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Hippocalcin-like protein 1 (Calcium-binding protein BDR-1) (HLP2) (Visinin-like protein 3) (VILIP-3)

 HPCL1_HUMAN             Reviewed;         193 AA.
P37235; Q969S5;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 164.
RecName: Full=Hippocalcin-like protein 1;
AltName: Full=Calcium-binding protein BDR-1;
AltName: Full=HLP2;
AltName: Full=Visinin-like protein 3;
Short=VILIP-3;
Name=HPCAL1; Synonyms=BDR1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8038222; DOI=10.1016/0167-4889(94)90062-0;
Kobayashi M., Takamatsu K., Fujishiro M., Saitoh S., Noguchi T.;
"Molecular cloning of a novel calcium-binding protein structurally
related to hippocalcin from human brain and chromosomal mapping of its
gene.";
Biochim. Biophys. Acta 1222:515-518(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[5]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U.,
Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
"Global profiling of co- and post-translationally N-myristoylated
proteomes in human cells.";
Nat. Commun. 5:4919-4919(2014).
-!- FUNCTION: May be involved in the calcium-dependent regulation of
rhodopsin phosphorylation.
-!- INTERACTION:
Q4VCS5-2:AMOT; NbExp=4; IntAct=EBI-749311, EBI-3891843;
Q9BXJ5:C1QTNF2; NbExp=9; IntAct=EBI-749311, EBI-2817707;
Q86UW9:DTX2; NbExp=5; IntAct=EBI-749311, EBI-740376;
Q9NP66:HMG20A; NbExp=4; IntAct=EBI-749311, EBI-740641;
P60370:KRTAP10-5; NbExp=3; IntAct=EBI-749311, EBI-10172150;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-749311, EBI-10172290;
P60410:KRTAP10-8; NbExp=5; IntAct=EBI-749311, EBI-10171774;
P60411:KRTAP10-9; NbExp=5; IntAct=EBI-749311, EBI-10172052;
Q9BYR5:KRTAP4-2; NbExp=3; IntAct=EBI-749311, EBI-10172511;
P26371:KRTAP5-9; NbExp=3; IntAct=EBI-749311, EBI-3958099;
Q7Z3S9:NOTCH2NL; NbExp=7; IntAct=EBI-749311, EBI-945833;
Q7DB77:tir (xeno); NbExp=3; IntAct=EBI-749311, EBI-6480811;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}.
-!- MISCELLANEOUS: Probably binds two or three calcium ions.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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EMBL; D16227; BAA03754.1; -; mRNA.
EMBL; BC009846; AAH09846.1; -; mRNA.
EMBL; BC017028; AAH17028.1; -; mRNA.
EMBL; BC017482; AAH17482.1; -; mRNA.
CCDS; CCDS1671.1; -.
PIR; S47565; S47565.
RefSeq; NP_001245286.1; NM_001258357.1.
RefSeq; NP_001245287.1; NM_001258358.1.
RefSeq; NP_001245288.1; NM_001258359.1.
RefSeq; NP_002140.2; NM_002149.3.
RefSeq; NP_602293.1; NM_134421.2.
RefSeq; XP_005246217.1; XM_005246160.1.
RefSeq; XP_005246218.1; XM_005246161.1.
RefSeq; XP_005246219.1; XM_005246162.1.
RefSeq; XP_005246220.1; XM_005246163.1.
RefSeq; XP_011508648.1; XM_011510346.2.
RefSeq; XP_011508649.1; XM_011510347.1.
RefSeq; XP_011508650.1; XM_011510348.1.
RefSeq; XP_016859439.1; XM_017003950.1.
RefSeq; XP_016859440.1; XM_017003951.1.
RefSeq; XP_016859441.1; XM_017003952.1.
RefSeq; XP_016859442.1; XM_017003953.1.
UniGene; Hs.580427; -.
UniGene; Hs.741268; -.
PDB; 5T7C; NMR; -; A=2-193.
PDBsum; 5T7C; -.
ProteinModelPortal; P37235; -.
SMR; P37235; -.
BioGrid; 109481; 33.
IntAct; P37235; 23.
STRING; 9606.ENSP00000310749; -.
iPTMnet; P37235; -.
PhosphoSitePlus; P37235; -.
SwissPalm; P37235; -.
BioMuta; HPCAL1; -.
DMDM; 20455519; -.
EPD; P37235; -.
PaxDb; P37235; -.
PeptideAtlas; P37235; -.
PRIDE; P37235; -.
DNASU; 3241; -.
Ensembl; ENST00000307845; ENSP00000310749; ENSG00000115756.
Ensembl; ENST00000381765; ENSP00000371184; ENSG00000115756.
Ensembl; ENST00000613496; ENSP00000478231; ENSG00000115756.
Ensembl; ENST00000620771; ENSP00000483786; ENSG00000115756.
Ensembl; ENST00000622018; ENSP00000482993; ENSG00000115756.
GeneID; 3241; -.
KEGG; hsa:3241; -.
CTD; 3241; -.
DisGeNET; 3241; -.
EuPathDB; HostDB:ENSG00000115756.12; -.
GeneCards; HPCAL1; -.
HGNC; HGNC:5145; HPCAL1.
HPA; HPA043245; -.
MIM; 600207; gene.
neXtProt; NX_P37235; -.
OpenTargets; ENSG00000115756; -.
PharmGKB; PA29418; -.
eggNOG; KOG0044; Eukaryota.
eggNOG; COG5126; LUCA.
GeneTree; ENSGT00760000118820; -.
HOGENOM; HOG000233019; -.
HOVERGEN; HBG108179; -.
InParanoid; P37235; -.
OMA; LEIVQXK; -.
OrthoDB; EOG091G11T4; -.
PhylomeDB; P37235; -.
TreeFam; TF300009; -.
ChiTaRS; HPCAL1; human.
GeneWiki; HPCAL1; -.
GenomeRNAi; 3241; -.
PRO; PR:P37235; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115756; -.
CleanEx; HS_HPCAL1; -.
ExpressionAtlas; P37235; baseline and differential.
Genevisible; P37235; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
CDD; cd00051; EFh; 2.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
Pfam; PF13499; EF-hand_7; 1.
Pfam; PF13833; EF-hand_8; 1.
SMART; SM00054; EFh; 3.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 3.
PROSITE; PS50222; EF_HAND_2; 4.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Lipoprotein; Membrane;
Metal-binding; Myristate; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:25255805}.
CHAIN 2 193 Hippocalcin-like protein 1.
/FTId=PRO_0000073771.
DOMAIN 23 58 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 60 95 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 96 131 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 144 179 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 73 84 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 109 120 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 157 168 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:25255805}.
CONFLICT 19 19 N -> K (in Ref. 1; BAA03754).
{ECO:0000305}.
CONFLICT 88 88 A -> G (in Ref. 1; BAA03754).
{ECO:0000305}.
CONFLICT 93 94 SR -> RG (in Ref. 1; BAA03754).
{ECO:0000305}.
HELIX 10 14 {ECO:0000244|PDB:5T7C}.
HELIX 25 35 {ECO:0000244|PDB:5T7C}.
STRAND 37 40 {ECO:0000244|PDB:5T7C}.
HELIX 46 54 {ECO:0000244|PDB:5T7C}.
HELIX 61 71 {ECO:0000244|PDB:5T7C}.
STRAND 75 77 {ECO:0000244|PDB:5T7C}.
HELIX 82 89 {ECO:0000244|PDB:5T7C}.
HELIX 97 105 {ECO:0000244|PDB:5T7C}.
STRAND 110 114 {ECO:0000244|PDB:5T7C}.
HELIX 118 132 {ECO:0000244|PDB:5T7C}.
HELIX 146 156 {ECO:0000244|PDB:5T7C}.
HELIX 167 174 {ECO:0000244|PDB:5T7C}.
HELIX 176 182 {ECO:0000244|PDB:5T7C}.
SEQUENCE 193 AA; 22313 MW; 87DCE938DCAD5E1F CRC64;
MGKQNSKLRP EVLQDLRENT EFTDHELQEW YKGFLKDCPT GHLTVDEFKK IYANFFPYGD
ASKFAEHVFR TFDTNGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISRSE
MLEIVQAIYK MVSSVMKMPE DESTPEKRTD KIFRQMDTNN DGKLSLEEFI RGAKSDPSIV
RLLQCDPSSA SQF


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