CHP3_HUMAN
ID CHP3_HUMAN Reviewed; 214 AA.
AC Q96BS2; F5H1Y5; Q9NWT9;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Calcineurin B homologous protein 3;
DE AltName: Full=Tescalcin;
DE Short=TSC;
GN Name=TESC; Synonyms=CHP3;
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] (ISOFORM 1), INTERACTION WITH SLC9A1,
RP CALCIUM-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11696366; DOI=10.1016/s0014-5793(01)02986-6;
RA Mailaender J., Mueller-Esterl W., Dedio J.;
RT "Human homolog of mouse tescalcin associates with Na(+)/H(+) exchanger
RT type-1.";
RL FEBS Lett. 507:331-335(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Signet-ring cell carcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
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 (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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 INTERACTION WITH SLC9A1.
RX PubMed=12809501; DOI=10.1021/bi027143d;
RA Li X., Liu Y., Kay C.M., Muller-Esterl W., Fliegel L.;
RT "The Na+/H+ exchanger cytoplasmic tail: structure, function, and
RT interactions with tescalcin.";
RL Biochemistry 42:7448-7456(2003).
RN [7]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=14661968; DOI=10.1021/bi034870f;
RA Gutierrez-Ford C., Levay K., Gomes A.V., Perera E.M., Som T., Kim Y.M.,
RA Benovic J.L., Berkovitz G.D., Slepak V.Z.;
RT "Characterization of tescalcin, a novel EF-hand protein with a single Ca2+-
RT binding site: metal-binding properties, localization in tissues and cells,
RT and effect on calcineurin.";
RL Biochemistry 42:14553-14565(2003).
RN [8]
RP FUNCTION IN MEGAKARYOCYTIC DIFFERENTIATION, INDUCTION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=17717601; DOI=10.1172/jci27465;
RA Levay K., Slepak V.Z.;
RT "Tescalcin is an essential factor in megakaryocytic differentiation
RT associated with Ets family gene expression.";
RL J. Clin. Invest. 117:2672-2683(2007).
RN [9]
RP FUNCTION, INTERACTION WITH SLC9A1, AND SUBCELLULAR LOCATION.
RX PubMed=18321853; DOI=10.1074/jbc.m800267200;
RA Zaun H.C., Shrier A., Orlowski J.;
RT "Calcineurin B homologous protein 3 promotes the biosynthetic maturation,
RT cell surface stability, and optimal transport of the Na+/H+ exchanger NHE1
RT isoform.";
RL J. Biol. Chem. 283:12456-12467(2008).
RN [10]
RP FUNCTION IN GRANULOCYTIC DIFFERENTIATION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=20060826; DOI=10.1016/j.yexcr.2010.01.007;
RA Levay K., Slepak V.Z.;
RT "Up- or downregulation of tescalcin in HL-60 cells is associated with their
RT differentiation to either granulocytic or macrophage-like lineage.";
RL Exp. Cell Res. 316:1254-1262(2010).
RN [11]
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 [12]
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).
RN [13]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25807930; DOI=10.1002/anie.201500342;
RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
RA Tate E.W.;
RT "Multifunctional reagents for quantitative proteome-wide analysis of
RT protein modification in human cells and dynamic profiling of protein
RT lipidation during vertebrate development.";
RL Angew. Chem. Int. Ed. 54:5948-5951(2015).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP INTERACTION WITH SLC9A1.
RX PubMed=30287853; DOI=10.1038/s41598-018-33096-5;
RA Fuchs S., Hansen S.C., Markones M., Mymrikov E.V., Heerklotz H., Hunte C.;
RT "Calcineurin B homologous protein 3 binds with high affinity to the CHP
RT binding domain of the human sodium/proton exchanger NHE1.";
RL Sci. Rep. 8:14837-14837(2018).
CC -!- FUNCTION: Functions as an integral cofactor in cell pH regulation by
CC controlling plasma membrane-type Na(+)/H(+) exchange activity. Promotes
CC the maturation, transport, cell surface stability and exchange activity
CC of SLC9A1/NHE1 at the plasma membrane. Promotes the induction of
CC hematopoietic stem cell differentiation toward megakaryocytic lineage.
CC Essential for the coupling of ERK cascade activation with the
CC expression of ETS family genes in megakaryocytic differentiation. Also
CC involved in granulocytic differentiation in a ERK-dependent manner.
CC Inhibits the phosphatase activity of calcineurin.
CC {ECO:0000269|PubMed:17717601, ECO:0000269|PubMed:18321853,
CC ECO:0000269|PubMed:20060826}.
CC -!- SUBUNIT: Monomer (By similarity). Homodimer; disulfide-linked (By
CC similarity). Interacts with SLC9A1/NHE1; the interaction enables an
CC optimal Na(+)/H(+) exchange activity (PubMed:11696366, PubMed:18321853,
CC PubMed:30287853, PubMed:12809501). {ECO:0000250|UniProtKB:Q9JKL5,
CC ECO:0000269|PubMed:11696366, ECO:0000269|PubMed:12809501,
CC ECO:0000269|PubMed:18321853, ECO:0000269|PubMed:30287853}.
CC -!- INTERACTION:
CC Q96BS2; Q9NP66: HMG20A; NbExp=2; IntAct=EBI-740653, EBI-740641;
CC Q96BS2; P19634: SLC9A1; NbExp=4; IntAct=EBI-740653, EBI-743635;
CC Q96BS2; Q9Y2W2: WBP11; NbExp=3; IntAct=EBI-740653, EBI-714455;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18321853}. Cytoplasm
CC {ECO:0000269|PubMed:18321853}. Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:18321853}. Cell
CC projection, lamellipodium {ECO:0000269|PubMed:11696366}. Cell
CC projection, ruffle membrane {ECO:0000250|UniProtKB:Q9JKL5}.
CC Note=Colocalizes with SLC9A1 at the plasma membrane.
CC {ECO:0000269|PubMed:18321853}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96BS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96BS2-2; Sequence=VSP_035518, VSP_035519;
CC Name=3;
CC IsoId=Q96BS2-3; Sequence=VSP_045287;
CC -!- TISSUE SPECIFICITY: Expressed in mature megakaryocytes and
CC polymorphonuclear granulocytes (at protein level). Abundantly expressed
CC in heart. Also expressed at a lower level in adult testis and salivary
CC gland, and in the placenta. {ECO:0000269|PubMed:11696366,
CC ECO:0000269|PubMed:20060826}.
CC -!- DEVELOPMENTAL STAGE: Strongly up-regulated in K562 cells treated by PMA
CC to promote megakaryocytic differentiation, but not when treated by DMSO
CC to promote granulocytic differentiation or by hemin to promote
CC erythroid differentiation (at protein level).
CC {ECO:0000269|PubMed:17717601}.
CC -!- INDUCTION: Up-regulated during granulocytic differentiation in a ERK-
CC dependent manner (is mediated by activation of ERK) (at protein level).
CC Up-regulated during the differentiation and maturation of primary
CC megakaryocytes. Down-regulated during monocytic-macrophage
CC differentiation in a ERK-dependent manner.
CC {ECO:0000269|PubMed:17717601, ECO:0000269|PubMed:20060826}.
CC -!- DOMAIN: Binds calcium via its EF-hands. Calcium-binding mediates a
CC conformational change. Can also bind magnesium (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family. CHP
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: Although PubMed:12809501 reports that TESC results in a
CC decrease in transporter activity of human SLC9A1, studies with rat
CC SLC9A1 show that TESC-binding results in the maturation and
CC accumulation of SLC9A1 at the cell surface.
CC {ECO:0000305|PubMed:18321853}.
CC -!- CAUTION: The interacting region of SLC9A1/NHE1 with CHP3 is
CC conflicting: Interaction with SLC9A1/NHE1 has been reported via
CC residues 503-545, the juxtamembrane region of the cytoplasmic C-
CC terminus (PubMed:11696366, PubMed:18321853, PubMed:30287853). However,
CC another publication has reported interaction with SLC9A1/NHE1 via
CC residues 633-815, the region of the cytoplasmic C-terminus more distal
CC to the membrane (PubMed:12809501). {ECO:0000269|PubMed:11696366,
CC ECO:0000269|PubMed:12809501, ECO:0000269|PubMed:18321853,
CC ECO:0000269|PubMed:30287853}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91288.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW98101.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF443207; AAL35615.1; -; mRNA.
DR EMBL; AK000614; BAA91288.1; ALT_INIT; mRNA.
DR EMBL; AC026368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW98101.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC015221; AAH15221.1; -; mRNA.
DR EMBL; BQ949772; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS53835.1; -. [Q96BS2-3]
DR CCDS; CCDS9183.3; -. [Q96BS2-1]
DR RefSeq; NP_001161797.1; NM_001168325.1. [Q96BS2-3]
DR RefSeq; NP_060369.3; NM_017899.3. [Q96BS2-1]
DR RefSeq; XP_016875022.1; XM_017019533.1.
DR AlphaFoldDB; Q96BS2; -.
DR SMR; Q96BS2; -.
DR BioGRID; 120330; 9.
DR IntAct; Q96BS2; 20.
DR MINT; Q96BS2; -.
DR STRING; 9606.ENSP00000334785; -.
DR iPTMnet; Q96BS2; -.
DR PhosphoSitePlus; Q96BS2; -.
DR SwissPalm; Q96BS2; -.
DR BioMuta; TESC; -.
DR DMDM; 284018160; -.
DR EPD; Q96BS2; -.
DR jPOST; Q96BS2; -.
DR MassIVE; Q96BS2; -.
DR MaxQB; Q96BS2; -.
DR PaxDb; Q96BS2; -.
DR PeptideAtlas; Q96BS2; -.
DR PRIDE; Q96BS2; -.
DR ProteomicsDB; 25797; -.
DR ProteomicsDB; 76106; -. [Q96BS2-1]
DR ProteomicsDB; 76107; -. [Q96BS2-2]
DR Antibodypedia; 45432; 180 antibodies from 24 providers.
DR DNASU; 54997; -.
DR Ensembl; ENST00000335209.12; ENSP00000334785.7; ENSG00000088992.18. [Q96BS2-1]
DR Ensembl; ENST00000470612.5; ENSP00000432716.1; ENSG00000088992.18. [Q96BS2-2]
DR Ensembl; ENST00000541210.5; ENSP00000445689.1; ENSG00000088992.18. [Q96BS2-3]
DR GeneID; 54997; -.
DR KEGG; hsa:54997; -.
DR MANE-Select; ENST00000335209.12; ENSP00000334785.7; NM_017899.4; NP_060369.3.
DR UCSC; uc001twh.4; human. [Q96BS2-1]
DR CTD; 54997; -.
DR DisGeNET; 54997; -.
DR GeneCards; TESC; -.
DR HGNC; HGNC:26065; TESC.
DR HPA; ENSG00000088992; Tissue enhanced (salivary).
DR MIM; 611585; gene.
DR neXtProt; NX_Q96BS2; -.
DR OpenTargets; ENSG00000088992; -.
DR PharmGKB; PA143485630; -.
DR VEuPathDB; HostDB:ENSG00000088992; -.
DR eggNOG; KOG0034; Eukaryota.
DR GeneTree; ENSGT00940000155845; -.
DR HOGENOM; CLU_112076_0_0_1; -.
DR InParanoid; Q96BS2; -.
DR OMA; EIETRMH; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q96BS2; -.
DR TreeFam; TF354284; -.
DR PathwayCommons; Q96BS2; -.
DR SignaLink; Q96BS2; -.
DR BioGRID-ORCS; 54997; 8 hits in 1075 CRISPR screens.
DR ChiTaRS; TESC; human.
DR GenomeRNAi; 54997; -.
DR Pharos; Q96BS2; Tbio.
DR PRO; PR:Q96BS2; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96BS2; protein.
DR Bgee; ENSG00000088992; Expressed in parotid gland and 150 other tissues.
DR ExpressionAtlas; Q96BS2; baseline and differential.
DR Genevisible; Q96BS2; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0019212; F:phosphatase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0030219; P:megakaryocyte differentiation; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0030854; P:positive regulation of granulocyte differentiation; IDA:UniProtKB.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; IMP:UniProtKB.
DR GO; GO:0032417; P:positive regulation of sodium:proton antiporter activity; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0051604; P:protein maturation; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IMP:UniProtKB.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR SMART; SM00054; EFh; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Cell projection; Cytoplasm;
KW Differentiation; Disulfide bond; Lipoprotein; Membrane; Metal-binding;
KW Myristate; Nucleus; Protein kinase inhibitor; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:25807930"
FT CHAIN 2..214
FT /note="Calcineurin B homologous protein 3"
FT /id="PRO_0000073859"
FT DOMAIN 110..145
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:14661968,
FT ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:25807930"
FT VAR_SEQ 43..69
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045287"
FT VAR_SEQ 139..163
FT /note="VEELLSGNPHIEKESARSIADGAMM -> KWSRSCCRETLTSRRSPLAPSPT
FT GP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035518"
FT VAR_SEQ 164..214
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_035519"
FT CONFLICT 209..211
FT /note="TMA -> NMG (in Ref. 5; BQ949772)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 214 AA; 24750 MW; AB3DBE6EA3EB5E60 CRC64;
MGAAHSASEE VRELEGKTGF SSDQIEQLHR RFKQLSGDQP TIRKENFNNV PDLELNPIRS
KIVRAFFDNR NLRKGPSGLA DEINFEDFLT IMSYFRPIDT TMDEEQVELS RKEKLRFLFH
MYDSDSDGRI TLEEYRNVVE ELLSGNPHIE KESARSIADG AMMEAASVCM GQMEPDQVYE
GITFEDFLKI WQGIDIETKM HVRFLNMETM ALCH
