PSC1_RAT
ID PSC1_RAT Reviewed; 111 AA.
AC P02782; P60808; Q499X0; Q63469;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Prostatic steroid-binding protein C1;
DE AltName: Full=Prostatein peptide C1;
DE Flags: Precursor;
GN Name=Psbpc1; Synonyms=Scgb1d2;
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].
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).
RN [2]
RP SEQUENCE REVISION.
RA Parker M.G.;
RL Submitted (JUL-1983) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6688048; DOI=10.1111/j.1432-1033.1983.tb07512.x;
RA Delaey B., Dirckx L., Peeters B., Volckaert G., Mous J., Heyns W.,
RA Rombauts W.;
RT "The nucleotide sequence of cDNA complementary to the C1 component of rat
RT prostatic binding protein.";
RL Eur. J. Biochem. 133:645-649(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kaushal V., Chatta G.S.;
RT "Sequence of C1 chain of mouse prostate steroid binding protein.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-111.
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-65.
RA Delaey B., Rombauts W., Volckaert G., Peeters B., Mous J., Heyns W.;
RT "Identification of a complementary-DNA clone containing part of the
RT sequence information for the C-1-polypeptide of rat prostatic binding
RT protein.";
RL Biochem. Soc. Trans. 10:51-51(1982).
RN [7]
RP PROTEIN SEQUENCE OF 24-111.
RX PubMed=7200013; DOI=10.1111/j.1432-1033.1982.tb06497.x;
RA Peeters B., Heyns W., Mous J., Rombauts W.;
RT "Structural studies on rat prostatic binding protein. The primary structure
RT of component C1 from subunit F.";
RL Eur. J. Biochem. 123:55-62(1982).
RN [8]
RP PROTEIN SEQUENCE OF 24-111.
RX PubMed=7198120; DOI=10.1016/s0021-9258(19)68334-1;
RA Liao S., Chen C., Huang I.-Y.;
RT "Prostate alpha-protein. Complete amino acid sequence of the component that
RT inhibits nuclear retention of the androgen-receptor complex.";
RL J. Biol. Chem. 257:122-125(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 -!- 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}.
CC -!- CAUTION: Was originally (Ref.4) thought to originate from mouse.
CC {ECO:0000305}.
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DR EMBL; V01255; CAA24568.1; -; mRNA.
DR EMBL; J00774; AAA41969.1; -; mRNA.
DR EMBL; J00773; AAA41969.1; JOINED; mRNA.
DR EMBL; V01545; CAA24787.1; -; mRNA.
DR EMBL; AF277385; AAG17693.1; -; mRNA.
DR EMBL; BC099696; AAH99696.1; -; mRNA.
DR PIR; A93286; BORT1.
DR RefSeq; NP_803435.1; NM_177482.1.
DR RefSeq; XP_008758450.1; XM_008760228.2.
DR RefSeq; XP_017444749.1; XM_017589260.1.
DR AlphaFoldDB; P02782; -.
DR SMR; P02782; -.
DR STRING; 10116.ENSRNOP00000027492; -.
DR PaxDb; P02782; -.
DR Ensembl; ENSRNOT00000027492; ENSRNOP00000027492; ENSRNOG00000020294.
DR GeneID; 309203; -.
DR KEGG; rno:309203; -.
DR UCSC; RGD:708459; rat.
DR CTD; 10647; -.
DR RGD; 708459; Psbpc1.
DR eggNOG; ENOG502SXZG; Eukaryota.
DR GeneTree; ENSGT00530000063866; -.
DR HOGENOM; CLU_166234_0_0_1; -.
DR InParanoid; P02782; -.
DR OMA; FISERVF; -.
DR OrthoDB; 1634878at2759; -.
DR PhylomeDB; P02782; -.
DR TreeFam; TF338526; -.
DR PRO; PR:P02782; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020294; Expressed in testis.
DR Genevisible; P02782; RN.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR CDD; cd00633; Secretoglobin; 1.
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; Lipid-binding; Reference proteome; Secreted;
KW Signal; Steroid-binding.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:7198120,
FT ECO:0000269|PubMed:7200013"
FT CHAIN 24..111
FT /note="Prostatic steroid-binding protein C1"
FT /id="PRO_0000036375"
FT CONFLICT 5
FT /note="K -> E (in Ref. 1; AAA41969)"
FT /evidence="ECO:0000305"
FT CONFLICT 15
FT /note="A -> S (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 17..18
FT /note="CC -> GG (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="N -> D (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 111 AA; 12763 MW; 2C1D11D003952945 CRC64;
MSTIKLSLCL LIMLAVCCYE ANASQICELV AHETISFLMK SEEELKKELE MYNAPPAAVE
AKLEVKRCVD QMSNGDRLVV AETLVYIFLE CGVKQWVETY YPEIDFYYDM N
