ID A0A3P8YBY8_ESOLU Unreviewed; 394 AA.
AC A0A3P8YBY8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Sex hormone-binding globulin {ECO:0000256|ARBA:ARBA00040510};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000014099.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000014099.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000014099.2}
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_010886196.1; XM_010887894.3.
DR RefSeq; XP_019898944.1; XM_020043385.1.
DR AlphaFoldDB; A0A3P8YBY8; -.
DR STRING; 8010.ENSELUP00000014099; -.
DR Ensembl; ENSELUT00000022802.2; ENSELUP00000014099.2; ENSELUG00000014170.2.
DR GeneID; 105020685; -.
DR KEGG; els:105020685; -.
DR GeneTree; ENSGT00940000154035; -.
DR InParanoid; A0A3P8YBY8; -.
DR OMA; FPLMQIS; -.
DR OrthoDB; 5316510at2759; -.
DR Proteomes; UP000265140; LG24.
DR Bgee; ENSELUG00000014170; Expressed in liver and 9 other cell types or tissues.
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; -; 2.
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:UP000265140};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Steroid-binding {ECO:0000256|ARBA:ARBA00022665}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..394
FT /note="Sex hormone-binding globulin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5027640745"
FT DOMAIN 40..214
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
SQ SEQUENCE 394 AA; 43384 MW; 6654499A94588CFD CRC64;
MGLLNTTTGE LLVSLCLTLL VWGAEGQGTG KVKLVSGSEE INLGQHQGTW APLMQTRENL
TQVKSIRSTF LFRTFDPEGV VFYGDTLNGK DWFILALKDG IPEMQIGKAD ILVSMHGGPK
INDGKWHLLE ISNNGDFVRL NVDSQKEVIV GLKSKMTESV LQGQIRLAIG GILVSPENLL
VPFQPAMDGC IRQGNWLNLS MPWETQQLGE PRPCYANIEP GSYFTGAGVA TFNTTELPAY
QTEDIGITIS IQGDSSMLNG TILSLKTPGE EIATTRLIVD NDLKNIKLTI RTIESISKSI
RFTKLTLTLK KNQLNMKTDE TEMKLESDDI PDYLSRWKEG MILAFGGLQE DRAPDNSNQY
LKGCLAKIQV LGQDVDLDRA LYKDASISSH SCPS
//