LCN5_RAT
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 03-AUG-2022, entry version 161.
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}.
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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; P06911; -.
DR GeneID; 29552; -.
DR KEGG; rno:29552; -.
DR UCSC; RGD:69320; rat.
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 OMA; MENIMPF; -.
DR OrthoDB; 1291941at2759; -.
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 tissues.
DR Genevisible; P06911; RN.
DR GO; GO:0005576; C:extracellular region; TAS:RGD.
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 PANTHER; PTHR11430; PTHR11430; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
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
