SHBG_PHOSU
ID SHBG_PHOSU Reviewed; 399 AA.
AC Q62588; P97518;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 88.
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 Phodopus sungorus (Striped hairy-footed hamster) (Djungarian hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Phodopus.
OX NCBI_TaxID=10044;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7495693; DOI=10.1016/0960-0760(95)00166-w;
RA Cates J.M., Damassa D.A., Gagin G.A., Dempsey R.V.;
RT "Hepatic expression of sex hormone-binding globulin associated with the
RT postnatal surge of serum androgen-binding activity in the Djungarian
RT hamster.";
RL J. Steroid Biochem. Mol. Biol. 55:147-158(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=9462298; DOI=10.1530/jrf.0.1110291;
RA Cates J.M., Damassa D.A.;
RT "Characterization and developmental expression patterns of testicular
RT androgen-binding protein in the Djungarian hamster (Phodopus sungorus).";
RL J. Reprod. Fertil. 111:291-298(1997).
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=In testis, it is
CC synthesized by the Sertoli cells, secreted into the lumen of the
CC seminiferous tubule and transported to the epididymis. {ECO:0000250}.
CC -!- PTM: Differentially glycosylated in liver (SHBG) and testis (ABP).
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DR EMBL; U16673; AAC52344.1; -; mRNA.
DR EMBL; U63010; AAB41681.1; -; mRNA.
DR AlphaFoldDB; Q62588; -.
DR SMR; Q62588; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Lipid-binding; Repeat; Secreted; Signal;
KW Steroid-binding.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..399
FT /note="Sex hormone-binding globulin"
FT /id="PRO_0000032559"
FT DOMAIN 43..214
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 221..387
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 191..214
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 359..387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT CONFLICT 289
FT /note="V -> I (in Ref. 2; AAB41681)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="G -> V (in Ref. 2; AAB41681)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 399 AA; 43842 MW; C173B70782425730 CRC64;
MENRDSVASL LLLLLLLPPP HTHQGQVLRH VVPTQNSQDS PARYLSNGPG QEPVAVMTID
LTQMSKPYSS FEFRTLDPEG VIFYGDTNTK DDWFMLGLRD GQLEIQMHNP WAQLTVGFGP
RLNDGRWHQV ELKMSGDSLQ LWVDGKELLC LRQISGTLAN NSWPSMRIAL GGLLLPTSSL
RFPLVPALDG CLRRDTWLGH QVHLSPSAPN LGNCDVDLQP GLFFPQGTHA EFSLQDIPQP
RTDPWSFSLE LGLKLVDGSG CLLALGTRTN SSWLSLHLQD QKVVLSSGVE PKLVLALDMG
LPLQLKLDIL KVVLSQGPKT EVLGASASRL AALRTLWSHP QGLLSLGALA GDNSSASFCL
SDLWVQGQRL DIDQALNRSQ NIWTHSCPHS PNNVSHISH
