HPCA_HUMAN
ID HPCA_HUMAN Reviewed; 193 AA.
AC P84074; B2R9T3; D3DPQ7; P32076; P41211; P70510;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Neuron-specific calcium-binding protein hippocalcin {ECO:0000305};
DE AltName: Full=Calcium-binding protein BDR-2;
GN Name=HPCA {ECO:0000312|HGNC:HGNC:5144}; Synonyms=BDR2;
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], AND TISSUE SPECIFICITY.
RC TISSUE=Hippocampus;
RX PubMed=8166736; DOI=10.1006/bbrc.1994.1491;
RA Takamatsu K., Kobayashi M., Saitoh S., Fujishiro M., Noguchi T.;
RT "Molecular cloning of human hippocalcin cDNA and chromosomal mapping of its
RT gene.";
RL Biochem. Biophys. Res. Commun. 200:606-611(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9931466; DOI=10.1016/s0378-1119(98)00526-5;
RA Masaki T., Sakai E., Furuta Y., Kobayashi M., Takamatsu K.;
RT "Genomic structure and chromosomal mapping of the human and mouse
RT hippocalcin genes.";
RL Gene 225:117-124(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF WILD-TYPE AND VARIANTS DYT2
RP ASN-71 AND THR-190 IN COMPLEX WITH CALCIUM, FUNCTION, SUBUNIT, INTERACTION
RP WITH CACNA1A AND CACNA1B, SUBCELLULAR LOCATION, CHARACTERIZATION OF
RP VARIANTS DYT2 ASN-71 AND THR-190, AND DOMAIN.
RX PubMed=28398555; DOI=10.1093/hmg/ddx133;
RA Helassa N., Antonyuk S.V., Lian L.Y., Haynes L.P., Burgoyne R.D.;
RT "Biophysical and functional characterization of hippocalcin mutants
RT responsible for human dystonia.";
RL Hum. Mol. Genet. 26:2426-2435(2017).
RN [7]
RP INVOLVEMENT IN DYT2, AND VARIANTS DYT2 ASN-71; LYS-75 AND THR-190.
RX PubMed=25799108; DOI=10.1016/j.ajhg.2015.02.007;
RA Charlesworth G., Angelova P.R., Bartolome-Robledo F., Ryten M.,
RA Trabzuni D., Stamelou M., Abramov A.Y., Bhatia K.P., Wood N.W.;
RT "Mutations in HPCA cause autosomal-recessive primary isolated dystonia.";
RL Am. J. Hum. Genet. 96:657-665(2015).
CC -!- FUNCTION: Calcium-binding protein that may play a role in the
CC regulation of voltage-dependent calcium channels (PubMed:28398555). May
CC also play a role in cyclic-nucleotide-mediated signaling through the
CC regulation of adenylate and guanylate cyclases (By similarity).
CC {ECO:0000250|UniProtKB:P84076, ECO:0000269|PubMed:28398555}.
CC -!- SUBUNIT: Oligomer; oligomerization is calcium-dependent
CC (PubMed:28398555). May interact with the voltage-dependent P/Q- and N-
CC type calcium channels CACNA1A and CACNA1B (PubMed:28398555).
CC {ECO:0000269|PubMed:28398555}.
CC -!- INTERACTION:
CC P84074; Q9BXJ5: C1QTNF2; NbExp=6; IntAct=EBI-12197079, EBI-2817707;
CC P84074; P12532: CKMT1B; NbExp=3; IntAct=EBI-12197079, EBI-1050662;
CC P84074; Q03060-25: CREM; NbExp=6; IntAct=EBI-12197079, EBI-12884642;
CC P84074; Q86UW9: DTX2; NbExp=3; IntAct=EBI-12197079, EBI-740376;
CC P84074; Q9BWX5: GATA5; NbExp=3; IntAct=EBI-12197079, EBI-12132270;
CC P84074; Q9UBH0: IL36RN; NbExp=3; IntAct=EBI-12197079, EBI-465156;
CC P84074; P55197-2: MLLT10; NbExp=3; IntAct=EBI-12197079, EBI-12853322;
CC P84074; Q969H8: MYDGF; NbExp=6; IntAct=EBI-12197079, EBI-718622;
CC P84074; P0CG20: PRR35; NbExp=3; IntAct=EBI-12197079, EBI-11986293;
CC P84074; O15427: SLC16A3; NbExp=5; IntAct=EBI-12197079, EBI-7600166;
CC P84074; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-12197079, EBI-11139477;
CC P84074; P14927: UQCRB; NbExp=3; IntAct=EBI-12197079, EBI-743128;
CC P84074; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-12197079, EBI-11957238;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P84076,
CC ECO:0000269|PubMed:28398555}. 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 (PubMed:28398555).
CC {ECO:0000250|UniProtKB:P84076, ECO:0000269|PubMed:28398555}.
CC -!- TISSUE SPECIFICITY: Brain specific. {ECO:0000269|PubMed:8166736}.
CC -!- DOMAIN: Binds 3 calcium via EF-hand domains. The cryptic EF-hand 1 does
CC not bind calcium. {ECO:0000269|PubMed:28398555}.
CC -!- PTM: Myristoylation facilitates association with membranes.
CC {ECO:0000250|UniProtKB:P84076}.
CC -!- DISEASE: Dystonia 2, torsion, autosomal recessive (DYT2) [MIM:224500]:
CC A form of torsion dystonia, a disease defined by the presence of
CC sustained involuntary muscle contractions, often leading to abnormal
CC postures. 'Torsion' refers to the twisting nature of body movements,
CC often affecting the trunk. DYT2 is a slowly progressive form that first
CC affects distal limbs and later involves the neck, orofacial, and
CC craniocervical regions. {ECO:0000269|PubMed:25799108,
CC ECO:0000269|PubMed:28398555}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; D16593; BAA04019.1; -; mRNA.
DR EMBL; AB015202; BAA74456.1; -; Genomic_DNA.
DR EMBL; AK313907; BAG36630.1; -; mRNA.
DR EMBL; CH471059; EAX07495.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07496.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07498.1; -; Genomic_DNA.
DR EMBL; BC001777; AAH01777.1; -; mRNA.
DR CCDS; CCDS370.1; -.
DR PIR; JC2186; JC2186.
DR RefSeq; NP_002134.2; NM_002143.2.
DR RefSeq; XP_005270849.1; XM_005270792.2.
DR RefSeq; XP_016856607.1; XM_017001118.1.
DR PDB; 5G4P; X-ray; 2.42 A; A/E=1-193.
DR PDB; 5G58; X-ray; 2.54 A; A/E=1-193.
DR PDB; 5M6C; X-ray; 3.00 A; A/E=1-193.
DR PDBsum; 5G4P; -.
DR PDBsum; 5G58; -.
DR PDBsum; 5M6C; -.
DR AlphaFoldDB; P84074; -.
DR SMR; P84074; -.
DR BioGRID; 109448; 38.
DR IntAct; P84074; 18.
DR STRING; 9606.ENSP00000362566; -.
DR TCDB; 8.A.82.2.8; the calmodulin calcium binding protein (calmodulin) family.
DR GlyGen; P84074; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P84074; -.
DR PhosphoSitePlus; P84074; -.
DR SwissPalm; P84074; -.
DR BioMuta; HPCA; -.
DR DMDM; 51317406; -.
DR EPD; P84074; -.
DR jPOST; P84074; -.
DR MassIVE; P84074; -.
DR MaxQB; P84074; -.
DR PaxDb; P84074; -.
DR PeptideAtlas; P84074; -.
DR PRIDE; P84074; -.
DR ProteomicsDB; 57746; -.
DR Antibodypedia; 31374; 98 antibodies from 21 providers.
DR DNASU; 3208; -.
DR Ensembl; ENST00000373467.4; ENSP00000362566.3; ENSG00000121905.10.
DR GeneID; 3208; -.
DR KEGG; hsa:3208; -.
DR MANE-Select; ENST00000373467.4; ENSP00000362566.3; NM_002143.3; NP_002134.2.
DR UCSC; uc001bwh.4; human.
DR CTD; 3208; -.
DR DisGeNET; 3208; -.
DR GeneCards; HPCA; -.
DR HGNC; HGNC:5144; HPCA.
DR HPA; ENSG00000121905; Tissue enriched (brain).
DR MalaCards; HPCA; -.
DR MIM; 142622; gene.
DR MIM; 224500; phenotype.
DR neXtProt; NX_P84074; -.
DR OpenTargets; ENSG00000121905; -.
DR Orphanet; 99657; Primary dystonia, DYT2 type.
DR PharmGKB; PA29417; -.
DR VEuPathDB; HostDB:ENSG00000121905; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000158110; -.
DR HOGENOM; CLU_072366_1_0_1; -.
DR InParanoid; P84074; -.
DR OMA; HCCDLEL; -.
DR OrthoDB; 1369072at2759; -.
DR PhylomeDB; P84074; -.
DR TreeFam; TF300009; -.
DR PathwayCommons; P84074; -.
DR SignaLink; P84074; -.
DR BioGRID-ORCS; 3208; 14 hits in 1067 CRISPR screens.
DR ChiTaRS; HPCA; human.
DR GeneWiki; Hippocalcin; -.
DR GenomeRNAi; 3208; -.
DR Pharos; P84074; Tbio.
DR PRO; PR:P84074; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P84074; protein.
DR Bgee; ENSG00000121905; Expressed in caudate nucleus and 148 other tissues.
DR Genevisible; P84074; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:Ensembl.
DR GO; GO:0032590; C:dendrite membrane; IEA:Ensembl.
DR GO; GO:0044327; C:dendritic spine head; IEA:Ensembl.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0032809; C:neuronal cell body membrane; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IEA:Ensembl.
DR GO; GO:0031584; P:activation of phospholipase D activity; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0071277; P:cellular response to calcium ion; IMP:UniProtKB.
DR GO; GO:0071257; P:cellular response to electrical stimulus; IEA:Ensembl.
DR GO; GO:1904009; P:cellular response to monosodium glutamate; IEA:Ensembl.
DR GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR GO; GO:0031283; P:negative regulation of guanylate cyclase activity; IEA:Ensembl.
DR GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IEA:Ensembl.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IEA:Ensembl.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IEA:Ensembl.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IMP:UniProtKB.
DR GO; GO:1904010; P:response to Aroclor 1254; IEA:Ensembl.
DR GO; GO:1901986; P:response to ketamine; IEA:Ensembl.
DR GO; GO:1902065; P:response to L-glutamate; IEA:Ensembl.
DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Cytoplasm; Disease variant; Dystonia; Lipoprotein;
KW Membrane; Metal-binding; Myristate; 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_0000073768"
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 ECO:0000269|PubMed:28398555, ECO:0007744|PDB:5G4P,
FT ECO:0007744|PDB:5G58, ECO:0007744|PDB:5M6C"
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 ECO:0000269|PubMed:28398555, ECO:0007744|PDB:5G4P,
FT ECO:0007744|PDB:5G58, ECO:0007744|PDB:5M6C"
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 ECO:0000269|PubMed:28398555, ECO:0007744|PDB:5G4P,
FT ECO:0007744|PDB:5G58, ECO:0007744|PDB:5M6C"
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 ECO:0000269|PubMed:28398555, ECO:0007744|PDB:5G4P,
FT ECO:0007744|PDB:5G58, ECO:0007744|PDB:5M6C"
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 ECO:0000269|PubMed:28398555, ECO:0007744|PDB:5G4P,
FT ECO:0007744|PDB:5G58, ECO:0007744|PDB:5M6C"
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 ECO:0000269|PubMed:28398555, ECO:0007744|PDB:5G4P,
FT ECO:0007744|PDB:5G58, ECO:0007744|PDB:5M6C"
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 ECO:0000269|PubMed:28398555, ECO:0007744|PDB:5G4P,
FT ECO:0007744|PDB:5G58, ECO:0007744|PDB:5M6C"
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 ECO:0000269|PubMed:28398555, ECO:0007744|PDB:5G4P,
FT ECO:0007744|PDB:5G58, ECO:0007744|PDB:5M6C"
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 ECO:0000269|PubMed:28398555, ECO:0007744|PDB:5G4P,
FT ECO:0007744|PDB:5G58, ECO:0007744|PDB:5M6C"
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 ECO:0000269|PubMed:28398555, ECO:0007744|PDB:5G4P,
FT ECO:0007744|PDB:5G58, ECO:0007744|PDB:5M6C"
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 ECO:0000269|PubMed:28398555, ECO:0007744|PDB:5G4P,
FT ECO:0007744|PDB:5G58, ECO:0007744|PDB:5M6C"
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 ECO:0000269|PubMed:28398555, ECO:0007744|PDB:5G4P,
FT ECO:0007744|PDB:5G58, ECO:0007744|PDB:5M6C"
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 ECO:0000269|PubMed:28398555, ECO:0007744|PDB:5G4P,
FT ECO:0007744|PDB:5G58, ECO:0007744|PDB:5M6C"
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 ECO:0000269|PubMed:28398555, ECO:0007744|PDB:5G4P,
FT ECO:0007744|PDB:5G58, ECO:0007744|PDB:5M6C"
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 ECO:0000269|PubMed:28398555, ECO:0007744|PDB:5G4P,
FT ECO:0007744|PDB:5G58, ECO:0007744|PDB:5M6C"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P84076"
FT VARIANT 21
FT /note="E -> D (in dbSNP:rs11554958)"
FT /id="VAR_048662"
FT VARIANT 71
FT /note="T -> N (in DYT2; no effect on protein localization;
FT no effect on protein abundance; no effect on protein
FT stability; no effect on protein 3D structure; decreased
FT oligomerization; changed calcium-binding; effect on
FT cooperativity for calcium-binding; no effect on affinity
FT for calcium; no effect on interaction with voltage-
FT dependent calcium channels; dbSNP:rs775863165)"
FT /evidence="ECO:0000269|PubMed:25799108,
FT ECO:0000269|PubMed:28398555"
FT /id="VAR_073803"
FT VARIANT 75
FT /note="N -> K (in DYT2; dbSNP:rs786205675)"
FT /evidence="ECO:0000269|PubMed:25799108"
FT /id="VAR_073804"
FT VARIANT 190
FT /note="A -> T (in DYT2; no effect on protein localization;
FT no effect on protein abundance; no effect on protein
FT stability; no effect on protein 3D structure; decreased
FT oligomerization; no effect on calcium-binding; no effect on
FT affinity for calcium; increased interaction with voltage-
FT dependent calcium channels; dbSNP:rs550921485)"
FT /evidence="ECO:0000269|PubMed:25799108,
FT ECO:0000269|PubMed:28398555"
FT /id="VAR_073805"
FT CONFLICT 94
FT /note="R -> P (in Ref. 1; BAA04019)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="A -> R (in Ref. 1; BAA04019)"
FT /evidence="ECO:0000305"
FT HELIX 10..18
FT /evidence="ECO:0007829|PDB:5G4P"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:5G4P"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:5G4P"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:5G4P"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:5G4P"
FT HELIX 58..72
FT /evidence="ECO:0007829|PDB:5G4P"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:5G4P"
FT HELIX 82..94
FT /evidence="ECO:0007829|PDB:5G4P"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:5G4P"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:5G4P"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:5G4P"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:5G4P"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:5G4P"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:5G4P"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:5G4P"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:5G4P"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:5G4P"
FT HELIX 177..183
FT /evidence="ECO:0007829|PDB:5G4P"
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
