HPCA_BOVIN
ID HPCA_BOVIN Reviewed; 193 AA.
AC Q4PL64; Q148J5;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Neuron-specific calcium-binding protein hippocalcin {ECO:0000305};
GN Name=HPCA {ECO:0000250|UniProtKB:P84074};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Krishnan A., Duda T., Sharma R.K.;
RT "Partial purification of bovine hippocalcin and cloning.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; DQ070851; AAY82250.1; -; mRNA.
DR EMBL; BC118268; AAI18269.1; -; mRNA.
DR RefSeq; NP_001020499.1; NM_001025328.2.
DR RefSeq; XP_005202975.1; XM_005202918.2.
DR RefSeq; XP_005202976.1; XM_005202919.3.
DR RefSeq; XP_005202977.1; XM_005202920.3.
DR AlphaFoldDB; Q4PL64; -.
DR SMR; Q4PL64; -.
DR STRING; 9913.ENSBTAP00000010971; -.
DR PaxDb; Q4PL64; -.
DR PRIDE; Q4PL64; -.
DR Ensembl; ENSBTAT00000010971; ENSBTAP00000010971; ENSBTAG00000008336.
DR Ensembl; ENSBTAT00000068148; ENSBTAP00000058334; ENSBTAG00000008336.
DR GeneID; 509772; -.
DR KEGG; bta:509772; -.
DR CTD; 3208; -.
DR VEuPathDB; HostDB:ENSBTAG00000008336; -.
DR VGNC; VGNC:29936; HPCA.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000158110; -.
DR HOGENOM; CLU_072366_1_0_1; -.
DR InParanoid; Q4PL64; -.
DR OMA; HCCDLEL; -.
DR OrthoDB; 1369072at2759; -.
DR TreeFam; TF300009; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000008336; Expressed in Ammon's horn and 79 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; ISS:UniProtKB.
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 2: Evidence at transcript 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_0000073767"
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
