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   24-JAN-2024, entry version 198.
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; 98.
DR   IntAct; P37235; 63.
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; 9606-ENSP00000483786; -.
DR   PeptideAtlas; P37235; -.
DR   ProteomicsDB; 55270; -.
DR   Pumba; P37235; -.
DR   Antibodypedia; 26673; 166 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   AGR; HGNC:5145; -.
DR   CTD; 3241; -.
DR   DisGeNET; 3241; -.
DR   GeneCards; HPCAL1; -.
DR   HGNC; HGNC:5145; HPCAL1.
DR   HPA; ENSG00000115756; Tissue enriched (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; RQHTEFN; -.
DR   OrthoDB; 339700at2759; -.
DR   PhylomeDB; P37235; -.
DR   TreeFam; TF300009; -.
DR   PathwayCommons; P37235; -.
DR   SignaLink; P37235; -.
DR   BioGRID-ORCS; 3241; 52 hits in 1153 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 203 other cell types or tissues.
DR   ExpressionAtlas; P37235; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   CDD; cd00051; EFh; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 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; CALCIUM BINDING PROTEINS; 1.
DR   PANTHER; PTHR23055:SF79; HIPPOCALCIN-LIKE PROTEIN 1; 1.
DR   Pfam; PF13499; EF-hand_7; 2.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00054; EFh; 3.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS00018; EF_HAND_1; 3.
DR   PROSITE; PS50222; EF_HAND_2; 4.
DR   Genevisible; P37235; HS.
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
//