MER10_EUPRA
ID MER10_EUPRA Reviewed; 75 AA.
AC P12350;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 3.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Mating pheromone Er-10;
DE AltName: Full=Euplomone R10;
DE Flags: Precursor;
GN Name=MAT10;
OS Euplotes raikovi.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Hypotrichia; Euplotida; Euplotidae; Euplotes.
OX NCBI_TaxID=5938;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1AF(1)1N;
RX PubMed=1722455; DOI=10.1111/j.1432-1033.1991.tb16430.x;
RA Miceli C., la Terza A., Bradshaw R., Luporini P.;
RT "Structural characterization of mating pheromone precursors of the ciliate
RT protozoan Euplotes raikovi. High conservation of pre and pro regions versus
RT high variability of secreted regions.";
RL Eur. J. Biochem. 202:759-764(1991).
RN [2]
RP PROTEIN SEQUENCE OF 38-75.
RX PubMed=2504286; DOI=10.1021/bi00438a049;
RA Raffioni S., Luporini P., Bradshaw R.A.;
RT "Purification, characterization, and amino acid sequence of the mating
RT pheromone Er-10 of the ciliate Euplotes raikovi.";
RL Biochemistry 28:5250-5256(1989).
RN [3]
RP STRUCTURE BY NMR OF 38-75, AND DISULFIDE BONDS.
RX PubMed=8515452; DOI=10.1006/jmbi.1993.1327;
RA Brown L.R., Mronga S., Bradshaw R.A., Ortenzi C., Luporini P.,
RA Wuethrich K.;
RT "Nuclear magnetic resonance solution structure of the pheromone Er-10 from
RT the ciliated protozoan Euplotes raikovi.";
RL J. Mol. Biol. 231:800-816(1993).
CC -!- FUNCTION: Mating ciliate pheromones (or gamones) are diffusible
CC extracellular communication signals that distinguish different
CC intraspecific classes of cells commonly referred to as 'mating types'.
CC They prepare the latter for conjugation by changing their cell surface
CC properties.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR EMBL; X61173; CAA43481.1; -; Genomic_DNA.
DR EMBL; X60453; CAA42982.1; -; Genomic_DNA.
DR PIR; S17341; S17341.
DR PIR; S19695; S19695.
DR PDB; 1ERP; NMR; -; A=38-75.
DR PDBsum; 1ERP; -.
DR AlphaFoldDB; P12350; -.
DR SMR; P12350; -.
DR EvolutionaryTrace; P12350; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005186; F:pheromone activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.50.10; -; 1.
DR InterPro; IPR016058; Pheromone_Er1_protoz.
DR InterPro; IPR009064; Pheromone_protoz.
DR InterPro; IPR036245; Pheromone_protoz_sf.
DR Pfam; PF06360; E_raikovi_mat; 1.
DR SUPFAM; SSF47014; SSF47014; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Pheromone;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..37
FT /evidence="ECO:0000269|PubMed:2504286"
FT /id="PRO_0000008672"
FT PEPTIDE 38..75
FT /note="Mating pheromone Er-10"
FT /id="PRO_0000008673"
FT DISULFID 40..56
FT /evidence="ECO:0000269|PubMed:8515452"
FT DISULFID 47..74
FT /evidence="ECO:0000269|PubMed:8515452"
FT DISULFID 52..64
FT /evidence="ECO:0000269|PubMed:8515452"
FT CONFLICT 74
FT /note="C -> V (in Ref. 1; CAA43481/CAA42982)"
FT /evidence="ECO:0000305"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:1ERP"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:1ERP"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:1ERP"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1ERP"
SQ SEQUENCE 75 AA; 8391 MW; FE9DA0ED555D4E95 CRC64;
MNKLAILAII AMVLFSANAF RFQSRIRSNV EAKTETRDLC EQSALQCNEQ GCHNFCSPED
KPGCLGMVWN PELCP
