ID   LCN5_RAT                Reviewed;         188 AA.
AC   P06911;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 2.
DT   24-JAN-2024, entry version 166.
DE   RecName: Full=Epididymal-specific lipocalin-5;
DE   AltName: Full=Androgen-dependent epididymal 18.5 kDa protein;
DE   AltName: Full=Epididymal retinoic acid-binding protein;
DE            Short=E-RABP;
DE   AltName: Full=Epididymal secretory protein I;
DE            Short=ESP-I;
DE   Contains:
DE     RecName: Full=Epididymal-specific lipocalin-5, B form;
DE   Contains:
DE     RecName: Full=Epididymal-specific lipocalin-5, C form;
DE   Flags: Precursor;
GN   Name=Lcn5; Synonyms=Erabp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wistar; TISSUE=Epididymis;
RX   PubMed=2125511; DOI=10.1095/biolreprod43.3.497;
RA   Moore A., Hall L., Hamilton D.W.;
RT   "An 18-kDa androgen-regulated protein that modifies galactosyltransferase
RT   activity is synthesized by the rat caput epididymidis, but has no
RT   structural similarity to rat milk alphalactalbumin.";
RL   Biol. Reprod. 43:497-506(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=1731756; DOI=10.1042/bj2810203;
RA   Girotti M., Jones R., Emery D.C., Chia W., Hall L.;
RT   "Structure and expression of the rat epididymal secretory protein I gene.
RT   An androgen-regulated member of the lipocalin superfamily with a rare
RT   splice donor site.";
RL   Biochem. J. 281:203-210(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 5-188, AND PROTEIN SEQUENCE OF 23-40.
RX   PubMed=2420796; DOI=10.1016/s0021-9258(19)89198-6;
RA   Brooks D.E., Means A.R., Wright E.J., Singh S.P., Tiver K.K.;
RT   "Molecular cloning of the cDNA for two major androgen-dependent secretory
RT   proteins of 18.5 kilodaltons synthesized by the rat epididymis.";
RL   J. Biol. Chem. 261:4956-4961(1986).
RN   [4]
RP   PROTEIN SEQUENCE OF 20-47, AND CHARACTERIZATION.
RX   PubMed=2165489; DOI=10.1016/s0021-9258(19)38241-9;
RA   Newcomer M.E., Ong D.E.;
RT   "Purification and crystallization of a retinoic acid-binding protein from
RT   rat epididymis. Identity with the major androgen-dependent epididymal
RT   proteins.";
RL   J. Biol. Chem. 265:12876-12879(1990).
RN   [5]
RP   PROTEIN SEQUENCE OF 58-66, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   PubMed=8069623; DOI=10.1016/0969-2126(93)90004-z;
RA   Newcomer M.E.;
RT   "Structure of the epididymal retinoic acid binding protein at 2.1-A
RT   resolution.";
RL   Structure 1:7-18(1993).
CC   -!- FUNCTION: Associates with spermatozoa in the epididymal fluid but does
CC       not bind tightly to them. Binds both all-trans and 9-cis retinoic acid.
CC       May act as a retinoid carrier protein which is required for epididymal
CC       function and/or sperm maturation.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Synthesized in the proximal part
CC       of the epididymis and secreted into the epididymal fluid.
CC   -!- TISSUE SPECIFICITY: Synthesized exclusively in the proximal part (caput
CC       epididymidis) of the epididymis. It makes up a substantial part of the
CC       total protein in the epididymal luminal fluid and binds to the sperm
CC       membrane.
CC   -!- PTM: There are two similar, immunologically cross-reacting forms of
CC       this protein, designated B and C, which probably result from different
CC       processing of the amino end.
CC   -!- PTM: The N-terminus of form C is probably blocked.
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X59831; CAA42493.1; -; Genomic_DNA.
DR   EMBL; X59832; CAA42494.1; -; mRNA.
DR   EMBL; M12790; AAA41127.1; -; mRNA.
DR   PIR; A43801; SQRTAD.
DR   RefSeq; NP_077050.1; NM_024136.1.
DR   RefSeq; XP_008759802.1; XM_008761580.2.
DR   PDB; 1EPA; X-ray; 2.10 A; A/B=23-186.
DR   PDB; 1EPB; X-ray; 2.20 A; A/B=23-186.
DR   PDBsum; 1EPA; -.
DR   PDBsum; 1EPB; -.
DR   AlphaFoldDB; P06911; -.
DR   SMR; P06911; -.
DR   STRING; 10116.ENSRNOP00000058570; -.
DR   iPTMnet; P06911; -.
DR   PhosphoSitePlus; P06911; -.
DR   PaxDb; 10116-ENSRNOP00000058570; -.
DR   Ensembl; ENSRNOT00055000923; ENSRNOP00055000736; ENSRNOG00055000529.
DR   Ensembl; ENSRNOT00060052906; ENSRNOP00060043983; ENSRNOG00060030414.
DR   Ensembl; ENSRNOT00065045096; ENSRNOP00065036979; ENSRNOG00065026118.
DR   GeneID; 29552; -.
DR   KEGG; rno:29552; -.
DR   UCSC; RGD:69320; rat.
DR   AGR; RGD:69320; -.
DR   CTD; 13863; -.
DR   RGD; 69320; Lcn5.
DR   VEuPathDB; HostDB:ENSRNOG00000058597; -.
DR   eggNOG; ENOG502TDU9; Eukaryota.
DR   HOGENOM; CLU_1424476_0_0_1; -.
DR   InParanoid; P06911; -.
DR   OrthoDB; 4846014at2759; -.
DR   PhylomeDB; P06911; -.
DR   TreeFam; TF336103; -.
DR   EvolutionaryTrace; P06911; -.
DR   PRO; PR:P06911; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000058597; Expressed in cerebellum and 4 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; TAS:RGD.
DR   GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR   CDD; cd19421; lipocalin_5_8-like; 1.
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   PANTHER; PTHR11430:SF71; EPIDIDYMAL-SPECIFIC LIPOCALIN-5; 1.
DR   PANTHER; PTHR11430; LIPOCALIN; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR01254; PGNDSYNTHASE.
DR   SUPFAM; SSF50814; Lipocalins; 1.
DR   PROSITE; PS00213; LIPOCALIN; 1.
DR   Genevisible; P06911; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond;
KW   Reference proteome; Secreted; Signal; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:2165489"
FT   CHAIN           20..188
FT                   /note="Epididymal-specific lipocalin-5, C form"
FT                   /id="PRO_0000339294"
FT   CHAIN           23..188
FT                   /note="Epididymal-specific lipocalin-5, B form"
FT                   /id="PRO_0000017869"
FT   DISULFID        82..176
FT   HELIX           30..33
FT                   /evidence="ECO:0007829|PDB:1EPA"
FT   STRAND          35..44
FT                   /evidence="ECO:0007829|PDB:1EPA"
FT   STRAND          59..66
FT                   /evidence="ECO:0007829|PDB:1EPA"
FT   STRAND          69..78
FT                   /evidence="ECO:0007829|PDB:1EPA"
FT   STRAND          81..91
FT                   /evidence="ECO:0007829|PDB:1EPA"
FT   STRAND          97..102
FT                   /evidence="ECO:0007829|PDB:1EPA"
FT   STRAND          105..114
FT                   /evidence="ECO:0007829|PDB:1EPA"
FT   STRAND          116..128
FT                   /evidence="ECO:0007829|PDB:1EPA"
FT   STRAND          131..141
FT                   /evidence="ECO:0007829|PDB:1EPA"
FT   HELIX           147..159
FT                   /evidence="ECO:0007829|PDB:1EPA"
FT   HELIX           164..166
FT                   /evidence="ECO:0007829|PDB:1EPA"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:1EPA"
FT   HELIX           175..182
FT                   /evidence="ECO:0007829|PDB:1EPA"
SQ   SEQUENCE   188 AA;  20670 MW;  8248BBB4C2D95355 CRC64;
     MENIMPFALL GLCVGLAAGT EGAVVKDFDI SKFLGFWYEI AFASKMGTPG LAHKEEKMGA
     MVVELKENLL ALTTTYYSED HCVLEKVTAT EGDGPAKFQV TRLSGKKEVV VEATDYLTYA
     IIDITSLVAG AVHRTMKLYS RSLDDNGEAL YNFRKITSDH GFSETDLYIL KHDLTCVKVL
     QSAAESRP
//