ID HPCA_MOUSE Reviewed; 193 AA. AC P84075; A2A7R4; P32076; P41211; P70510; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JAN-2024, entry version 151. DE RecName: Full=Neuron-specific calcium-binding protein hippocalcin {ECO:0000305}; GN Name=Hpca {ECO:0000312|MGI:MGI:1336200}; 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 [GENOMIC DNA]. RC STRAIN=129/SvJ; RX PubMed=9931466; DOI=10.1016/s0378-1119(98)00526-5; RA Masaki T., Sakai E., Furuta Y., Kobayashi M., Takamatsu K.; RT "Genomic structure and chromosomal mapping of the human and mouse RT hippocalcin genes."; RL Gene 225:117-124(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain; RX PubMed=11978849; DOI=10.1523/jneurosci.22-09-03730.2002; RA Fehr C., Shirley R.L., Belknap J.K., Crabbe J.C., Buck K.J.; RT "Congenic mapping of alcohol and pentobarbital withdrawal liability loci to RT a <1 centimorgan interval of murine chromosome 4: identification of Mpdz as RT a candidate gene."; RL J. Neurosci. 22:3730-3738(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Retina; 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 [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Calcium-binding protein that may play a role in the CC regulation of voltage-dependent calcium channels. May also play a role CC in cyclic-nucleotide-mediated signaling through the regulation of CC adenylate and guanylate cyclases. {ECO:0000250|UniProtKB:P84074, CC ECO:0000250|UniProtKB:P84076}. CC -!- SUBUNIT: Oligomer; oligomerization is calcium-dependent. May interact CC with the voltage-dependent P/Q- and N-type calcium channels CACNA1A and CC CACNA1B. {ECO:0000250|UniProtKB:P84074}. CC -!- INTERACTION: CC P84075; Q08460: Kcnma1; NbExp=3; IntAct=EBI-2128343, EBI-1633915; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P84074, CC ECO:0000250|UniProtKB:P84076}. Membrane {ECO:0000250|UniProtKB:P84076}; CC Peripheral membrane protein {ECO:0000250|UniProtKB:P84076}. CC Note=Association with membranes is calcium-dependent (By similarity). CC Enriched in the perinuclear region, probably at the trans Golgi network CC in response to calcium (By similarity). {ECO:0000250|UniProtKB:P84074, CC ECO:0000250|UniProtKB:P84076}. CC -!- DOMAIN: Binds 3 calcium via EF-hand domains. The cryptic EF-hand 1 does CC not bind calcium. {ECO:0000250|UniProtKB:P84074}. CC -!- PTM: Myristoylation facilitates association with membranes. CC {ECO:0000250|UniProtKB:P84076}. CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}. 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; AB015200; BAA74455.1; -; Genomic_DNA. DR EMBL; AF326551; AAL37397.1; -; mRNA. DR EMBL; AF326552; AAL37398.1; -; mRNA. DR EMBL; AK002992; BAB22502.1; -; mRNA. DR EMBL; AL606977; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC049607; AAH49607.1; -; mRNA. DR EMBL; BC058588; AAH58588.1; -; mRNA. DR CCDS; CCDS18682.1; -. DR RefSeq; NP_001123891.1; NM_001130419.2. DR RefSeq; NP_001273010.1; NM_001286081.1. DR RefSeq; NP_001273012.1; NM_001286083.1. DR RefSeq; NP_034601.1; NM_010471.4. DR RefSeq; XP_006502838.1; XM_006502775.3. DR RefSeq; XP_006502839.1; XM_006502776.3. DR RefSeq; XP_006502840.1; XM_006502777.1. DR RefSeq; XP_011238748.1; XM_011240446.2. DR AlphaFoldDB; P84075; -. DR SMR; P84075; -. DR BioGRID; 200404; 3. DR IntAct; P84075; 1. DR STRING; 10090.ENSMUSP00000112145; -. DR iPTMnet; P84075; -. DR PhosphoSitePlus; P84075; -. DR SwissPalm; P84075; -. DR jPOST; P84075; -. DR MaxQB; P84075; -. DR PaxDb; 10090-ENSMUSP00000112145; -. DR PeptideAtlas; P84075; -. DR ProteomicsDB; 273189; -. DR Pumba; P84075; -. DR Antibodypedia; 31374; 112 antibodies from 22 providers. DR DNASU; 15444; -. DR Ensembl; ENSMUST00000030572.10; ENSMUSP00000030572.4; ENSMUSG00000028785.14. DR Ensembl; ENSMUST00000095807.10; ENSMUSP00000093486.4; ENSMUSG00000028785.14. DR Ensembl; ENSMUST00000116442.9; ENSMUSP00000112143.3; ENSMUSG00000028785.14. DR Ensembl; ENSMUST00000116444.10; ENSMUSP00000112145.3; ENSMUSG00000028785.14. DR Ensembl; ENSMUST00000139450.8; ENSMUSP00000119178.3; ENSMUSG00000028785.14. DR Ensembl; ENSMUST00000164649.8; ENSMUSP00000129548.2; ENSMUSG00000028785.14. DR GeneID; 15444; -. DR KEGG; mmu:15444; -. DR UCSC; uc008uwb.3; mouse. DR AGR; MGI:1336200; -. DR CTD; 3208; -. DR MGI; MGI:1336200; Hpca. DR VEuPathDB; HostDB:ENSMUSG00000028785; -. DR eggNOG; KOG0044; Eukaryota. DR GeneTree; ENSGT00940000158110; -. DR InParanoid; P84075; -. DR OMA; GAVMKMP; -. DR OrthoDB; 339700at2759; -. DR PhylomeDB; P84075; -. DR TreeFam; TF300009; -. DR BioGRID-ORCS; 15444; 1 hit in 78 CRISPR screens. DR ChiTaRS; Hpca; mouse. DR PRO; PR:P84075; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; P84075; Protein. DR Bgee; ENSMUSG00000028785; Expressed in CA3 field of hippocampus and 114 other cell types or tissues. DR ExpressionAtlas; P84075; baseline and differential. DR GO; GO:0030424; C:axon; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0032839; C:dendrite cytoplasm; ISO:MGI. DR GO; GO:0032590; C:dendrite membrane; ISO:MGI. DR GO; GO:0044327; C:dendritic spine head; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0032809; C:neuronal cell body membrane; ISO:MGI. DR GO; GO:0043204; C:perikaryon; ISO:MGI. DR GO; GO:0098794; C:postsynapse; ISO:MGI. DR GO; GO:0003779; F:actin binding; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB. DR GO; GO:0019900; F:kinase binding; ISO:MGI. DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl. DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB. DR GO; GO:0071257; P:cellular response to electrical stimulus; IEA:Ensembl. DR GO; GO:1905232; P:cellular response to L-glutamate; ISO:MGI. DR GO; GO:0048839; P:inner ear development; IDA:MGI. DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISO:MGI. DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:MGI. DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; ISS:UniProtKB. DR GO; GO:1904010; P:response to Aroclor 1254; IEA:Ensembl. DR GO; GO:1901986; P:response to ketamine; IEA:Ensembl. DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl. DR CDD; cd00051; EFh; 2. DR Gene3D; 1.10.238.10; EF-hand; 1. 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; CALCIUM BINDING PROTEINS; 1. DR PANTHER; PTHR23055:SF57; NEURON-SPECIFIC CALCIUM-BINDING PROTEIN HIPPOCALCIN; 1. DR Pfam; PF00036; EF-hand_1; 1. DR Pfam; PF13499; EF-hand_7; 1. DR PRINTS; PR00450; RECOVERIN. DR SMART; SM00054; EFh; 3. DR SUPFAM; SSF47473; EF-hand; 1. DR PROSITE; PS00018; EF_HAND_1; 3. DR PROSITE; PS50222; EF_HAND_2; 3. DR Genevisible; P84075; MM. PE 1: Evidence at protein level; KW Calcium; Cytoplasm; Lipoprotein; Membrane; Metal-binding; Myristate; KW Reference proteome; Repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P84076" FT CHAIN 2..193 FT /note="Neuron-specific calcium-binding protein hippocalcin" FT /id="PRO_0000073769" 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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" 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|UniProtKB:P84076" SQ SEQUENCE 193 AA; 22427 MW; 3DBEA176AC945DB1 CRC64; MGKQNSKLRP EMLQDLRENT EFSELELQEW YKGFLKDCPT GILNVDEFKK IYANFFPYGD ASKFAEHVFR TFDTNSDGTI DFREFIIALS VTSRGRLEQK LMWAFSMYDL DGNGYISREE MLEIVQAIYK MVSSVMKMPE DESTPEKRTE KIFRQMDTNN DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA SQF //