MER1_EUPRA
ID MER1_EUPRA Reviewed; 75 AA.
AC P10774; Q27149;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Mating pheromone Er-1/Er-3;
DE AltName: Full=Euplomone R1/R3;
DE Flags: Precursor;
GN Name=MAT1;
GN and
GN Name=MAT3;
OS Euplotes raikovi.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Hypotrichia; Euplotida; Euplotidae; Euplotes.
OX NCBI_TaxID=5938;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2470086; DOI=10.1073/pnas.86.9.3016;
RA Miceli C., Laterza A., Melli M.;
RT "Isolation and structural characterization of cDNA clones encoding the
RT mating pheromone Er-1 secreted by the ciliate Euplotes raikovi.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:3016-3020(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=1542697; DOI=10.1073/pnas.89.5.1988;
RA Miceli C., La Terza A., Bradshaw R.A., Luporini P.;
RT "Identification and structural characterization of a cDNA clone encoding a
RT membrane-bound form of the polypeptide pheromone Er-1 in the ciliate
RT protozoan Euplotes raikovi.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1988-1992(1992).
RN [3]
RP PROTEIN SEQUENCE OF 36-75.
RX PubMed=3142868; DOI=10.1016/s0021-9258(19)81338-8;
RA Raffioni S., Luporini P., Chait B.T., Disper S.S., Bradshaw R.A.;
RT "Primary structure of the mating pheromone Er-1 of the ciliate Euplotes
RT raikovi.";
RL J. Biol. Chem. 263:18152-18159(1988).
RN [4]
RP PROTEIN SEQUENCE OF 36-75, AND MASS SPECTROMETRY.
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 [5]
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 [6]
RP CHARACTERIZATION.
RX PubMed=10749941; DOI=10.1091/mbc.11.4.1445;
RA Ortenzi C., Alimenti C., Vallesi A., Di Pretoro B., Terza A.L.,
RA Luporini P.;
RT "The autocrine mitogenic loop of the ciliate Euplotes raikovi: the
RT pheromone membrane-bound forms are the cell binding sites and potential
RT signaling receptors of soluble pheromones.";
RL Mol. Biol. Cell 11:1445-1455(2000).
RN [7]
RP STRUCTURE BY NMR.
RX PubMed=7833812; DOI=10.1002/pro.5560030918;
RA Mronga S., Luginbuhl P., Brown L.R., Ortenzi C., Luporini P.,
RA Bradshaw R.A., Wuethrich K.;
RT "The NMR solution structure of the pheromone Er-1 from the ciliated
RT protozoan Euplotes raikovi.";
RL Protein Sci. 3:1527-1536(1994).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS).
RX PubMed=7479748; DOI=10.1073/pnas.92.22.10172;
RA Weiss M.S., Anderson D.H., Raffioni S., Bradshaw R.A., Ortenzi C.,
RA Luporini P., Eisenberg D.;
RT "A cooperative model for receptor recognition and cell adhesion: evidence
RT from the molecular packing in the 1.6-A crystal structure of the pheromone
RT Er-1 from the ciliated protozoan Euplotes raikovi.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10172-10176(1995).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS).
RX PubMed=9344754; DOI=10.1006/jmbi.1997.1318;
RA Anderson D.H., Weiss M.S., Eisenberg D.;
RT "Charges, hydrogen bonds, and correlated motions in the 1-A resolution
RT refined structure of the mating pheromone Er-1 from Euplotes raikovi.";
RL J. Mol. Biol. 273:479-500(1997).
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. The membrane-bound form promotes inter-cellular
CC communication and adhesion for mating pair formation and may act as
CC binding site for the secreted form.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P10774-1; Sequence=Displayed;
CC Name=2; Synonyms=Er-1 mem;
CC IsoId=P10774-2; Sequence=VSP_011848;
CC -!- MASS SPECTROMETRY: Mass=4410.5; Method=Plasma desorption;
CC Evidence={ECO:0000269|PubMed:1549567};
CC -!- MISCELLANEOUS: [Isoform 1]: Secreted.
CC -!- MISCELLANEOUS: [Isoform 2]: Membrane bound. {ECO:0000305}.
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DR EMBL; J04141; AAA99212.1; -; mRNA.
DR EMBL; M86864; AAA29124.1; -; mRNA.
DR PIR; A38236; A38236.
DR PDB; 1ERC; NMR; -; A=36-75.
DR PDB; 2ERL; X-ray; 1.00 A; A=36-75.
DR PDB; 6E6O; X-ray; 0.70 A; A=36-75.
DR PDBsum; 1ERC; -.
DR PDBsum; 2ERL; -.
DR PDBsum; 6E6O; -.
DR AlphaFoldDB; P10774; -.
DR SMR; P10774; -.
DR EvolutionaryTrace; P10774; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; 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; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Membrane; Pheromone; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 20..35
FT /evidence="ECO:0000269|PubMed:1549567,
FT ECO:0000269|PubMed:3142868"
FT /id="PRO_0000008668"
FT PEPTIDE 36..75
FT /note="Mating pheromone Er-1/Er-3"
FT /evidence="ECO:0000269|PubMed:3142868"
FT /id="PRO_0000008669"
FT DISULFID 38..54
FT /evidence="ECO:0000269|PubMed:1304918"
FT DISULFID 45..71
FT /evidence="ECO:0000269|PubMed:1304918"
FT DISULFID 50..63
FT /evidence="ECO:0000269|PubMed:1304918"
FT VAR_SEQ 1
FT /note="M -> MGCTSDLCHMASVLSKYQSLFLYLCRSNNCVGPLNSINRFFSGTVHV
FT ISFSINFRM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1542697"
FT /id="VSP_011848"
FT CONFLICT 25
FT /note="R -> S (in Ref. 2; AAA29124)"
FT /evidence="ECO:0000305"
FT HELIX 37..44
FT /evidence="ECO:0007829|PDB:6E6O"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:6E6O"
FT HELIX 58..70
FT /evidence="ECO:0007829|PDB:6E6O"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6E6O"
SQ SEQUENCE 75 AA; 8282 MW; 71E2208A0111AE19 CRC64;
MNKLAILAII AMVLFSANAF RFQSRLRSNV EAKTGDACEQ AAIQCVESAC ESLCTEGEDR
TGCYMYIYSN CPPYV
