ID A0A2Y9L2L1_ENHLU Unreviewed; 395 AA.
AC A0A2Y9L2L1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Sex hormone-binding globulin {ECO:0000256|ARBA:ARBA00040510};
GN Name=LOC111161194 {ECO:0000313|RefSeq:XP_022380477.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022380477.1};
RN [1] {ECO:0000313|RefSeq:XP_022380477.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022380477.1};
RG RefSeq;
RL Submitted (NOV-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_022380477.1; XM_022524769.1.
DR AlphaFoldDB; A0A2Y9L2L1; -.
DR KEGG; elk:111161194; -.
DR Proteomes; UP000248482; 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; -; 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:UP000248482};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..395
FT /note="Sex hormone-binding globulin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016052464"
FT DOMAIN 37..210
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
SQ SEQUENCE 395 AA; 42853 MW; EAE8C4B2CBEA3989 CRC64;
MEGRGLLATS PGWLSLLLLL LPRPGHQGRR IQDSPAVHLS SGSGQEPITI MTFDFTKIRK
SFSSFELQTW DPEGVIFYGD TNPEDDWFVL ALRDGRSEIQ LHNQLAQVTV SAGPRLDDGR
WHQVEVRVLE DSLLLSVDGE EVLRLRQVSG SLASKPQPII RIALGGLLFP ASSLRLPLVP
ALDGCLRRST WLDPQAQTSG SVPTRSLKSC ALQSQPGTFF PPGTRAEFNL QDIPQPHAEP
WAFSLDLGLQ QAAGSGHLLA LGTPENPSQL SLHLQDQKVV VSSGTRPDLD LPLVLGLPLQ
LKLAASGAVL NQGSKKEILA LPDLDLASLL KLWVRPQGRL FLGALPGETS SASFCLNGLW
AQGQKLDMDQ ALSRSEDIWT HSCPQGPNNG TDTTH
//