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 04-NOV-2026, entry version 165. 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}. 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; 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_011248837.3. DR AlphaFoldDB; P97497; -. DR SMR; P97497; -. DR FunCoup; P97497; 20. DR STRING; 10090.ENSMUSP00000005334; -. DR GlyCosmos; P97497; 3 sites, No reported glycans. DR GlyGen; P97497; 3 sites. DR PhosphoSitePlus; P97497; -. DR CPTAC; non-CPTAC-4061; -. DR PaxDb; 10090-ENSMUSP00000005334; -. DR PeptideAtlas; P97497; -. DR ProteomicsDB; 257150; -. DR Antibodypedia; 24226; 837 antibodies from 39 providers. DR DNASU; 20415; -. DR Ensembl; ENSMPUT00000009106; ENSMPUP00000008959; ENSMPUG00000009031. DR Ensembl; ENSMUST00000005334.3; ENSMUSP00000005334.3; ENSMUSG00000005202.3. DR GeneID; 20415; -. DR KEGG; mmu:20415; -. DR UCSC; uc007jqp.2; mouse. DR AGR; MGI:98295; -. 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; ACLRHWV; -. DR OrthoDB; 6275838at2759; -. DR PhylomeDB; P97497; -. DR BioGRID-ORCS; 20415; 4 hits in 80 CRISPR screens. DR PRO; PR:P97497; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; P97497; protein. DR Bgee; ENSMUSG00000005202; Expressed in blastoderm cell in morula and 38 other cell types or tissues. DR ExpressionAtlas; P97497; baseline and differential. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0005497; F:androgen binding; IBA:GO_Central. DR GO; GO:0005496; F:steroid binding; IBA:GO_Central. DR GO; GO:0007285; P:primary spermatocyte growth; ISO:GO_Central. DR CDD; cd00110; LamG; 1. DR FunFam; 2.60.120.200:FF:000107; Sex hormone-binding globulin; 1. DR FunFam; 2.60.120.200:FF:000355; Sex hormone-binding globulin; 1. DR Gene3D; 2.60.120.200; -; 2. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR051145; GAS-SHBG-PROS. DR InterPro; IPR001791; Laminin_G. DR PANTHER; PTHR24040; LAMININ G-LIKE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR24040:SF3; SEX HORMONE-BINDING GLOBULIN; 1. DR Pfam; PF00054; Laminin_G_1; 1. DR SMART; SM00282; LamG; 2. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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 //