MER2_EUPRA
ID MER2_EUPRA Reviewed; 75 AA.
AC P26886;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Mating pheromone Er-2/Er-9;
DE AltName: Full=Euplomone R2/R9;
DE Flags: Precursor;
GN Name=MAT2;
GN and
GN Name=MAT9;
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=1BF(1)13;
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 36-75.
RC STRAIN=13;
RX PubMed=1549567; DOI=10.1073/pnas.89.6.2071;
RA Raffioni S., Miceli C., Vallesi A., Chowdhury S.K., Chait B.T.,
RA Luporini P., Bradshaw R.A.;
RT "Primary structure of Euplotes raikovi pheromones: comparison of five
RT sequences of pheromones from cells with variable mating interactions.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2071-2075(1992).
RN [3]
RP DISULFIDE BONDS.
RX PubMed=1304918; DOI=10.1002/pro.5560010609;
RA Stewart A.E., Raffioni S., Chaudhary T., Chait B.T., Luporini P.,
RA Bradshaw R.A.;
RT "The disulfide bond pairing of the pheromones Er-1 and Er-2 of the ciliated
RT protozoan Euplotes raikovi.";
RL Protein Sci. 1:777-785(1992).
RN [4]
RP STRUCTURE BY NMR.
RX PubMed=7833811; DOI=10.1002/pro.5560030917;
RA Ottiger M., Szyperski T., Luginbuhl P., Ortenzi C., Luporini P.,
RA Bradshaw R.A., Wuethrich K.;
RT "The NMR solution structure of the pheromone Er-2 from the ciliated
RT protozoan Euplotes raikovi.";
RL Protein Sci. 3:1515-1526(1994).
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; X61174; CAA43482.1; -; Genomic_DNA.
DR PIR; S19696; S19696.
DR PDB; 1ERD; NMR; -; A=36-75.
DR PDBsum; 1ERD; -.
DR AlphaFoldDB; P26886; -.
DR SMR; P26886; -.
DR EvolutionaryTrace; P26886; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000772; F:mating pheromone activity; IEA:InterPro.
DR Gene3D; 1.10.10.190; -; 1.
DR InterPro; IPR016057; Pheromone_Er2/Er23_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..35
FT /evidence="ECO:0000269|PubMed:1549567"
FT /id="PRO_0000008670"
FT PEPTIDE 36..75
FT /note="Mating pheromone Er-2/Er-9"
FT /id="PRO_0000008671"
FT DISULFID 40..55
FT /evidence="ECO:0000269|PubMed:1304918"
FT DISULFID 47..72
FT /evidence="ECO:0000269|PubMed:1304918"
FT DISULFID 52..63
FT /evidence="ECO:0000269|PubMed:1304918"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:1ERD"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:1ERD"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:1ERD"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:1ERD"
SQ SEQUENCE 75 AA; 8194 MW; 894D5B6E46641D6F CRC64;
MNKLAILAII AMVLFSANAF RLQSRLRSNM EASARDPMTC EQAMASCEHT MCGYCQGPLY
MTCIGITTDP ECGLP
