HPCL1_MOUSE
ID HPCL1_MOUSE Reviewed; 193 AA.
AC P62748; P35333;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Hippocalcin-like protein 1;
DE AltName: Full=Neural visinin-like protein 3;
DE Short=NVL-3;
DE Short=NVP-3;
DE AltName: Full=Visinin-like protein 3;
DE Short=VILIP-3;
GN Name=Hpcal1;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RA Ritter B., Modregger J., Plomann M.;
RT "Interactions of the murine neural visinin-like protein 3 (mNVP-3).";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
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: May be involved in the calcium-dependent regulation of
CC rhodopsin phosphorylation.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P37235}; Lipid-
CC anchor {ECO:0000250|UniProtKB:P37235}.
CC -!- MISCELLANEOUS: Probably binds two or three calcium ions. {ECO:0000250}.
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; AF085192; AAC35552.1; -; mRNA.
DR EMBL; BC001997; AAH01997.1; -; mRNA.
DR CCDS; CCDS25830.1; -.
DR RefSeq; NP_057886.1; NM_016677.4.
DR RefSeq; XP_006515219.1; XM_006515156.3.
DR RefSeq; XP_006515220.1; XM_006515157.2.
DR AlphaFoldDB; P62748; -.
DR SMR; P62748; -.
DR BioGRID; 207322; 9.
DR IntAct; P62748; 4.
DR MINT; P62748; -.
DR STRING; 10090.ENSMUSP00000071756; -.
DR iPTMnet; P62748; -.
DR PhosphoSitePlus; P62748; -.
DR SwissPalm; P62748; -.
DR EPD; P62748; -.
DR jPOST; P62748; -.
DR MaxQB; P62748; -.
DR PaxDb; P62748; -.
DR PeptideAtlas; P62748; -.
DR PRIDE; P62748; -.
DR ProteomicsDB; 273347; -.
DR Antibodypedia; 26673; 150 antibodies from 24 providers.
DR DNASU; 53602; -.
DR Ensembl; ENSMUST00000071858; ENSMUSP00000071756; ENSMUSG00000071379.
DR GeneID; 53602; -.
DR KEGG; mmu:53602; -.
DR UCSC; uc007ncw.1; mouse.
DR CTD; 3241; -.
DR MGI; MGI:1855689; Hpcal1.
DR VEuPathDB; HostDB:ENSMUSG00000071379; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000154645; -.
DR HOGENOM; CLU_072366_1_0_1; -.
DR InParanoid; P62748; -.
DR OMA; LEIVQXK; -.
DR OrthoDB; 1369072at2759; -.
DR PhylomeDB; P62748; -.
DR TreeFam; TF300009; -.
DR BioGRID-ORCS; 53602; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Hpcal1; mouse.
DR PRO; PR:P62748; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P62748; protein.
DR Bgee; ENSMUSG00000071379; Expressed in cerebellum lobe and 259 other tissues.
DR ExpressionAtlas; P62748; baseline and differential.
DR Genevisible; P62748; MM.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; 4.
PE 1: Evidence at protein level;
KW Calcium; Lipoprotein; Membrane; Metal-binding; Myristate;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P37235"
FT CHAIN 2..193
FT /note="Hippocalcin-like protein 1"
FT /id="PRO_0000073772"
FT DOMAIN 41..58
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
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:P37235"
SQ SEQUENCE 193 AA; 22338 MW; B7251445F834F91D CRC64;
MGKQNSKLRP EVLQDLREHT EFTDHELQEW YKGFLKDCPT GHLTVDEFKK IYANFFPYGD
ASKFAEHVFR TFDTNSDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISRSE
MLEIVQAIYK MVSSVMKMPE DESTPEKRTD KIFRQMDTNN DGKLSLEEFI KGAKSDPSIV
RLLQCDPSSA SQF