ID   SHBG_CROCR              Reviewed;         393 AA.
AC   A0EQL2;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Sex hormone-binding globulin;
DE            Short=SHBG;
DE   Flags: Precursor;
GN   Name=SHBG;
OS   Crocuta crocuta (Spotted hyena).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Hyaenidae; Crocuta.
OX   NCBI_TaxID=9678;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Miguel-Queralt S., Yalcinkaya T.M., Avvakumov G.V., Place N., Siiteri P.K.,
RA   Glickman S.E., Hammond G.L.;
RT   "Unusual steroid-binding properties of hyena sex hormone-binding
RT   globulin.";
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; DQ285473; ABB89081.1; -; mRNA.
DR   AlphaFoldDB; A0EQL2; -.
DR   SMR; A0EQL2; -.
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..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..393
FT                   /note="Sex hormone-binding globulin"
FT                   /id="PRO_0000278833"
FT   DOMAIN          35..208
FT                   /note="Laminin G-like 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DOMAIN          215..381
FT                   /note="Laminin G-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   CARBOHYD        371
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        387
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        183..208
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT   DISULFID        353..381
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
SQ   SEQUENCE   393 AA;  42443 MW;  F715EE01E60FDF57 CRC64;
     MEGRGPLATS PRRRWLLLLL LLPHSHQRIQ DPPAVHLSSA SGQGPVTIMT FDFTKMRKTS
     SSFELRTWDP EGVILYGDTD PHEDWFMLGL RGGRPEIQIH NHVARLTVGA GPRLDDGKWH
     QVEVKVLGDL LLLTVDGEEV LCLKQVFGPL ASRPQPVVRI AVGGLPFPPS SLRLPLVPAL
     DGCVRRGSWL DHQAQTSVSA LSGSPRSCGV ESQPGSFFPP GAHAEFSLQD LPQPHAEPWA
     FSLDLGLQLA AGSGHLLALG TPENPPRLSL QLQDQKVVLS SAWGPQLHLP LVLGAPLQLK
     LAASGVTLSQ GPETEILALP LSDPGSLLNL WVQPHARLFL GALPGEAASA SFCLDGLWAQ
     GQKLDMDRAL NRSQNIWTHS CPQSLGNDTD TTH