SHBG_MOUSE
ID SHBG_MOUSE Reviewed; 403 AA.
AC P97497; Q0VB52;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, 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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=2753230; DOI=10.1016/0303-7207(89)90084-1;
RA Wang Y.-M., Sullivan P.M., Petrusz P., Yarbrough W.G., Joseph D.R.;
RT "The androgen-binding protein gene is expressed in CD1 mouse testis.";
RL Mol. Cell. Endocrinol. 63:85-92(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
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; U85644; AAB42088.1; -; mRNA.
DR EMBL; BC120785; AAI20786.1; -; mRNA.
DR EMBL; BC120787; AAI20788.1; -; mRNA.
DR CCDS; CCDS24899.1; -.
DR RefSeq; NP_035497.1; NM_011367.2.
DR RefSeq; XP_011247139.1; XM_011248837.2.
DR AlphaFoldDB; P97497; -.
DR SMR; P97497; -.
DR STRING; 10090.ENSMUSP00000005334; -.
DR GlyGen; P97497; 3 sites.
DR PhosphoSitePlus; P97497; -.
DR CPTAC; non-CPTAC-4061; -.
DR PaxDb; P97497; -.
DR PeptideAtlas; P97497; -.
DR PRIDE; P97497; -.
DR ProteomicsDB; 257150; -.
DR Antibodypedia; 24226; 736 antibodies from 36 providers.
DR DNASU; 20415; -.
DR Ensembl; ENSMUST00000005334; ENSMUSP00000005334; ENSMUSG00000005202.
DR GeneID; 20415; -.
DR KEGG; mmu:20415; -.
DR UCSC; uc007jqp.2; mouse.
DR CTD; 6462; -.
DR MGI; MGI:98295; Shbg.
DR VEuPathDB; HostDB:ENSMUSG00000005202; -.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT00940000154035; -.
DR HOGENOM; CLU_063172_0_0_1; -.
DR InParanoid; P97497; -.
DR OMA; NLSMPWE; -.
DR OrthoDB; 1279734at2759; -.
DR PhylomeDB; P97497; -.
DR TreeFam; TF334367; -.
DR BioGRID-ORCS; 20415; 4 hits in 75 CRISPR screens.
DR PRO; PR:P97497; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P97497; protein.
DR Bgee; ENSMUSG00000005202; Expressed in morula and 36 other tissues.
DR ExpressionAtlas; P97497; baseline and differential.
DR Genevisible; P97497; MM.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005496; F:steroid binding; IBA:GO_Central.
DR GO; GO:0007285; P:primary spermatocyte growth; ISO:MGI.
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; 2.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Lipid-binding; Reference proteome; Repeat;
KW Secreted; Signal; Steroid-binding.
FT SIGNAL 1..30
FT /evidence="ECO:0000250"
FT CHAIN 31..403
FT /note="Sex hormone-binding globulin"
FT /id="PRO_0000032558"
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 284
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"
SQ SEQUENCE 403 AA; 44816 MW; 5198DDD1CDC23530 CRC64;
MEKRDSVALH WRLLLLLLLL MPPPTHQGRA LRHIDPIQSA QDPPAKYLSN GPGQEPVMVM
TIDLTKISKP HSSFEFRTWD PEGVIFYGDT NTEDDWFLLG LRAGQLEIQL HNAWARLTVG
FGPRLDDGRW HPVELKMNGD SLLLWVDGKE MLCLRQISAS LADHSQRSMR IALGGLLLPT
SKLRFPLVPA LDGCIRRDIW LGHQAQLSAS PRTSLGNCDV DLQPGLFFPP GTHAEFSLQD
IPQPHADPWT FSLELGFKLV DGSGQLLALG TGTNSSWLNI HLQNQSVVLS SEAEPKVVLP
LDVGLPLQLT LDRVKVVLSQ GPKMEVLSMS LLRPASLWRL WSHPQGHLSL GALPGESSSA
SFCLSDFWVQ GQRLDIDQAL SRSQDIWTHS CPQRPSNDTR TSH
