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Database: UniProt
Entry: A0A2Y9L2L1_ENHLU
LinkDB: A0A2Y9L2L1_ENHLU
Original site: A0A2Y9L2L1_ENHLU 
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
//
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