HPCL1_HUMAN
ID HPCL1_HUMAN Reviewed; 193 AA.
AC P37235; Q969S5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Hippocalcin-like protein 1;
DE AltName: Full=Calcium-binding protein BDR-1;
DE AltName: Full=HLP2;
DE AltName: Full=Visinin-like protein 3;
DE Short=VILIP-3;
GN Name=HPCAL1; Synonyms=BDR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8038222; DOI=10.1016/0167-4889(94)90062-0;
RA Kobayashi M., Takamatsu K., Fujishiro M., Saitoh S., Noguchi T.;
RT "Molecular cloning of a novel calcium-binding protein structurally related
RT to hippocalcin from human brain and chromosomal mapping of its gene.";
RL Biochim. Biophys. Acta 1222:515-518(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Pancreas;
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].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [5]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
CC -!- FUNCTION: May be involved in the calcium-dependent regulation of
CC rhodopsin phosphorylation.
CC -!- INTERACTION:
CC P37235; A2BDD9: AMOT; NbExp=3; IntAct=EBI-749311, EBI-17286414;
CC P37235; P54253: ATXN1; NbExp=7; IntAct=EBI-749311, EBI-930964;
CC P37235; Q9H6X5-2: C19orf44; NbExp=4; IntAct=EBI-749311, EBI-12061599;
CC P37235; Q9BXJ5: C1QTNF2; NbExp=11; IntAct=EBI-749311, EBI-2817707;
CC P37235; P07451: CA3; NbExp=3; IntAct=EBI-749311, EBI-12208965;
CC P37235; Q8IYK4: COLGALT2; NbExp=4; IntAct=EBI-749311, EBI-10263496;
CC P37235; Q03060-25: CREM; NbExp=6; IntAct=EBI-749311, EBI-12884642;
CC P37235; Q86UW9: DTX2; NbExp=4; IntAct=EBI-749311, EBI-740376;
CC P37235; O95967: EFEMP2; NbExp=3; IntAct=EBI-749311, EBI-743414;
CC P37235; P54753: EPHB3; NbExp=3; IntAct=EBI-749311, EBI-968308;
CC P37235; O75084: FZD7; NbExp=3; IntAct=EBI-749311, EBI-746917;
CC P37235; Q9BWX5: GATA5; NbExp=3; IntAct=EBI-749311, EBI-12132270;
CC P37235; Q9NP66: HMG20A; NbExp=4; IntAct=EBI-749311, EBI-740641;
CC P37235; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-749311, EBI-11959885;
CC P37235; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-749311, EBI-11749135;
CC P37235; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-749311, EBI-10172150;
CC P37235; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-749311, EBI-10172290;
CC P37235; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-749311, EBI-10171774;
CC P37235; P60411: KRTAP10-9; NbExp=6; IntAct=EBI-749311, EBI-10172052;
CC P37235; Q9BYP8: KRTAP17-1; NbExp=3; IntAct=EBI-749311, EBI-11988175;
CC P37235; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-749311, EBI-10172511;
CC P37235; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-749311, EBI-3958099;
CC P37235; Q99732: LITAF; NbExp=4; IntAct=EBI-749311, EBI-725647;
CC P37235; Q99750: MDFI; NbExp=3; IntAct=EBI-749311, EBI-724076;
CC P37235; Q969H8: MYDGF; NbExp=4; IntAct=EBI-749311, EBI-718622;
CC P37235; P41271-2: NBL1; NbExp=3; IntAct=EBI-749311, EBI-12135485;
CC P37235; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-749311, EBI-945833;
CC P37235; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-749311, EBI-22310682;
CC P37235; Q9NWW9: PLAAT2; NbExp=3; IntAct=EBI-749311, EBI-12253270;
CC P37235; O75830: SERPINI2; NbExp=3; IntAct=EBI-749311, EBI-750144;
CC P37235; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-749311, EBI-5235340;
CC P37235; Q9NRR2: TPSG1; NbExp=3; IntAct=EBI-749311, EBI-17210651;
CC P37235; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-749311, EBI-11957238;
CC P37235; P54577: YARS1; NbExp=3; IntAct=EBI-749311, EBI-1048893;
CC P37235; Q8N720: ZNF655; NbExp=3; IntAct=EBI-749311, EBI-625509;
CC P37235; Q7DB77: tir; Xeno; NbExp=3; IntAct=EBI-749311, EBI-6480811;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: Probably binds two or three calcium ions. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; D16227; BAA03754.1; -; mRNA.
DR EMBL; BC009846; AAH09846.1; -; mRNA.
DR EMBL; BC017028; AAH17028.1; -; mRNA.
DR EMBL; BC017482; AAH17482.1; -; mRNA.
DR CCDS; CCDS1671.1; -.
DR PIR; S47565; S47565.
DR RefSeq; NP_001245286.1; NM_001258357.1.
DR RefSeq; NP_001245287.1; NM_001258358.1.
DR RefSeq; NP_001245288.1; NM_001258359.1.
DR RefSeq; NP_002140.2; NM_002149.3.
DR RefSeq; NP_602293.1; NM_134421.2.
DR RefSeq; XP_005246217.1; XM_005246160.1.
DR RefSeq; XP_005246218.1; XM_005246161.1.
DR RefSeq; XP_005246219.1; XM_005246162.1.
DR RefSeq; XP_005246220.1; XM_005246163.1.
DR RefSeq; XP_011508648.1; XM_011510346.2.
DR RefSeq; XP_011508649.1; XM_011510347.1.
DR RefSeq; XP_011508650.1; XM_011510348.1.
DR RefSeq; XP_016859439.1; XM_017003950.1.
DR RefSeq; XP_016859440.1; XM_017003951.1.
DR RefSeq; XP_016859441.1; XM_017003952.1.
DR RefSeq; XP_016859442.1; XM_017003953.1.
DR PDB; 5T7C; NMR; -; A=2-193.
DR PDBsum; 5T7C; -.
DR AlphaFoldDB; P37235; -.
DR SMR; P37235; -.
DR BioGRID; 109481; 90.
DR IntAct; P37235; 62.
DR MINT; P37235; -.
DR STRING; 9606.ENSP00000483786; -.
DR ChEMBL; CHEMBL4295755; -.
DR iPTMnet; P37235; -.
DR PhosphoSitePlus; P37235; -.
DR SwissPalm; P37235; -.
DR BioMuta; HPCAL1; -.
DR DMDM; 20455519; -.
DR EPD; P37235; -.
DR jPOST; P37235; -.
DR MassIVE; P37235; -.
DR PaxDb; P37235; -.
DR PeptideAtlas; P37235; -.
DR PRIDE; P37235; -.
DR ProteomicsDB; 55270; -.
DR Antibodypedia; 26673; 150 antibodies from 24 providers.
DR DNASU; 3241; -.
DR Ensembl; ENST00000307845.8; ENSP00000310749.3; ENSG00000115756.13.
DR Ensembl; ENST00000381765.7; ENSP00000371184.3; ENSG00000115756.13.
DR Ensembl; ENST00000613496.4; ENSP00000478231.1; ENSG00000115756.13.
DR Ensembl; ENST00000620771.4; ENSP00000483786.1; ENSG00000115756.13.
DR Ensembl; ENST00000622018.4; ENSP00000482993.1; ENSG00000115756.13.
DR GeneID; 3241; -.
DR KEGG; hsa:3241; -.
DR MANE-Select; ENST00000307845.8; ENSP00000310749.3; NM_002149.4; NP_002140.2.
DR CTD; 3241; -.
DR DisGeNET; 3241; -.
DR GeneCards; HPCAL1; -.
DR HGNC; HGNC:5145; HPCAL1.
DR HPA; ENSG00000115756; Tissue enhanced (brain).
DR MIM; 600207; gene.
DR neXtProt; NX_P37235; -.
DR OpenTargets; ENSG00000115756; -.
DR PharmGKB; PA29418; -.
DR VEuPathDB; HostDB:ENSG00000115756; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000154645; -.
DR HOGENOM; CLU_072366_1_0_1; -.
DR InParanoid; P37235; -.
DR OMA; LEIVQXK; -.
DR OrthoDB; 1369072at2759; -.
DR PhylomeDB; P37235; -.
DR TreeFam; TF300009; -.
DR PathwayCommons; P37235; -.
DR SignaLink; P37235; -.
DR BioGRID-ORCS; 3241; 52 hits in 1075 CRISPR screens.
DR ChiTaRS; HPCAL1; human.
DR GeneWiki; HPCAL1; -.
DR GenomeRNAi; 3241; -.
DR Pharos; P37235; Tbio.
DR PRO; PR:P37235; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P37235; protein.
DR Bgee; ENSG00000115756; Expressed in cerebellar vermis and 201 other tissues.
DR ExpressionAtlas; P37235; baseline and differential.
DR Genevisible; P37235; HS.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; TAS:ProtInc.
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 3D-structure; Calcium; Lipoprotein; Membrane; Metal-binding; Myristate;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805"
FT CHAIN 2..193
FT /note="Hippocalcin-like protein 1"
FT /id="PRO_0000073771"
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:0000269|PubMed:25255805"
FT CONFLICT 19
FT /note="N -> K (in Ref. 1; BAA03754)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="A -> G (in Ref. 1; BAA03754)"
FT /evidence="ECO:0000305"
FT CONFLICT 93..94
FT /note="SR -> RG (in Ref. 1; BAA03754)"
FT /evidence="ECO:0000305"
FT HELIX 10..14
FT /evidence="ECO:0007829|PDB:5T7C"
FT HELIX 25..35
FT /evidence="ECO:0007829|PDB:5T7C"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:5T7C"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:5T7C"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:5T7C"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:5T7C"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:5T7C"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:5T7C"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:5T7C"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:5T7C"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:5T7C"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:5T7C"
FT HELIX 176..182
FT /evidence="ECO:0007829|PDB:5T7C"
SQ 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
