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SHBG_RAT
ID   SHBG_RAT                Reviewed;         403 AA.
AC   P08689; Q4QR94; Q63029;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 146.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=2432609; DOI=10.1073/pnas.84.2.339;
RA   Joseph D.R., Hall S.H., French F.S.;
RT   "Rat androgen-binding protein: evidence for identical subunits and amino
RT   acid sequence homology with human sex hormone-binding globulin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:339-343(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   PubMed=2840566; DOI=10.1210/mend-2-1-3;
RA   Joseph D.R., Hall S.H., Conti M., French F.S.;
RT   "The gene structure of rat androgen-binding protein: identification of
RT   potential regulatory deoxyribonucleic acid elements of a follicle-
RT   stimulating hormone-regulated protein.";
RL   Mol. Endocrinol. 2:3-13(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-239, AND ALTERNATIVE SPLICING.
RC   STRAIN=Sprague-Dawley; TISSUE=Fetal liver;
RX   PubMed=1702422; DOI=10.1016/s0021-9258(18)52414-5;
RA   Sullivan P.M., Petrusz P., Szpirer C., Joseph D.R.;
RT   "Alternative processing of androgen-binding protein RNA transcripts in
RT   fetal rat liver. Identification of a transcript formed by trans splicing.";
RL   J. Biol. Chem. 266:143-154(1991).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-403 (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=3135485; DOI=10.1210/mend-2-2-125;
RA   Reventos J., Hammond G.L., Crozat A., Brooks D.E., Gunsalus G.L.,
RA   Bardin C.W., Musto N.A.;
RT   "Hormonal regulation of rat androgen-binding protein (ABP) messenger
RT   ribonucleic acid and homology of human testosterone-estradiol-binding
RT   globulin and ABP complementary deoxyribonucleic acids.";
RL   Mol. Endocrinol. 2:125-132(1988).
RN   [6]
RP   PROTEIN SEQUENCE OF 171-181.
RX   PubMed=1855466; DOI=10.1210/endo-129-2-690;
RA   Danzo B.J., Parrott J.A., Skinner M.K.;
RT   "Analysis of the steroid binding domain of rat androgen-binding protein.";
RL   Endocrinology 129:690-696(1991).
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.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=In testis, it is synthesized by
CC       the Sertoli cells, secreted into the lumen of the seminiferous tubule
CC       and transported to the epididymis.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=1;
CC         IsoId=P08689-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P08689-2; Sequence=VSP_006093, VSP_006094;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is only expressed in the liver.
CC   -!- DEVELOPMENTAL STAGE: In the fetal liver, expressed from day 14 to day
CC       17 after conception.
CC   -!- MISCELLANEOUS: A putative trans-splicing which involves HDC and SHBG
CC       gene regions produces a fusion protein expressed in fetal liver.
CC   -!- MISCELLANEOUS: [Isoform 2]: Incomplete sequence. {ECO:0000305}.
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DR   EMBL; M15034; AAA40648.1; -; mRNA.
DR   EMBL; M19993; AAA40650.1; -; Genomic_DNA.
DR   EMBL; BC097336; AAH97336.1; -; mRNA.
DR   EMBL; M38759; AAA63476.1; ALT_TERM; mRNA.
DR   EMBL; M31179; AAA40649.1; -; mRNA.
DR   PIR; A40935; A26371.
DR   RefSeq; NP_036782.1; NM_012650.1. [P08689-1]
DR   AlphaFoldDB; P08689; -.
DR   SMR; P08689; -.
DR   STRING; 10116.ENSRNOP00000015248; -.
DR   BindingDB; P08689; -.
DR   ChEMBL; CHEMBL4932; -.
DR   GlyGen; P08689; 2 sites.
DR   PaxDb; P08689; -.
DR   PRIDE; P08689; -.
DR   GeneID; 24775; -.
DR   KEGG; rno:24775; -.
DR   UCSC; RGD:3671; rat. [P08689-1]
DR   CTD; 6462; -.
DR   RGD; 3671; Shbg.
DR   eggNOG; KOG3927; Eukaryota.
DR   HOGENOM; CLU_063172_0_0_1; -.
DR   InParanoid; P08689; -.
DR   PhylomeDB; P08689; -.
DR   TreeFam; TF334367; -.
DR   PRO; PR:P08689; -.
DR   Proteomes; UP000002494; Unplaced.
DR   Genevisible; P08689; RN.
DR   GO; GO:0005615; C:extracellular space; TAS:RGD.
DR   GO; GO:0005496; F:steroid binding; IBA:GO_Central.
DR   GO; GO:0007285; P:primary spermatocyte growth; IMP:RGD.
DR   CDD; cd00110; LamG; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001791; Laminin_G.
DR   Pfam; PF00054; Laminin_G_1; 1.
DR   SMART; SM00282; LamG; 1.
DR   SUPFAM; SSF49899; SSF49899; 2.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Lipid-binding; Reference proteome; Repeat; Secreted; Signal;
KW   Steroid-binding.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..403
FT                   /note="Sex hormone-binding globulin"
FT                   /id="PRO_0000032561"
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        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"
FT   VAR_SEQ         1..38
FT                   /note="MEKGEVASLRCRLLLLLLLLTLPPTHQGRTLRHIDPIQ -> QSREERGRAR
FT                   SVGLDFRLHK (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006093"
FT   VAR_SEQ         241..245
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_006094"
FT   CONFLICT        347
FT                   /note="H -> R (in Ref. 5; AAA40649)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   403 AA;  44533 MW;  2B359392CEFDF39D CRC64;
     MEKGEVASLR CRLLLLLLLL TLPPTHQGRT LRHIDPIQSA QDSPAKYLSN GPGQEPVTVL
     TIDLTKISKP SSSFEFRTWD PEGVIFYGDT NTEDDWFMLG LRDGQLEIQL HNLWARLTVG
     FGPRLNDGRW HPVELKMNGD SLLLWVDGKE MLCLRQVSAS LADHPQLSMR IALGGLLLPT
     SKLRFPLVPA LDGCIRRDIW LGHQAQLSTS ARTSLGNCDV DLQPGLFFPP GTHAEFSLQD
     IPQPHTDPWT FSLELGFKLV DGAGRLLTLG TGTNSSWLTL HLQDQTVVLS SEAEPKLALP
     LAVGLPLQLK LDVFKVALSQ GPKMEVLSTS LLRLASLWRL WSHPQGHLSL GALPGEDSSA
     SFCLSDLWVQ GQRLDIDKAL SRSQDIWTHS CPQSPSNDTH TSH
 
 
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