ID SHBG_HUMAN Reviewed; 402 AA. AC P04278; B0FWH4; E9PGW1; F5H5Z8; I3L1N7; P14689; Q16616; Q3MIL0; AC Q6ISD2; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 2. DT 11-NOV-2015, entry version 164. 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 AltName: Full=Testosterone-estradiol-binding globulin; DE Short=TeBG; DE AltName: Full=Testosterone-estrogen-binding globulin; DE Flags: Precursor; GN Name=SHBG; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL NUCLEOTIDE SEQUENCE [MRNA] RP (ISOFORM 2), AND ALTERNATIVE SPLICING. RC TISSUE=Testis; RX PubMed=2587256; DOI=10.1093/nar/17.22.9245; RA Gershagen S., Lundwall A., Fernlund P.; RT "Characterization of the human sex hormone binding globulin (SHBG) RT gene and demonstration of two transcripts in both liver and testis."; RL Nucleic Acids Res. 17:9245-9258(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING. RC TISSUE=Testis; RX PubMed=2608061; DOI=10.1210/mend-3-11-1869; RA Hammond G.L., Underhill D.A., Rykse H.M., Smith C.L.; RT "The human sex hormone-binding globulin gene contains exons for RT androgen-binding protein and two other testicular messenger RNAs."; RL Mol. Endocrinol. 3:1869-1876(1989). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RX PubMed=15028279; DOI=10.1016/j.ygeno.2003.09.023; RA Jin P., Fu G.K., Wilson A.D., Yang J., Chien D., Hawkins P.R., RA Au-Young J., Stuve L.L.; RT "PCR isolation and cloning of novel splice variant mRNAs from known RT drug target genes."; RL Genomics 83:566-571(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in RT the human lineage."; RL Nature 440:1045-1049(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Liver; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-402 (ISOFORM 1). RC TISSUE=Liver; RX PubMed=3569533; DOI=10.1016/0014-5793(87)80121-7; RA Hammond G.L., Underhill D.A., Smith C.L., Goping I.S., Harley M.J., RA Musto N.A., Cheng C.Y., Bardin C.W.; RT "The cDNA-deduced primary structure of human sex hormone-binding RT globulin and location of its steroid-binding domain."; RL FEBS Lett. 215:100-104(1987). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-402 (ISOFORM 4). RC TISSUE=Liver; RA Kahn S.M., Nakhla A.M., Hryb D.J., Rosner W., Romas N.A.; RT "Human sex hormone-binding globulin gene transcript expression in RT liver, prostate, breast, testis, and brain- multiple promoters and RT complex alternative splicing."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 47-402 (ISOFORM 1). RC TISSUE=Liver; RX PubMed=2956126; DOI=10.1016/0014-5793(87)80890-6; RA Gershagen S., Fernlund P., Lundwall A.; RT "A cDNA coding for human sex hormone binding globulin. Homology to RT vitamin K-dependent protein S."; RL FEBS Lett. 220:129-135(1987). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 121-402 (ISOFORM 1). RC TISSUE=Liver; RX PubMed=2956125; DOI=10.1016/0014-5793(87)80261-2; RA Que B.G., Petra P.H.; RT "Characterization of a cDNA coding for sex steroid-binding protein of RT human plasma."; RL FEBS Lett. 219:405-409(1987). RN [10] RP PROTEIN SEQUENCE OF 30-54. RX PubMed=3702459; DOI=10.1016/0022-4731(86)90442-5; RA Hammond G.L., Robinson P.A., Sugino H., Ward D.N., Finne J.; RT "Physicochemical characteristics of human sex hormone binding RT globulin: evidence for two identical subunits."; RL J. Steroid Biochem. 24:815-824(1986). RN [11] RP PROTEIN SEQUENCE OF 30-402. RX PubMed=3542030; DOI=10.1021/bi00371a048; RA Walsh K.A., Titani K., Takio K., Kumar S., Hayes R., Petra P.H.; RT "Amino acid sequence of the sex steroid binding protein of human blood RT plasma."; RL Biochemistry 25:7584-7590(1986). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-380. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [13] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-380. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [14] RP VARIANT ASN-356, CHARACTERIZATION OF VARIANT ASN-356, AND RP GLYCOSYLATION. RX PubMed=1400872; DOI=10.1210/jc.75.4.1066; RA Power S.G.A., Bocchinfuso W.P., Pallesen M., Warmels-Rodenhiser S., RA Van Baelen H., Hammond G.L.; RT "Molecular analyses of a human sex hormone-binding globulin variant: RT evidence for an additional carbohydrate chain."; RL J. Clin. Endocrinol. Metab. 75:1066-1070(1992). RN [15] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 42-211. RX PubMed=10675319; DOI=10.1093/emboj/19.4.504; RA Grishkovskaya I., Avvakumov G.V., Sklenar G., Dales D., Hammond G.L., RA Muller Y.A.; RT "Crystal structure of human sex hormone-binding globulin: steroid RT transport by a laminin G-like domain."; RL EMBO J. 19:504-512(2000). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-218. RX PubMed=12065592; DOI=10.1074/jbc.M203999200; RA Grishkovskaya I., Avvakumov G.V., Hammond G.L., Catalano M.G., RA Muller Y.A.; RT "Steroid ligands bind human sex hormone-binding globulin in specific RT orientations and produce distinct changes in protein conformation."; RL J. Biol. Chem. 277:32086-32093(2002). RN [17] RP VARIANT ASN-356. RX PubMed=7714097; DOI=10.1210/jc.80.4.1253; RA Hardy D.O., Carino C., Catterall J.F., Larrea F.; RT "Molecular characterization of a genetic variant of the steroid RT hormone-binding globulin gene in heterozygous subjects."; RL J. Clin. Endocrinol. Metab. 80:1253-1256(1995). RN [18] RP VARIANTS HIS-25 AND ASN-356. RX PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions RT of human genes."; RL Nat. Genet. 22:231-238(1999). RN [19] RP ERRATUM. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). CC -!- FUNCTION: Functions as an androgen transport protein, but may also CC be involved in receptor mediated processes. Each dimer binds one CC molecule of steroid. Specific for 5-alpha-dihydrotestosterone, CC testosterone, and 17-beta-estradiol. Regulates the plasma CC metabolic clearance rate of steroid hormones by controlling their CC plasma concentration. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=In testis, it CC is synthesized by the Sertoli cells, secreted into the lumen of CC the seminiferous tubule and transported to the epididymis. CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=SHBG, SHBGr-1; CC IsoId=P04278-1; Sequence=Displayed; CC Name=2; Synonyms=Sex hormone binding globulin-gene-related protein CC (SHBGgrp), SHBGr-2; CC IsoId=P04278-2; Sequence=VSP_006090, VSP_006091, VSP_006092; CC Note=Incomplete sequence.; CC Name=3; CC IsoId=P04278-3; Sequence=VSP_006091, VSP_006092; CC Note=No experimental confirmation available.; CC Name=4; CC IsoId=P04278-4; Sequence=VSP_045358; CC Name=5; CC IsoId=P04278-5; Sequence=VSP_045376; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are present in liver CC and testis. CC -!- PTM: Variant Asn-356 contains one N-linked (GlcNAc...) at position CC 356. {ECO:0000269|PubMed:1400872, ECO:0000269|PubMed:16335952, CC ECO:0000269|PubMed:19159218}. CC -!- SIMILARITY: Contains 2 laminin G-like domains. CC {ECO:0000255|PROSITE-ProRule:PRU00122}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA29309.1; Type=Frameshift; Positions=47, 52, 54; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Androgen-binding protein entry; CC URL="https://en.wikipedia.org/wiki/Androgen-binding_protein"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/SHBGID42286ch17p13.html"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X16349; CAA34398.1; -; Genomic_DNA. DR EMBL; X16350; CAA34399.1; -; Genomic_DNA. DR EMBL; X16351; CAA34400.1; -; mRNA. DR EMBL; M31651; AAC18778.1; -; Genomic_DNA. DR EMBL; CD013955; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC069597; AAH69597.1; -; mRNA. DR EMBL; BC101785; AAI01786.1; -; mRNA. DR EMBL; BC112186; AAI12187.1; -; mRNA. DR EMBL; AC007421; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X05403; CAA28987.1; -; mRNA. DR EMBL; EU352661; ABY67999.1; -; mRNA. DR EMBL; X05885; CAA29309.1; ALT_FRAME; mRNA. DR EMBL; X05792; CAA29234.1; -; mRNA. DR CCDS; CCDS11117.1; -. [P04278-1] DR CCDS; CCDS54082.1; -. [P04278-3] DR CCDS; CCDS54083.1; -. [P04278-4] DR CCDS; CCDS58513.1; -. [P04278-5] DR PIR; S09606; BOHUS. DR RefSeq; NP_001031.2; NM_001040.4. [P04278-1] DR RefSeq; NP_001139751.1; NM_001146279.2. [P04278-5] DR RefSeq; NP_001139752.1; NM_001146280.2. [P04278-3] DR RefSeq; NP_001139753.1; NM_001146281.2. [P04278-4] DR RefSeq; NP_001276042.1; NM_001289113.1. DR RefSeq; NP_001276043.1; NM_001289114.1. DR RefSeq; NP_001276044.1; NM_001289115.1. DR RefSeq; NP_001276045.1; NM_001289116.1. DR UniGene; Hs.632235; -. DR PDB; 1D2S; X-ray; 1.55 A; A=42-217. DR PDB; 1F5F; X-ray; 1.70 A; A=30-234. DR PDB; 1KDK; X-ray; 1.70 A; A=41-217. DR PDB; 1KDM; X-ray; 2.35 A; A=41-217. DR PDB; 1LHN; X-ray; 2.00 A; A=30-218. DR PDB; 1LHO; X-ray; 2.00 A; A=30-218. DR PDB; 1LHU; X-ray; 1.80 A; A=30-218. DR PDB; 1LHV; X-ray; 2.00 A; A=30-218. DR PDB; 1LHW; X-ray; 1.75 A; A=30-218. DR PDBsum; 1D2S; -. DR PDBsum; 1F5F; -. DR PDBsum; 1KDK; -. DR PDBsum; 1KDM; -. DR PDBsum; 1LHN; -. DR PDBsum; 1LHO; -. DR PDBsum; 1LHU; -. DR PDBsum; 1LHV; -. DR PDBsum; 1LHW; -. DR ProteinModelPortal; P04278; -. DR SMR; P04278; 32-391. DR BioGrid; 112359; 58. DR IntAct; P04278; 2. DR STRING; 9606.ENSP00000369816; -. DR BindingDB; P04278; -. DR ChEMBL; CHEMBL3305; -. DR DrugBank; DB01406; Danazol. DR DrugBank; DB00858; Drostanolone. DR DrugBank; DB00783; Estradiol. DR DrugBank; DB04574; Estropipate. DR DrugBank; DB01185; Fluoxymesterone. DR DrugBank; DB00741; Hydrocortisone. DR DrugBank; DB06710; Methyltestosterone. DR DrugBank; DB00648; Mitotane. DR DrugBank; DB00717; Norethindrone. DR DrugBank; DB00421; Spironolactone. DR DrugBank; DB00624; Testosterone. DR DrugBank; DB05275; transdermal testosterone gel. DR UniCarbKB; P04278; -. DR BioMuta; SHBG; -. DR DMDM; 134907; -. DR PaxDb; P04278; -. DR PeptideAtlas; P04278; -. DR PRIDE; P04278; -. DR DNASU; 6462; -. DR Ensembl; ENST00000380450; ENSP00000369816; ENSG00000129214. [P04278-1] DR Ensembl; ENST00000416273; ENSP00000388867; ENSG00000129214. [P04278-3] DR Ensembl; ENST00000441599; ENSP00000393426; ENSG00000129214. [P04278-4] DR Ensembl; ENST00000575903; ENSP00000458973; ENSG00000129214. [P04278-5] DR GeneID; 6462; -. DR KEGG; hsa:6462; -. DR UCSC; uc002gie.2; human. [P04278-1] DR CTD; 6462; -. DR GeneCards; SHBG; -. DR HGNC; HGNC:10839; SHBG. DR MIM; 182205; gene. DR neXtProt; NX_P04278; -. DR PharmGKB; PA35745; -. DR eggNOG; ENOG410IKW6; Eukaryota. DR eggNOG; ENOG410YKMT; LUCA. DR GeneTree; ENSGT00530000063339; -. DR HOGENOM; HOG000285982; -. DR HOVERGEN; HBG017800; -. DR InParanoid; P04278; -. DR OMA; EIQLHNH; -. DR PhylomeDB; P04278; -. DR TreeFam; TF334367; -. DR ChiTaRS; SHBG; human. DR EvolutionaryTrace; P04278; -. DR GeneWiki; Sex_hormone-binding_globulin; -. DR GenomeRNAi; 6462; -. DR NextBio; 25109; -. DR PRO; PR:P04278; -. DR Proteomes; UP000005640; Chromosome 17. DR Bgee; P04278; -. DR CleanEx; HS_SHBG; -. DR ExpressionAtlas; P04278; baseline and differential. DR Genevisible; P04278; HS. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB. DR GO; GO:0005497; F:androgen binding; TAS:ProtInc. DR GO; GO:0007285; P:primary spermatocyte growth; IEA:Ensembl. DR Gene3D; 2.60.120.200; -; 2. DR InterPro; IPR013320; ConA-like_dom. 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 3D-structure; Alternative splicing; Complete proteome; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Lipid-binding; Polymorphism; Reference proteome; Repeat; Secreted; KW Signal; Steroid-binding. FT SIGNAL 1 29 {ECO:0000269|PubMed:3542030, FT ECO:0000269|PubMed:3702459}. FT CHAIN 30 402 Sex hormone-binding globulin. FT {ECO:0000269|PubMed:3542030}. FT /FTId=PRO_0000032557. FT DOMAIN 45 217 Laminin G-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT DOMAIN 224 390 Laminin G-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT CARBOHYD 36 36 O-linked (GalNAc...). FT {ECO:0000269|PubMed:1400872}. FT /FTId=CAR_000174. FT CARBOHYD 380 380 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:3542030}. FT CARBOHYD 396 396 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:1400872, FT ECO:0000269|PubMed:3542030}. FT DISULFID 193 217 {ECO:0000255|PROSITE-ProRule:PRU00122, FT ECO:0000269|PubMed:3542030}. FT DISULFID 362 390 {ECO:0000255|PROSITE-ProRule:PRU00122, FT ECO:0000269|PubMed:3542030}. FT VAR_SEQ 1 37 MESRGPLATSRLLLLLLLLLLRHTRQGWALRPVLPTQ -> FT PRFKGSPAVLFKLTYAVITCFSLRLTHPPRPW (in FT isoform 2). {ECO:0000305}. FT /FTId=VSP_006090. FT VAR_SEQ 186 203 Missing (in isoform 5). {ECO:0000305}. FT /FTId=VSP_045376. FT VAR_SEQ 239 353 Missing (in isoform 4). FT {ECO:0000303|Ref.7}. FT /FTId=VSP_045358. FT VAR_SEQ 285 293 KVVLSSGSG -> EKTLPPLFA (in isoform 2 and FT isoform 3). FT {ECO:0000303|PubMed:15028279}. FT /FTId=VSP_006091. FT VAR_SEQ 294 402 Missing (in isoform 2 and isoform 3). FT {ECO:0000303|PubMed:15028279}. FT /FTId=VSP_006092. FT VARIANT 22 22 R -> H (in dbSNP:rs9282845). FT /FTId=VAR_022002. FT VARIANT 25 25 R -> H (in dbSNP:rs6260). FT {ECO:0000269|PubMed:10391209}. FT /FTId=VAR_013946. FT VARIANT 185 185 P -> L (in dbSNP:rs6258). FT /FTId=VAR_016182. FT VARIANT 356 356 D -> N (polymorphism; generates a N- FT glycosylation site; dbSNP:rs6259). FT {ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:1400872, FT ECO:0000269|PubMed:7714097}. FT /FTId=VAR_013129. FT CONFLICT 22 22 R -> Q (in Ref. 5; CAA28987). FT {ECO:0000305}. FT CONFLICT 334 334 A -> L (in Ref. 2; AAC18778). FT {ECO:0000305}. FT CONFLICT 336 336 L -> S (in Ref. 2; AAC18778). FT {ECO:0000305}. FT STRAND 44 47 {ECO:0000244|PDB:1D2S}. FT STRAND 56 62 {ECO:0000244|PDB:1D2S}. FT HELIX 63 65 {ECO:0000244|PDB:1D2S}. FT STRAND 70 78 {ECO:0000244|PDB:1D2S}. FT STRAND 80 90 {ECO:0000244|PDB:1D2S}. FT TURN 91 93 {ECO:0000244|PDB:1D2S}. FT STRAND 94 101 {ECO:0000244|PDB:1D2S}. FT STRAND 104 113 {ECO:0000244|PDB:1D2S}. FT STRAND 115 119 {ECO:0000244|PDB:1D2S}. FT STRAND 126 128 {ECO:0000244|PDB:1D2S}. FT STRAND 130 137 {ECO:0000244|PDB:1D2S}. FT STRAND 140 145 {ECO:0000244|PDB:1D2S}. FT STRAND 148 153 {ECO:0000244|PDB:1D2S}. FT HELIX 160 162 {ECO:0000244|PDB:1LHU}. FT STRAND 167 174 {ECO:0000244|PDB:1D2S}. FT HELIX 179 181 {ECO:0000244|PDB:1D2S}. FT STRAND 182 184 {ECO:0000244|PDB:1D2S}. FT STRAND 192 200 {ECO:0000244|PDB:1D2S}. FT HELIX 202 204 {ECO:0000244|PDB:1D2S}. FT STRAND 205 209 {ECO:0000244|PDB:1D2S}. SQ SEQUENCE 402 AA; 43779 MW; 5A3B1885E4E7A460 CRC64; MESRGPLATS RLLLLLLLLL LRHTRQGWAL RPVLPTQSAH DPPAVHLSNG PGQEPIAVMT FDLTKITKTS SSFEVRTWDP EGVIFYGDTN PKDDWFMLGL RDGRPEIQLH NHWAQLTVGA GPRLDDGRWH QVEVKMEGDS VLLEVDGEEV LRLRQVSGPL TSKRHPIMRI ALGGLLFPAS NLRLPLVPAL DGCLRRDSWL DKQAEISASA PTSLRSCDVE SNPGIFLPPG TQAEFNLRDI PQPHAEPWAF SLDLGLKQAA GSGHLLALGT PENPSWLSLH LQDQKVVLSS GSGPGLDLPL VLGLPLQLKL SMSRVVLSQG SKMKALALPP LGLAPLLNLW AKPQGRLFLG ALPGEDSSTS FCLNGLWAQG QRLDVDQALN RSHEIWTHSC PQSPGNGTDA SH //