ID A0A2K5F214_AOTNA Unreviewed; 422 AA.
AC A0A2K5F214;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Sex hormone-binding globulin {ECO:0000256|ARBA:ARBA00040510};
DE AltName: Full=Sex steroid-binding protein {ECO:0000256|ARBA:ARBA00041855};
DE AltName: Full=Testis-specific androgen-binding protein {ECO:0000256|ARBA:ARBA00041528};
GN Name=SHBG {ECO:0000313|Ensembl:ENSANAP00000039502.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000039502.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000039502.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00037620}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00122}.
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DR RefSeq; XP_012312924.1; XM_012457501.1.
DR AlphaFoldDB; A0A2K5F214; -.
DR STRING; 37293.ENSANAP00000039502; -.
DR Ensembl; ENSANAT00000057602.1; ENSANAP00000039502.1; ENSANAG00000037137.1.
DR GeneID; 105720805; -.
DR CTD; 6462; -.
DR GeneTree; ENSGT00940000154035; -.
DR OMA; FPLMQIS; -.
DR OrthoDB; 5316510at2759; -.
DR Proteomes; UP000233020; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Steroid-binding {ECO:0000256|ARBA:ARBA00022665}.
FT DOMAIN 65..237
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
SQ SEQUENCE 422 AA; 46105 MW; CEDF5F307A3C542E CRC64;
MQVCLPLHTL PRVVRAPSGQ RLTMESRGPL ATSRLLLLLL LLATHQGWAL RPILPTQRAQ
DSPGVHLSNG PGHEPVAVMT FDLTKITKPF SSFELRTWDP EGVIFYGDTN PKDDWFMLGL
RDGRPEIQLH NSWAQLTVGA GPRLDDGRWH QVEVKIDGDS VLLRVDGEEV LCLRQVSGPL
ASKDHPTMRI AVGGLLFPSS NLRLPLTPAL DGCLRRDSWL DKQAKISASA PTSLRSCDVE
SNPGIFLPPG THAEFNLQDI PQPHAEPWAF SLDLGLEQAA GSGHLLALGT PENPSWLSLY
LQDQKVVLSS GLGPGLDLPL VLGLPLQLKL SMSRVILSQG LKMEVFALPS LRLAPLLNLW
DQPQGRLFLG ALPGEDSSTS FCLNGLWAQG QRLDVDRALN RSHDIWTHSC PQNPGNGTDA
SH
//
