HPCA_RAT
ID HPCA_RAT Reviewed; 193 AA.
AC P84076; 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 130.
DE RecName: Full=Neuron-specific calcium-binding protein hippocalcin {ECO:0000305};
DE AltName: Full=P23K {ECO:0000303|PubMed:1543495};
GN Name=Hpca {ECO:0000312|RGD:620060};
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], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=1280427; DOI=10.1016/0006-291x(92)91587-g;
RA Kobayashi M., Takamatsu K., Saitoh S., Miura M., Noguchi T.;
RT "Molecular cloning of hippocalcin, a novel calcium-binding protein of the
RT recoverin family exclusively expressed in hippocampus.";
RL Biochem. Biophys. Res. Commun. 189:511-517(1992).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=8240319; DOI=10.1006/bbrc.1993.2351;
RA Kobayashi M., Takamatsu K., Saitoh S., Miura M., Noguchi T.;
RT "Molecular cloning of hippocalcin, a novel calcium-binding protein of the
RT recoverin family exclusively expressed in hippocampus.";
RL Biochem. Biophys. Res. Commun. 196:1017-1017(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Olfactory epithelium;
RX PubMed=15336960; DOI=10.1016/j.bbrc.2004.07.123;
RA Mammen A., Simpson P.J., Nighorn A., Imanishi Y., Palczewski K.,
RA Ronnett G.V., Moon C.;
RT "Hippocalcin in the olfactory epithelium: a mediator of second messenger
RT signaling.";
RL Biochem. Biophys. Res. Commun. 322:1131-1139(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 PRELIMINARY PROTEIN SEQUENCE OF 51-63; 101-116 AND 138-145, SUBCELLULAR
RP LOCATION, TOPOLOGY, AND CALCIUM-BINDING.
RC TISSUE=Brain;
RX PubMed=1543495; DOI=10.1016/0006-291x(92)91635-4;
RA Takamatsu K., Kitamura K., Noguchi T.;
RT "Isolation and characterization of recoverin-like Ca(2+)-binding protein
RT from rat brain.";
RL Biochem. Biophys. Res. Commun. 183:245-251(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-37.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=8938744; DOI=10.1016/0306-4522(96)00344-2;
RA Grant A.L., Jones A., Thomas K.L., Wisden W.;
RT "Characterization of the rat hippocalcin gene: the 5' flanking region
RT directs expression to the hippocampus.";
RL Neuroscience 75:1099-1115(1996).
RN [7]
RP PROTEIN SEQUENCE OF 51-94; 138-148; 164-171 AND 175-181, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [8]
RP MYRISTOYLATION AT GLY-2, CALCIUM-BINDING, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RX PubMed=8360179; DOI=10.1016/s0021-9258(17)46711-1;
RA Kobayashi M., Takamatsu K., Saitoh S., Noguchi T.;
RT "Myristoylation of hippocalcin is linked to its calcium-dependent membrane
RT association properties.";
RL J. Biol. Chem. 268:18898-18904(1993).
CC -!- FUNCTION: Calcium-binding protein that may play a role in the
CC regulation of voltage-dependent calcium channels (By similarity). May
CC also play a role in cyclic-nucleotide-mediated signaling through the
CC regulation of adenylate and guanylate cyclases (PubMed:15336960).
CC {ECO:0000250|UniProtKB:P84074, ECO:0000269|PubMed:15336960}.
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 P84076; P14100: PDE1A; Xeno; NbExp=2; IntAct=EBI-908193, EBI-907809;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1543495}.
CC Membrane {ECO:0000269|PubMed:1543495, ECO:0000269|PubMed:8360179};
CC Peripheral membrane protein {ECO:0000269|PubMed:1543495,
CC ECO:0000269|PubMed:8360179}. Note=Association with membranes is
CC calcium-dependent (PubMed:8360179, PubMed:1543495). Enriched in the
CC perinuclear region, probably at the trans Golgi network in response to
CC calcium (By similarity). {ECO:0000250|UniProtKB:P84074,
CC ECO:0000269|PubMed:1543495, ECO:0000269|PubMed:8360179}.
CC -!- TISSUE SPECIFICITY: Neuron-specific in the hippocampus
CC (PubMed:1280427). Also detected in olfactory eptihelium
CC (PubMed:15336960). {ECO:0000269|PubMed:1280427,
CC ECO:0000269|PubMed:15336960}.
CC -!- DOMAIN: Binds 3 calcium via EF-hand domains. The cryptic EF-hand 1 does
CC not bind calcium. {ECO:0000269|PubMed:1543495,
CC ECO:0000269|PubMed:8360179}.
CC -!- PTM: Myristoylation facilitates association with membranes.
CC {ECO:0000269|PubMed:8360179}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; D12573; BAA02122.1; -; mRNA.
DR EMBL; AY442172; AAR14053.1; -; mRNA.
DR EMBL; BC087632; AAH87632.1; -; mRNA.
DR EMBL; X96993; CAA65718.1; -; Genomic_DNA.
DR PIR; JC1347; JC1347.
DR PIR; PS0344; PS0344.
DR RefSeq; NP_058818.1; NM_017122.1.
DR RefSeq; XP_006238982.1; XM_006238920.2.
DR RefSeq; XP_006238983.1; XM_006238921.3.
DR AlphaFoldDB; P84076; -.
DR SMR; P84076; -.
DR CORUM; P84076; -.
DR IntAct; P84076; 3.
DR STRING; 10116.ENSRNOP00000009153; -.
DR iPTMnet; P84076; -.
DR PhosphoSitePlus; P84076; -.
DR SwissPalm; P84076; -.
DR jPOST; P84076; -.
DR PaxDb; P84076; -.
DR PRIDE; P84076; -.
DR Ensembl; ENSRNOT00000009153; ENSRNOP00000009153; ENSRNOG00000006979.
DR GeneID; 29177; -.
DR KEGG; rno:29177; -.
DR CTD; 3208; -.
DR RGD; 620060; Hpca.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000158110; -.
DR HOGENOM; CLU_072366_1_0_1; -.
DR InParanoid; P84076; -.
DR OMA; HCCDLEL; -.
DR OrthoDB; 1369072at2759; -.
DR PhylomeDB; P84076; -.
DR TreeFam; TF300009; -.
DR PRO; PR:P84076; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000006979; Expressed in frontal cortex and 4 other tissues.
DR Genevisible; P84076; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; IDA:RGD.
DR GO; GO:0032590; C:dendrite membrane; IDA:RGD.
DR GO; GO:0044327; C:dendritic spine head; IDA:RGD.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:RGD.
DR GO; GO:0031584; P:activation of phospholipase D activity; IDA:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; IEP:RGD.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IEP:RGD.
DR GO; GO:1904009; P:cellular response to monosodium glutamate; IDA:RGD.
DR GO; GO:0048839; P:inner ear development; ISO:RGD.
DR GO; GO:0031283; P:negative regulation of guanylate cyclase activity; IDA:RGD.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IDA:RGD.
DR GO; GO:0010518; P:positive regulation of phospholipase activity; IDA:RGD.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IDA:RGD.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; ISS:UniProtKB.
DR GO; GO:1904010; P:response to Aroclor 1254; IEP:RGD.
DR GO; GO:1901986; P:response to ketamine; IEP:RGD.
DR GO; GO:1902065; P:response to L-glutamate; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; IEP:RGD.
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; Direct protein sequencing; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8360179"
FT CHAIN 2..193
FT /note="Neuron-specific calcium-binding protein hippocalcin"
FT /id="PRO_0000073770"
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:0000269|PubMed:8360179"
FT CONFLICT 60
FT /note="D -> G (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="M -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="N -> D (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 142..143
FT /note="ES -> TF (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
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
