SHBG_RAT
ID SHBG_RAT Reviewed; 403 AA.
AC P08689; Q4QR94; Q63029;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Sex hormone-binding globulin;
DE Short=SHBG;
DE AltName: Full=Sex steroid-binding protein;
DE Short=SBP;
DE AltName: Full=Testis-specific androgen-binding protein;
DE Short=ABP;
DE Flags: Precursor;
GN Name=Shbg;
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] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=2432609; DOI=10.1073/pnas.84.2.339;
RA Joseph D.R., Hall S.H., French F.S.;
RT "Rat androgen-binding protein: evidence for identical subunits and amino
RT acid sequence homology with human sex hormone-binding globulin.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:339-343(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=2840566; DOI=10.1210/mend-2-1-3;
RA Joseph D.R., Hall S.H., Conti M., French F.S.;
RT "The gene structure of rat androgen-binding protein: identification of
RT potential regulatory deoxyribonucleic acid elements of a follicle-
RT stimulating hormone-regulated protein.";
RL Mol. Endocrinol. 2:3-13(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-239, AND ALTERNATIVE SPLICING.
RC STRAIN=Sprague-Dawley; TISSUE=Fetal liver;
RX PubMed=1702422; DOI=10.1016/s0021-9258(18)52414-5;
RA Sullivan P.M., Petrusz P., Szpirer C., Joseph D.R.;
RT "Alternative processing of androgen-binding protein RNA transcripts in
RT fetal rat liver. Identification of a transcript formed by trans splicing.";
RL J. Biol. Chem. 266:143-154(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-403 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=3135485; DOI=10.1210/mend-2-2-125;
RA Reventos J., Hammond G.L., Crozat A., Brooks D.E., Gunsalus G.L.,
RA Bardin C.W., Musto N.A.;
RT "Hormonal regulation of rat androgen-binding protein (ABP) messenger
RT ribonucleic acid and homology of human testosterone-estradiol-binding
RT globulin and ABP complementary deoxyribonucleic acids.";
RL Mol. Endocrinol. 2:125-132(1988).
RN [6]
RP PROTEIN SEQUENCE OF 171-181.
RX PubMed=1855466; DOI=10.1210/endo-129-2-690;
RA Danzo B.J., Parrott J.A., Skinner M.K.;
RT "Analysis of the steroid binding domain of rat androgen-binding protein.";
RL Endocrinology 129:690-696(1991).
CC -!- FUNCTION: Functions as an androgen transport protein, but may also be
CC involved in receptor mediated processes. Each dimer binds one molecule
CC of steroid. Specific for 5-alpha-dihydrotestosterone, testosterone, and
CC 17-beta-estradiol. Regulates the plasma metabolic clearance rate of
CC steroid hormones by controlling their plasma concentration (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=In testis, it is synthesized by
CC the Sertoli cells, secreted into the lumen of the seminiferous tubule
CC and transported to the epididymis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P08689-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P08689-2; Sequence=VSP_006093, VSP_006094;
CC -!- TISSUE SPECIFICITY: Isoform 2 is only expressed in the liver.
CC -!- DEVELOPMENTAL STAGE: In the fetal liver, expressed from day 14 to day
CC 17 after conception.
CC -!- MISCELLANEOUS: A putative trans-splicing which involves HDC and SHBG
CC gene regions produces a fusion protein expressed in fetal liver.
CC -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {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; M15034; AAA40648.1; -; mRNA.
DR EMBL; M19993; AAA40650.1; -; Genomic_DNA.
DR EMBL; BC097336; AAH97336.1; -; mRNA.
DR EMBL; M38759; AAA63476.1; ALT_TERM; mRNA.
DR EMBL; M31179; AAA40649.1; -; mRNA.
DR PIR; A40935; A26371.
DR RefSeq; NP_036782.1; NM_012650.1. [P08689-1]
DR AlphaFoldDB; P08689; -.
DR SMR; P08689; -.
DR STRING; 10116.ENSRNOP00000015248; -.
DR BindingDB; P08689; -.
DR ChEMBL; CHEMBL4932; -.
DR GlyGen; P08689; 2 sites.
DR PaxDb; P08689; -.
DR PRIDE; P08689; -.
DR GeneID; 24775; -.
DR KEGG; rno:24775; -.
DR UCSC; RGD:3671; rat. [P08689-1]
DR CTD; 6462; -.
DR RGD; 3671; Shbg.
DR eggNOG; KOG3927; Eukaryota.
DR HOGENOM; CLU_063172_0_0_1; -.
DR InParanoid; P08689; -.
DR PhylomeDB; P08689; -.
DR TreeFam; TF334367; -.
DR PRO; PR:P08689; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P08689; RN.
DR GO; GO:0005615; C:extracellular space; TAS:RGD.
DR GO; GO:0005496; F:steroid binding; IBA:GO_Central.
DR GO; GO:0007285; P:primary spermatocyte growth; IMP:RGD.
DR CDD; cd00110; LamG; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00054; Laminin_G_1; 1.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Lipid-binding; Reference proteome; Repeat; Secreted; Signal;
KW Steroid-binding.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..403
FT /note="Sex hormone-binding globulin"
FT /id="PRO_0000032561"
FT DOMAIN 46..218
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 225..391
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 194..218
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 363..391
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT VAR_SEQ 1..38
FT /note="MEKGEVASLRCRLLLLLLLLTLPPTHQGRTLRHIDPIQ -> QSREERGRAR
FT SVGLDFRLHK (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006093"
FT VAR_SEQ 241..245
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006094"
FT CONFLICT 347
FT /note="H -> R (in Ref. 5; AAA40649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 44533 MW; 2B359392CEFDF39D CRC64;
MEKGEVASLR CRLLLLLLLL TLPPTHQGRT LRHIDPIQSA QDSPAKYLSN GPGQEPVTVL
TIDLTKISKP SSSFEFRTWD PEGVIFYGDT NTEDDWFMLG LRDGQLEIQL HNLWARLTVG
FGPRLNDGRW HPVELKMNGD SLLLWVDGKE MLCLRQVSAS LADHPQLSMR IALGGLLLPT
SKLRFPLVPA LDGCIRRDIW LGHQAQLSTS ARTSLGNCDV DLQPGLFFPP GTHAEFSLQD
IPQPHTDPWT FSLELGFKLV DGAGRLLTLG TGTNSSWLTL HLQDQTVVLS SEAEPKLALP
LAVGLPLQLK LDVFKVALSQ GPKMEVLSTS LLRLASLWRL WSHPQGHLSL GALPGEDSSA
SFCLSDLWVQ GQRLDIDKAL SRSQDIWTHS CPQSPSNDTH TSH