ID   SG2A1_RAT               Reviewed;          95 AA.
AC   Q9JHB9;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Secretoglobin family 2A member 1;
DE   AltName: Full=Prostatic steroid-binding protein C3.2;
DE   Flags: Precursor;
GN   Name=Scgb2a1 {ECO:0000312|RGD:3424};
GN   Synonyms=Psbpc3 {ECO:0000312|RGD:3424};
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] {ECO:0000305, ECO:0000312|EMBL:CAB75892.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=6685625; DOI=10.1002/j.1460-2075.1983.tb01498.x;
RA   Hurst H.C., Parker M.G.;
RT   "Rat prostatic steroid binding protein: DNA sequence and transcript maps of
RT   the two C3 genes.";
RL   EMBO J. 2:769-774(1983).
CC   -!- FUNCTION: Part of prostatein which is the major secretory glycoprotein
CC       of ventral prostate gland. Steroid-binding protein; can bind non-polar
CC       steroids, cholesterol and a group of small proline-rich peptides (By
CC       similarity). {ECO:0000250|UniProtKB:P02780}.
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 non-covalent association forms tetrameric (C1:C3/C3:C2)
CC       prostatein molecules (By similarity). {ECO:0000250|UniProtKB:P02780}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed at very low level in ventral prostate.
CC       {ECO:0000269|PubMed:6685625}.
CC   -!- INDUCTION: By testosterone. {ECO:0000269|PubMed:6685625}.
CC   -!- SIMILARITY: Belongs to the secretoglobin family. Lipophilin subfamily.
CC       {ECO:0000305}.
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DR   EMBL; V01260; CAB75892.1; -; Genomic_DNA.
DR   EMBL; V01261; CAB75892.1; JOINED; Genomic_DNA.
DR   EMBL; V01262; CAB75892.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q9JHB9; -.
DR   SMR; Q9JHB9; -.
DR   GlyGen; Q9JHB9; 2 sites.
DR   UCSC; RGD:3424; rat.
DR   RGD; 3424; Scgb2a1.
DR   InParanoid; Q9JHB9; -.
DR   PhylomeDB; Q9JHB9; -.
DR   PRO; PR:Q9JHB9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Glycoprotein; Lipid-binding; Reference proteome; Secreted; Signal;
KW   Steroid-binding.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..95
FT                   /note="Secretoglobin family 2A member 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000284683"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   95 AA;  10622 MW;  B209F1BE177C52A4 CRC64;
     MKLVFLFLLV TIPICCYASG SGCSILDEVI RGTINSTVTL HDYMKLVKPY VHDHFTANAV
     KQFKQCFLDQ TNKTVENVGV MTEAIFNSES CQQPS