SHBG_RABIT
ID SHBG_RABIT Reviewed; 398 AA.
AC P15196; Q28663; Q28669;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 113.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Liver;
RX PubMed=9203991; DOI=10.1677/joe.0.1530373;
RA Lee W.M., Wong A.S., Tu A.W.K., Cheung C.H., Li J.C., Hammond G.L.;
RT "Rabbit sex hormone binding globulin: primary structure, tissue expression,
RT and structure/function analyses by expression in Escherichia coli.";
RL J. Endocrinol. 153:373-384(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10746639; DOI=10.1210/endo.141.4.7406;
RA Ip Y.C., Lee W.M., Hammond G.L.;
RT "The rabbit sex hormone-binding globulin gene: structural organization and
RT characterization of its 5-flanking region.";
RL Endocrinology 141:1356-1365(2000).
RN [3]
RP PROTEIN SEQUENCE OF 32-398.
RC TISSUE=Serum;
RX PubMed=2808412; DOI=10.1016/s0021-9258(19)47267-0;
RA Griffin P.R., Kumar S., Shabanowitz J., Charbonneau H., Namkung P.C.,
RA Walsh K.A., Hunt D.F., Petra P.H.;
RT "The amino acid sequence of the sex steroid-binding protein of rabbit
RT serum.";
RL J. Biol. Chem. 264:19066-19075(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 103-398.
RC STRAIN=New Zealand; TISSUE=Testis;
RA Yarbrough W.G., Welch J.E., Joseph D.R.;
RL Submitted (AUG-1988) 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.
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; U57553; AAB72240.1; -; mRNA.
DR EMBL; AF144711; AAF70547.1; -; Genomic_DNA.
DR EMBL; X12661; CAA31187.1; -; mRNA.
DR PIR; A34436; A34436.
DR RefSeq; NP_001075839.1; NM_001082370.1.
DR AlphaFoldDB; P15196; -.
DR SMR; P15196; -.
DR STRING; 9986.ENSOCUP00000002218; -.
DR ChEMBL; CHEMBL1075202; -.
DR PRIDE; P15196; -.
DR GeneID; 100009224; -.
DR KEGG; ocu:100009224; -.
DR CTD; 6462; -.
DR eggNOG; KOG3927; Eukaryota.
DR InParanoid; P15196; -.
DR OrthoDB; 1279734at2759; -.
DR PRO; PR:P15196; -.
DR Proteomes; UP000001811; Unplaced.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Lipid-binding;
KW Reference proteome; Repeat; Secreted; Signal; Steroid-binding.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:2808412"
FT CHAIN 32..398
FT /note="Sex hormone-binding globulin"
FT /id="PRO_0000032560"
FT DOMAIN 41..213
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 220..386
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 392
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 189..213
FT DISULFID 358..386
FT CONFLICT 103
FT /note="I -> V (in Ref. 4; CAA31187)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="L -> I (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 326..327
FT /note="PS -> SP (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="Q -> K (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="D -> V (in Ref. 4; CAA31187)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..395
FT /note="TD -> SV (in Ref. 4; CAA31187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 43154 MW; 23B7F6FD27D592B8 CRC64;
MATPPLVPLL LLLLLLLPHA HHRLALRSVL ATQRAQDSPA VHLINGLGQE PIQVLTFDLT
RLVKASSSFE LRTWDSEGVI FYGDTSPKDD WFMLGLRDGR PEIQMHNPWA QLTVGAGPRL
DDGSWHQVHV KIRGDSVLLE VDGKEVLRLS QVSGTLHDKP QPVMKLAVGG LLFPPSSLRL
PLVPALDGCL RRGSWLDPQA QISASAHASR RSCDVELQPG IFFPPGTHAE FSLQDIPQPQ
TEPWAFSLDL ELKPSEGSGR LLALGTPEDP NWLSLHLQDQ KVVLSSGMEP GLDLPLAWGL
PLQLKLGVST AVLSQGSKKQ ALGLPPSGLG PLLNLWAQPQ GRLFLGALPG EDSSASFCLD
GLWAQGQKLD MDKALNRSQD IWTHSCPSSP GNGTDTSH
