."
FT /evidence="ECO:0000269|PubMed:12032348,
FT ECO:0000269|PubMed:19008222"
FT MUTAGEN 242
FT /note="D->A: Loss of magnesium-binding."
FT /evidence="ECO:0000269|PubMed:19008222"
FT MUTAGEN 249
FT /note="D->A: No effect on magnesium-binding."
FT /evidence="ECO:0000269|PubMed:19008222"
FT MUTAGEN 315
FT /note="D->A: Loss of binding to ITPRs; when associated with
FT A-238; A-240; A-317; A-352 and A-354."
FT /evidence="ECO:0000269|PubMed:12032348"
FT MUTAGEN 317
FT /note="N->A: Loss of binding to ITPRs; when associated with
FT A-238; A-240; A-315; A-352 and A-354."
FT /evidence="ECO:0000269|PubMed:12032348"
FT MUTAGEN 323
FT /note="S->A: Loss of phosphorylation and loss of calcium
FT release by InsP(3)."
FT /evidence="ECO:0000269|PubMed:14685260"
FT MUTAGEN 352
FT /note="D->A: Loss of binding to ITPRs; when associated with
FT A-238; A-240; A-315; A-317 and A-354."
FT /evidence="ECO:0000269|PubMed:12032348"
FT MUTAGEN 354
FT /note="N->A: Loss of binding to ITPRs; when associated with
FT A-238; A-240; A-315; A-317 and A-352."
FT /evidence="ECO:0000269|PubMed:12032348"
FT CONFLICT 140
FT /note="Q -> R (in Ref. 4; AAH30201)"
FT /evidence="ECO:0000305"
FT HELIX 224..240
FT /evidence="ECO:0007829|PDB:3OX6"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:3OX6"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:3OX6"
FT HELIX 263..274
FT /evidence="ECO:0007829|PDB:3OX6"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:2K7B"
FT HELIX 283..294
FT /evidence="ECO:0007829|PDB:3OX6"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:3OX6"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:3OX6"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:3OX6"
FT HELIX 324..335
FT /evidence="ECO:0007829|PDB:3OX6"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:2K7C"
FT HELIX 341..351
FT /evidence="ECO:0007829|PDB:3OX6"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:3OX6"
FT HELIX 361..367
FT /evidence="ECO:0007829|PDB:3OX6"
FT INIT_MET Q9NZU7-1:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT LIPID Q9NZU7-1:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:10625670"
FT LIPID Q9NZU7-1:4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:10625670"
FT INIT_MET Q9NZU7-2:1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT LIPID Q9NZU7-2:2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:10625670"
FT LIPID Q9NZU7-2:4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:10625670"
SQ SEQUENCE 370 AA; 39838 MW; 3444721152E01AA7 CRC64;
MGGGDGAAFK RPGDGARLQR VLGLGSRREP RSLPAGGPAP RRTAPPPPGH ASAGPAAMSS
HIAKSESKTS LLKAAAAAAS GGSRAPRHGP ARDPGLPSRR LPGSCPATPQ SSGDPSSRRP
LCRPAPREEG ARGSQRVLPQ AHCRPREALP AAASRPSPSS PLPPARGRDG EERGLSPALG
LRGSLRARGR GDSVPAAASE ADPFLHRLRP MLSSAFGQDR SLRPEEIEEL REAFREFDKD
KDGYINCRDL GNCMRTMGYM PTEMELIELS QQINMNLGGH VDFDDFVELM GPKLLAETAD
MIGVKELRDA FREFDTNGDG EISTSELREA MRKLLGHQVG HRDIEEIIRD VDLNGDGRVD
FEEFVRMMSR
