HPCA_MOUSE
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 03-AUG-2022, entry version 143.
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}.
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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; 2.
DR IntAct; P84075; 1.
DR STRING; 10090.ENSMUSP00000112145; -.
DR iPTMnet; P84075; -.
DR PhosphoSitePlus; P84075; -.
DR jPOST; P84075; -.
DR MaxQB; P84075; -.
DR PaxDb; P84075; -.
DR PeptideAtlas; P84075; -.
DR PRIDE; P84075; -.
DR ProteomicsDB; 273189; -.
DR Antibodypedia; 31374; 98 antibodies from 21 providers.
DR DNASU; 15444; -.
DR Ensembl; ENSMUST00000030572; ENSMUSP00000030572; ENSMUSG00000028785.
DR Ensembl; ENSMUST00000095807; ENSMUSP00000093486; ENSMUSG00000028785.
DR Ensembl; ENSMUST00000116442; ENSMUSP00000112143; ENSMUSG00000028785.
DR Ensembl; ENSMUST00000116444; ENSMUSP00000112145; ENSMUSG00000028785.
DR Ensembl; ENSMUST00000139450; ENSMUSP00000119178; ENSMUSG00000028785.
DR Ensembl; ENSMUST00000164649; ENSMUSP00000129548; ENSMUSG00000028785.
DR GeneID; 15444; -.
DR KEGG; mmu:15444; -.
DR UCSC; uc008uwb.3; mouse.
DR CTD; 3208; -.
DR MGI; MGI:1336200; Hpca.
DR VEuPathDB; HostDB:ENSMUSG00000028785; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000158110; -.
DR InParanoid; P84075; -.
DR OMA; HCCDLEL; -.
DR OrthoDB; 1369072at2759; -.
DR PhylomeDB; P84075; -.
DR TreeFam; TF300009; -.
DR BioGRID-ORCS; 15444; 1 hit in 73 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 111 other tissues.
DR ExpressionAtlas; P84075; baseline and differential.
DR Genevisible; P84075; MM.
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:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
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:0031584; P:activation of phospholipase D activity; ISO:MGI.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
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:1904009; P:cellular response to monosodium glutamate; ISO:MGI.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
DR GO; GO:0031283; P:negative regulation of guanylate cyclase activity; ISO:MGI.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; ISO:MGI.
DR GO; GO:0010518; P:positive regulation of phospholipase activity; ISO: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:1902065; P:response to L-glutamate; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
DR CDD; cd00051; EFh; 2.
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; PTHR23055; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
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
