ID   A0A0H5S397_BRUMA        Unreviewed;       347 AA.
AC   A0A0H5S397;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   29-MAY-2024, entry version 42.
DE   RecName: Full=Calcium uniporter protein {ECO:0000256|RuleBase:RU367035};
GN   Name=Bma-mcu-1 {ECO:0000313|EMBL:CRZ22680.1,
GN   ECO:0000313|WBParaSite:Bm4745a.1};
GN   ORFNames=BM_Bm4745 {ECO:0000313|EMBL:CRZ22680.1};
OS   Brugia malayi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=6279 {ECO:0000313|EMBL:CRZ22680.1};
RN   [1] {ECO:0000313|EMBL:CRZ22680.1, ECO:0000313|Proteomes:UP000006672}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FR3 {ECO:0000313|EMBL:CRZ22680.1,
RC   ECO:0000313|Proteomes:UP000006672};
RX   PubMed=17885136; DOI=10.1126/science.1145406;
RA   Ghedin E., Wang S., Spiro D., Caler E., Zhao Q., Crabtree J., Allen J.E.,
RA   Delcher A.L., Guiliano D.B., Miranda-Saavedra D., Angiuoli S.V., Creasy T.,
RA   Amedeo P., Haas B., El-Sayed N.M., Wortman J.R., Feldblyum T., Tallon L.,
RA   Schatz M., Shumway M., Koo H., Salzberg S.L., Schobel S., Pertea M.,
RA   Pop M., White O., Barton G.J., Carlow C.K., Crawford M.J., Daub J.,
RA   Dimmic M.W., Estes C.F., Foster J.M., Ganatra M., Gregory W.F.,
RA   Johnson N.M., Jin J., Komuniecki R., Korf I., Kumar S., Laney S., Li B.W.,
RA   Li W., Lindblom T.H., Lustigman S., Ma D., Maina C.V., Martin D.M.,
RA   McCarter J.P., McReynolds L., Mitreva M., Nutman T.B., Parkinson J.,
RA   Peregrin-Alvarez J.M., Poole C., Ren Q., Saunders L., Sluder A.E.,
RA   Smith K., Stanke M., Unnasch T.R., Ware J., Wei A.D., Weil G.,
RA   Williams D.J., Zhang Y., Williams S.A., Fraser-Liggett C., Slatko B.,
RA   Blaxter M.L., Scott A.L.;
RT   "Draft genome of the filarial nematode parasite Brugia malayi.";
RL   Science 317:1756-1760(2007).
RN   [2] {ECO:0000313|EMBL:CRZ22680.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FR3 {ECO:0000313|EMBL:CRZ22680.1};
RA   Gao Y.W., Fan S.T., Sun H.T., Wang Z., Gao X.L., Li Y.G., Wang T.C.,
RA   Zhang K., Xu W.W., Yu Z.J., Xia X.Z.;
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|WBParaSite:Bm4745a.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (DEC-2019) to UniProtKB.
CC   -!- FUNCTION: Mitochondrial inner membrane calcium uniporter that mediates
CC       calcium uptake into mitochondria. Constitutes a pore-forming and
CC       calcium-conducting subunit. Mitochondrial calcium homeostasis plays key
CC       roles in cellular physiology and regulates cell bioenergetics,
CC       cytoplasmic calcium signals and activation of cell death pathways.
CC       {ECO:0000256|RuleBase:RU367035}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC       inner membrane {ECO:0000256|ARBA:ARBA00004448,
CC       ECO:0000256|RuleBase:RU367035}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU367035}.
CC   -!- DOMAIN: Forms a well-packed pentamer with an overall cylindrical shape.
CC       The inner core of the pentamer is formed with the second transmembrane
CC       region and the second coiled-coil region: while the transmembrane
CC       regions pack into a five-helix bundle having a largely polar pore
CC       across the membrane, the coiled-coil outside the membrane forms a
CC       pentamer with a hydrophobic core. The inner core is wrapped by the
CC       first transmembrane region through contacts between the first and the
CC       second transmembrane regions. The second transmembrane is followed by
CC       the inner juxtamembrane region (IJMH) that orients at a wide angle
CC       relative to the second transmembrane. The two core domains are held
CC       together on the periphery by the outer juxtamembrane helix (OJMH).
CC       {ECO:0000256|RuleBase:RU367035}.
CC   -!- SIMILARITY: Belongs to the MCU (TC 1.A.77) family.
CC       {ECO:0000256|ARBA:ARBA00005653, ECO:0000256|RuleBase:RU367035}.
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DR   EMBL; LN856618; CRZ22680.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H5S397; -.
DR   STRING; 6279.A0A0H5S397; -.
DR   EnsemblMetazoa; Bm4745a.1; Bm4745a.1; WBGene00225006.
DR   WBParaSite; Bm4745a.1; Bm4745a.1; WBGene00225006.
DR   InParanoid; A0A0H5S397; -.
DR   OMA; DDIYVEY; -.
DR   OrthoDB; 469277at2759; -.
DR   Proteomes; UP000006672; Unassembled WGS sequence.
DR   GO; GO:1990246; C:uniplex complex; IEA:TreeGrafter.
DR   GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblMetazoa.
DR   GO; GO:0015292; F:uniporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0036444; P:calcium import into the mitochondrion; IEA:EnsemblMetazoa.
DR   GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IEA:UniProtKB-UniRule.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:EnsemblMetazoa.
DR   GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; IEA:EnsemblMetazoa.
DR   GO; GO:0061041; P:regulation of wound healing; IEA:EnsemblMetazoa.
DR   InterPro; IPR006769; MCU_C.
DR   InterPro; IPR039055; MCU_fam.
DR   PANTHER; PTHR13462; CALCIUM UNIPORTER PROTEIN, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13462:SF10; CALCIUM UNIPORTER PROTEIN, MITOCHONDRIAL; 1.
DR   Pfam; PF04678; MCU; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU367035};
KW   Calcium channel {ECO:0000256|RuleBase:RU367035};
KW   Calcium transport {ECO:0000256|RuleBase:RU367035};
KW   Ion channel {ECO:0000256|RuleBase:RU367035};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW   ECO:0000256|RuleBase:RU367035};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367035};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128,
KW   ECO:0000256|RuleBase:RU367035};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792,
KW   ECO:0000256|RuleBase:RU367035};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006672};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU367035};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU367035};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367035}.
FT   TRANSMEM        215..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367035"
FT   TRANSMEM        246..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU367035"
FT   DOMAIN          91..300
FT                   /note="Calcium uniporter protein C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04678"
SQ   SEQUENCE   347 AA;  40613 MW;  1BE8D3CF29BCA063 CRC64;
     MRCRWYSITG LLQQRQQHLQ IQLSTCYINL NNMHHLRRCS NDTTRGNLHI WCQSGLPLLE
     VPLPSRREIC QFTLKPISDT VSRFCKNIEC EDKGIEIVYV YSTSGNRIAG STLLKHLLLR
     GNFRLRINDF IYTVEVPSSK DVIANIMADG DVMQKFDGLR STIAPLYSIM NVEVYKAFQE
     RLLIEEYENV KAELKPLIQA KFKFDEFCRK RAQRILWLTL AAMGFQAGFL ARLTWWDYSW
     DVMEPITYFA THATLIASFA YYLYTNQYYN HNDHKKRAIS LYFHKKAAKS NFDISRFNEL
     QNVASSIKHD LKKLRDPLYQ HLPTARLASL LQESGKVQPR SFTKERS
//