ID   ESP4_ZOOVI              Reviewed;         172 AA.
AC   P35578;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Epididymal secretory protein 4;
DE   AltName: Full=C731;
DE   AltName: Full=Epididymal secretory protein IV;
DE   AltName: Full=LESP IV;
DE   Flags: Precursor;
OS   Zootoca vivipara (Common lizard) (Lacerta vivipara).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC   Lacertibaenia; Lacertidae; Zootoca.
OX   NCBI_TaxID=8524;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-172, AND PROTEIN SEQUENCE OF 22-34.
RC   STRAIN=Jacquin; TISSUE=Epididymis;
RX   PubMed=1807785;
RA   Morel L., Depeiges A., Dufaure J.-P.;
RT   "Molecular cloning and characterization of a cDNA encoding for the mature
RT   form of a specific androgen dependent epididymal protein.";
RL   Cell. Mol. Biol. 37:757-764(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 22-34.
RC   STRAIN=Jacquin; TISSUE=Epididymis;
RX   PubMed=8486691; DOI=10.1016/s0021-9258(18)82200-1;
RA   Morel L., Dufaure J.-P., Depeiges A.;
RT   "LESP, an androgen-regulated lizard epididymal secretory protein family
RT   identified as a new member of the lipocalin superfamily.";
RL   J. Biol. Chem. 268:10274-10281(1993).
CC   -!- FUNCTION: Could transport small hydrophobic molecules into the
CC       epididymal fluid during the sperm maturation. Binds to the head region
CC       of spermatozoa and plays a key role in sperm maturation.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- TISSUE SPECIFICITY: Secreted by the epididymal epithelial cells.
CC   -!- DEVELOPMENTAL STAGE: Synthesized during the reproductive cycle.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
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DR   EMBL; X71356; CAA50491.1; -; mRNA.
DR   EMBL; X63151; CAA44854.1; -; mRNA.
DR   PIR; A46695; A46695.
DR   AlphaFoldDB; P35578; -.
DR   SMR; P35578; -.
DR   GO; GO:0005615; C:extracellular space; 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; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR   InterPro; IPR002972; PstgldnD_synth.
DR   PANTHER; PTHR11430; PTHR11430; 1.
DR   PANTHER; PTHR11430:SF86; PTHR11430:SF86; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   SUPFAM; SSF50814; SSF50814; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Secreted; Signal; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:1807785,
FT                   ECO:0000269|PubMed:8486691"
FT   CHAIN           22..172
FT                   /note="Epididymal secretory protein 4"
FT                   /id="PRO_0000017870"
FT   DISULFID        82..167
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   172 AA;  19463 MW;  F22D8D4CD2267EC0 CRC64;
     MIAVLLLVFG MTPDYIFPVS ADIPVVPNFD AQKTVGKWHP IGMASKLPEV PEYEQKISPM
     DHMVELTDGD MKLTANYMDG VCKEATAMLK HTDKPGVFKF TGGEIRMMDI DYEKYLIMYM
     KKSTFEAMYL SARGSDVGDD IKEKFKKLVL EQNFPEAHIK YFNAEQCTPT AA