FCA1_TRYCR
ID FCA1_TRYCR Reviewed; 211 AA.
AC P07749; Q26256; Q26915; Q27055; Q94786; Q94797;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Flagellar calcium-binding protein;
DE Short=FCABP;
DE AltName: Full=1F8 protein;
DE AltName: Full=24 kDa antigen;
DE AltName: Full=29 kDa flagella protein;
DE AltName: Full=ALC-1 antigen;
DE AltName: Full=F29;
DE AltName: Full=P24;
GN Name=FCABP;
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Y;
RX PubMed=2412209; DOI=10.1093/nar/13.16.5789;
RA Gonzalez A., Lerner T.J., Huecas M., Sosa-Pineda B., Nogueira N.,
RA Lizardi P.M.;
RT "Apparent generation of a segmented mRNA from two separate tandem gene
RT families in Trypanosoma cruzi.";
RL Nucleic Acids Res. 13:5789-5804(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE, AND CALCIUM-BINDING.
RX PubMed=2681200; DOI=10.1016/s0021-9258(18)51512-x;
RA Engman D.M., Krause K.-H., Blumin J.H., Kim K.S., Kirchhoff L.V.,
RA Donelson J.E.;
RT "A novel flagellar Ca2+-binding protein in trypanosomes.";
RL J. Biol. Chem. 264:18627-18631(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-23.
RC STRAIN=Y;
RX PubMed=1381253; DOI=10.1016/0248-4900(92)90119-l;
RA Ouaissi A., Aguirre T., Plumas-Marty B., Piras M., Schoneck R.,
RA Gras-Masse H., Taibi A., Loyens M., Tartar A., Capron A., Piras R.;
RT "Cloning and sequencing of a 24-kDa Trypanosoma cruzi specific antigen
RT released in association with membrane vesicles and defined by a monoclonal
RT antibody.";
RL Biol. Cell 75:11-17(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Miranda;
RX PubMed=8948328; DOI=10.1006/expr.1996.0127;
RA Porcel B.M., Bontempi E.J., Henriksson J., Rydaaker M., Aaslund L.,
RA Segura E.L., Pettersson U., Ruiz A.M.;
RT "Trypanosoma rangeli and Trypanosoma cruzi: molecular characterization of
RT genes encoding putative calcium-binding proteins, highly conserved in
RT trypanosomatids.";
RL Exp. Parasitol. 84:387-399(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=PBOL;
RX PubMed=7496390; DOI=10.1111/j.1550-7408.1995.tb01587.x;
RA Godsel L.M., Olson C.L., Lacava Z.G.M., Engman D.M.;
RT "Comparison of the 24 kDa flagellar calcium-binding protein cDNA of two
RT strains of Trypanosoma cruzi.";
RL J. Eukaryot. Microbiol. 42:320-322(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASN-23 AND PHE-152.
RC STRAIN=Y;
RA Tanaka M., Tanaka T., Mitsui Y., Yamamoto M., Wood J.N.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DM28C;
RA Maldonado R.A., Linss J., Thomaz N., Olson C.L., Engman D.M.,
RA Goldenberg S.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May contribute to the rapid motility of the trypanosomes,
CC playing a role either in flagellar structure or in calcium metabolism.
CC Could alternate between a GDP-bound inactive form to a calcium/GTP-
CC bound active form.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum.
CC -!- DOMAIN: This protein has four EF-hand domains, three of which may be
CC functional calcium-binding sites.
CC -!- SIMILARITY: Belongs to the calflagin family. {ECO:0000305}.
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DR EMBL; X02838; CAA26599.1; -; Genomic_DNA.
DR EMBL; S43664; AAB23113.2; -; mRNA.
DR EMBL; Z54193; CAA90898.1; -; Genomic_DNA.
DR EMBL; L26971; AAA99985.1; -; mRNA.
DR EMBL; D87512; BAA13411.1; -; mRNA.
DR EMBL; U70035; AAB08762.1; -; mRNA.
DR PIR; A34311; A34311.
DR PDB; 3CS1; X-ray; 2.00 A; A=1-211.
DR PDBsum; 3CS1; -.
DR AlphaFoldDB; P07749; -.
DR SMR; P07749; -.
DR VEuPathDB; TriTrypDB:BCY84_04509; -.
DR VEuPathDB; TriTrypDB:C3747_6g496; -.
DR VEuPathDB; TriTrypDB:C4B63_35g78; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_784; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0006360; -.
DR VEuPathDB; TriTrypDB:TcCL_ESM00363; -.
DR VEuPathDB; TriTrypDB:TcCLB.507491.151; -.
DR VEuPathDB; TriTrypDB:TcCLB.509391.30; -.
DR VEuPathDB; TriTrypDB:TCDM_08082; -.
DR VEuPathDB; TriTrypDB:TcG_08330; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_010035; -.
DR VEuPathDB; TriTrypDB:TcYC6_0054930; -.
DR EvolutionaryTrace; P07749; -.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 1.
DR DisProt; DP02940; -.
DR InterPro; IPR003299; Calflagin-bd.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR PRINTS; PR01362; CALFLAGIN.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell projection; Cilium; Flagellum; Metal-binding;
KW Repeat.
FT CHAIN 1..211
FT /note="Flagellar calcium-binding protein"
FT /id="PRO_0000073738"
FT DOMAIN 45..80
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..116
FT /note="EF-hand 2"
FT /evidence="ECO:0000305"
FT DOMAIN 127..162
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 164..199
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 144
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 183
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VARIANT 23
FT /note="K -> N (in strain: Miranda, PBOL and DM28C)"
FT /evidence="ECO:0000269|PubMed:1381253, ECO:0000269|Ref.6"
FT VARIANT 33
FT /note="R -> P (in strain: DM28C)"
FT VARIANT 71
FT /note="H -> Y (in strain: Miranda, PBOL and DM28C)"
FT VARIANT 79
FT /note="K -> R (in strain: DM28C)"
FT VARIANT 85
FT /note="P -> S (in strain: PBOL and DM28C)"
FT VARIANT 86
FT /note="R -> G (in strain: DM28C)"
FT VARIANT 98
FT /note="A -> S (in strain: PBOL)"
FT VARIANT 100
FT /note="A -> T (in strain: PBOL)"
FT VARIANT 100
FT /note="A -> V (in strain: Miranda)"
FT VARIANT 152
FT /note="L -> F (in strain: Miranda, DM28C and PBOL)"
FT /evidence="ECO:0000269|Ref.6"
FT VARIANT 210
FT /note="S -> K (in strain: Miranda)"
FT CONFLICT 3
FT /note="A -> G (in Ref. 6; BAA13411)"
FT /evidence="ECO:0000305"
FT HELIX 24..37
FT /evidence="ECO:0007829|PDB:3CS1"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:3CS1"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:3CS1"
FT HELIX 67..76
FT /evidence="ECO:0007829|PDB:3CS1"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:3CS1"
FT HELIX 87..106
FT /evidence="ECO:0007829|PDB:3CS1"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3CS1"
FT HELIX 116..137
FT /evidence="ECO:0007829|PDB:3CS1"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:3CS1"
FT HELIX 149..162
FT /evidence="ECO:0007829|PDB:3CS1"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:3CS1"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:3CS1"
FT HELIX 186..201
FT /evidence="ECO:0007829|PDB:3CS1"
SQ SEQUENCE 211 AA; 23736 MW; 74C3FDE8C820DF85 CRC64;
MGACGSKGST SDKGLASDKD GKKAKDRKEA WERIRQAIPR EKTAEAKQRR IELFKKFDKN
ETGKLCYDEV HSGCLEVLKL DEFTPRVRDI TKRAFDKARA LGSKLENKGS EDFVEFLEFR
LMLCYIYDFF ELTVMFDEID ASGNMLVDEE ELKRAVPKLE AWGAKVEDPA ALFKELDKNG
TGSVTFDEFA AWASAVKLDA DGDPDNVPES A
