MEN2_EUPNO
ID MEN2_EUPNO Reviewed; 60 AA.
AC P83235;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Mating pheromone En-2;
OS Euplotes nobilii (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC Hypotrichia; Euplotida; Euplotidae; Euplotes.
OX NCBI_TaxID=184062;
RN [1]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC STRAIN=AC-1;
RX PubMed=11943175; DOI=10.1016/s0014-5793(02)02393-1;
RA Alimenti C., Ortenzi C., Carratore V., Luporini P.;
RT "Structural characterization of a protein pheromone from a cold-adapted
RT (Antarctic) single-cell eukaryote, the ciliate Euplotes nobilii.";
RL FEBS Lett. 514:329-332(2002).
RN [2]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=19621350; DOI=10.1002/iub.228;
RA Alimenti C., Vallesi A., Pedrini B., Wuthrich K., Luporini P.;
RT "Molecular cold-adaptation: comparative analysis of two homologous families
RT of psychrophilic and mesophilic signal proteins of the protozoan ciliate,
RT Euplotes.";
RL IUBMB Life 61:838-845(2009).
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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11943175}.
CC -!- MASS SPECTROMETRY: Mass=6298.92; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11943175};
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DR PDB; 2NSW; NMR; -; A=1-60.
DR PDBsum; 2NSW; -.
DR AlphaFoldDB; P83235; -.
DR BMRB; P83235; -.
DR SMR; P83235; -.
DR EvolutionaryTrace; P83235; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005186; F:pheromone activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Pheromone;
KW Secreted.
FT CHAIN 1..60
FT /note="Mating pheromone En-2"
FT /id="PRO_0000186200"
FT DISULFID 11..39
FT /evidence="ECO:0000269|PubMed:19621350"
FT DISULFID 24..35
FT /evidence="ECO:0000269|PubMed:19621350"
FT DISULFID 31..57
FT /evidence="ECO:0000269|PubMed:19621350"
FT DISULFID 36..48
FT /evidence="ECO:0000269|PubMed:19621350"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:2NSW"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:2NSW"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:2NSW"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:2NSW"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:2NSW"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:2NSW"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:2NSW"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:2NSW"
SQ SEQUENCE 60 AA; 6304 MW; 6EDF181F712E29CD CRC64;
DIEDFYTSET CPYKNDSQLA WDTCSGGTGN CGTVCCGQCF SFPVSQSCAG MADSNDCPNA