ID   APHR_CRICR              Reviewed;         167 AA.
AC   P09465;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 3.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Aphrodisin;
DE   Flags: Precursor;
OS   Cricetus cricetus (Black-bellied hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetus.
OX   NCBI_TaxID=10034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Vagina;
RX   PubMed=7892229; DOI=10.1073/pnas.92.6.2091;
RA   Maegert H.-J., Hadrys T., Cieslak A., Groeger A., Feller S.,
RA   Forssmann W.-G.;
RT   "cDNA sequence and expression pattern of the putative pheromone carrier
RT   aphrodisin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:2091-2095(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 17-167, DISULFIDE BONDS, PYROGLUTAMATE FORMATION AT
RP   GLN-17, AND GLYCOSYLATION AT ASN-57 AND ASN-85.
RX   PubMed=3182809; DOI=10.1016/s0021-9258(18)37444-1;
RA   Henzel W.J., Rodriguez H., Singer A.G., Stults J.T., Macrides F.,
RA   Agosta W.C., Niall H.;
RT   "The primary structure of aphrodisin.";
RL   J. Biol. Chem. 263:16682-16687(1988).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 17-167.
RX   PubMed=11152604; DOI=10.1006/jmbi.2000.4241;
RA   Vincent F., Lobel D., Brown K., Spinelli S., Grote P., Breer H.,
RA   Cambillau C., Tegoni M.;
RT   "Crystal structure of aphrodisin, a sex pheromone from female hamster.";
RL   J. Mol. Biol. 305:459-469(2001).
CC   -!- FUNCTION: Acts as an aphrodisiac pheromone, reliably eliciting
CC       copulatory behavior from male hamster.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed in the vagina, uterus, and Bartholin's
CC       glands of female hamsters. Secreted in vaginal discharge.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
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DR   EMBL; X65238; CAA46342.1; -; mRNA.
DR   PIR; I48075; I48075.
DR   PDB; 1E5P; X-ray; 1.63 A; A/B/C/D=17-167.
DR   PDBsum; 1E5P; -.
DR   AlphaFoldDB; P09465; -.
DR   SMR; P09465; -.
DR   iPTMnet; P09465; -.
DR   EvolutionaryTrace; P09465; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR   Gene3D; 2.40.128.20; -; 1.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR002345; Lipocalin.
DR   InterPro; IPR022272; Lipocalin_CS.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   InterPro; IPR002448; OBP-like.
DR   PANTHER; PTHR11430; PTHR11430; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR01173; ODORANTBNDNG.
DR   SUPFAM; SSF50814; SSF50814; 1.
DR   PROSITE; PS00213; LIPOCALIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Pyrrolidone carboxylic acid; Secreted; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000269|PubMed:3182809"
FT   CHAIN           17..167
FT                   /note="Aphrodisin"
FT                   /evidence="ECO:0000269|PubMed:3182809"
FT                   /id="PRO_0000017878"
FT   MOD_RES         17
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:3182809"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:3182809"
FT   CARBOHYD        85
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:3182809"
FT   DISULFID        54..58
FT                   /evidence="ECO:0000269|PubMed:3182809"
FT   DISULFID        73..165
FT                   /evidence="ECO:0000269|PubMed:3182809"
FT   HELIX           20..22
FT                   /evidence="ECO:0007829|PDB:1E5P"
FT   STRAND          27..35
FT                   /evidence="ECO:0007829|PDB:1E5P"
FT   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:1E5P"
FT   STRAND          48..55
FT                   /evidence="ECO:0007829|PDB:1E5P"
FT   TURN            56..59
FT                   /evidence="ECO:0007829|PDB:1E5P"
FT   STRAND          60..69
FT                   /evidence="ECO:0007829|PDB:1E5P"
FT   STRAND          72..83
FT                   /evidence="ECO:0007829|PDB:1E5P"
FT   STRAND          88..103
FT                   /evidence="ECO:0007829|PDB:1E5P"
FT   STRAND          105..115
FT                   /evidence="ECO:0007829|PDB:1E5P"
FT   STRAND          121..132
FT                   /evidence="ECO:0007829|PDB:1E5P"
FT   HELIX           136..148
FT                   /evidence="ECO:0007829|PDB:1E5P"
FT   HELIX           153..155
FT                   /evidence="ECO:0007829|PDB:1E5P"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:1E5P"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:1E5P"
SQ   SEQUENCE   167 AA;  18954 MW;  018CBAF4626EAC0D CRC64;
     MVKILLLALV FSLAHAQDFA ELQGKWYTIV IAADNLEKIE EGGPLRFYFR HIDCYKNCSE
     MEITFYVITN NQCSKTTVIG YLKGNGTYQT QFEGNNIFQP LYITSDKIFF TNKNMDRAGQ
     ETNMIVVAGK GNALTPEENE ILVQFAHEKK IPVENILNIL ATDTCPE