ID   PSC2_RAT                Reviewed;         112 AA.
AC   P02781;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Prostatic steroid-binding protein C2;
DE   AltName: Full=Prostatein peptide C2;
DE   Flags: Precursor;
GN   Name=Psbpc2;
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 [GENOMIC DNA].
RX   PubMed=2881277; DOI=10.1093/nar/15.4.1627;
RA   Delaey B., Dirckx L., Decourt J.-L., Claessens F., Peeters B., Rombauts W.;
RT   "Rat prostatic binding protein: the complete sequence of the C2 gene and
RT   its flanking regions.";
RL   Nucleic Acids Res. 15:1627-1641(1987).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-112, AND PYROGLUTAMATE FORMATION AT GLN-21.
RX   PubMed=6343081; DOI=10.1111/j.1432-1033.1983.tb07417.x;
RA   Peeters B., Heyns W., Mous J., Rombauts W.;
RT   "Structural studies on rat prostatic binding protein. The primary structure
RT   of component C2 from subunit S.";
RL   Eur. J. Biochem. 132:669-679(1983).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-100.
RX   PubMed=6896362; DOI=10.1038/298092a0;
RA   Parker M.G., Needham M., White R.;
RT   "Prostatic steroid binding protein: gene duplication and steroid binding.";
RL   Nature 298:92-94(1982).
CC   -!- FUNCTION: Part of prostatein which is the major secretory glycoprotein
CC       of ventral prostate gland.
CC   -!- SUBUNIT: Prostatein is composed of three different peptides called C1,
CC       C2 and C3. These form covalent C1:C3 (F) and C2:C3 (S) heterodimers
CC       whose noncovalent association forms tetrameric (C1:C3/C3:C2) prostatein
CC       molecules.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Linked by three disulfide bonds to C3.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:6343081}.
CC   -!- MISCELLANEOUS: The heterodimer can bind non-polar steroids, cholesterol
CC       and a group of small proline-rich peptides.
CC   -!- SIMILARITY: Belongs to the secretoglobin family. Lipophilin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; X05034; CAA28708.1; -; Genomic_DNA.
DR   EMBL; V01256; CAA24569.1; -; mRNA.
DR   EMBL; J00776; AAA51641.1; -; mRNA.
DR   PIR; A03251; BORT2.
DR   RefSeq; NP_997476.2; NM_207593.2.
DR   AlphaFoldDB; P02781; -.
DR   SMR; P02781; -.
DR   STRING; 10116.ENSRNOP00000027498; -.
DR   PaxDb; P02781; -.
DR   Ensembl; ENSRNOT00000027498; ENSRNOP00000027498; ENSRNOG00000020301.
DR   GeneID; 293731; -.
DR   KEGG; rno:293731; -.
DR   CTD; 404552; -.
DR   RGD; 1302961; Psbpc2.
DR   GeneTree; ENSGT00530000063866; -.
DR   HOGENOM; CLU_166234_0_0_1; -.
DR   InParanoid; P02781; -.
DR   OrthoDB; 1634878at2759; -.
DR   TreeFam; TF338526; -.
DR   PRO; PR:P02781; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Genevisible; P02781; RN.
DR   GO; GO:0005576; C:extracellular region; TAS:RGD.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005496; F:steroid binding; TAS:RGD.
DR   InterPro; IPR016126; Secretoglobin.
DR   InterPro; IPR035960; Secretoglobin_sf.
DR   Pfam; PF01099; Uteroglobin; 1.
DR   SUPFAM; SSF48201; SSF48201; 1.
DR   PROSITE; PS51311; SCGB; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Lipid-binding;
KW   Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal;
KW   Steroid-binding.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:6343081"
FT   CHAIN           21..112
FT                   /note="Prostatic steroid-binding protein C2"
FT                   /id="PRO_0000036376"
FT   MOD_RES         21
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000305|PubMed:6343081"
FT   DISULFID        28
FT                   /note="Interchain (with C3 chain)"
FT                   /evidence="ECO:0000305"
FT   DISULFID        69
FT                   /note="Interchain (with C3 chain)"
FT                   /evidence="ECO:0000305"
FT   DISULFID        92
FT                   /note="Interchain (with C3 chain)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26
FT                   /note="Missing (in Ref. 3; CAA24569/AAA51641)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        88
FT                   /note="I -> T (in Ref. 3; CAA24569/AAA51641)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        96..112
FT                   /note="VWLQINFPRGRWFSEIN -> YGYK (in Ref. 3; CAA24569)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   112 AA;  12828 MW;  DA65A6A82E677864 CRC64;
     MRLSLCLLTI LVVCCYEANG QTLAGQVCQA LQDVTITFLL NPEEELKREL EEFDAPPEAV
     EANLKVKRCI NKIMYGDRLS MGTSLVFIML KCDVKVWLQI NFPRGRWFSE IN