ID FCGRN_HUMAN Reviewed; 365 AA. AC P55899; Q5HYM5; Q9HBV7; Q9NZ19; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 197. DE RecName: Full=IgG receptor FcRn large subunit p51; DE Short=FcRn; DE AltName: Full=IgG Fc fragment receptor transporter alpha chain; DE AltName: Full=Neonatal Fc receptor; DE Flags: Precursor; GN Name=FCGRT; Synonyms=FCRN; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Placenta; RX PubMed=7964511; DOI=10.1084/jem.180.6.2377; RA Story C.M., Mikulska J., Simister N.E.; RT "A major histocompatibility complex class I-like Fc receptor cloned from RT human placenta: possible role in transfer of immunoglobulin G from mother RT to fetus."; RL J. Exp. Med. 180:2377-2381(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Tiwari B., Junghans R.P.; RT "Partial sequence of the human fcgrt gene and its 5' upstream region."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10998088; DOI=10.1046/j.1365-2370.2000.00225.x; RA Mikulska J.E., Pablo L., Canel J., Simister N.E.; RT "Cloning and analysis of the gene encoding the human neonatal Fc RT receptor."; RL Eur. J. Immunogenet. 27:231-240(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Rectum tumor; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [7] RP PROTEIN SEQUENCE OF 24-38. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally verified RT cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [8] RP FUNCTION. RX PubMed=12578848; DOI=10.1093/intimm/dxg018; RA Ward E.S., Zhou J., Ghetie V., Ober R.J.; RT "Evidence to support the cellular mechanism involved in serum IgG RT homeostasis in humans."; RL Int. Immunol. 15:187-195(2003). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [12] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH ECHOVIRUS 11 AND RP ECHOVIRUS 30 PROTEIN VP1 (MICROBIAL INFECTION). RX PubMed=30808762; DOI=10.1073/pnas.1817341116; RA Morosky S., Wells A.I., Lemon K., Evans A.S., Schamus S., Bakkenist C.J., RA Coyne C.B.; RT "The neonatal Fc receptor is a pan-echovirus receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 116:3758-3763(2019). RN [13] RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), FUNCTION (MICROBIAL RP INFECTION), SUBCELLULAR LOCATION, AND INTERACTION WITH ECHOVIRUS 6 PROTEIN RP VP1 (MICROBIAL INFECTION). RX PubMed=31104841; DOI=10.1016/j.cell.2019.04.035; RA Zhao X., Zhang G., Liu S., Chen X., Peng R., Dai L., Qu X., Li S., Song H., RA Gao Z., Yuan P., Liu Z., Li C., Shang Z., Li Y., Zhang M., Qi J., Wang H., RA Du N., Wu Y., Bi Y., Gao S., Shi Y., Yan J., Zhang Y., Xie Z., Wei W., RA Gao G.F.; RT "Human Neonatal Fc Receptor Is the Cellular Uncoating Receptor for RT Enterovirus B."; RL Cell 177:1553-1565.E16(2019). RN [14] {ECO:0007744|PDB:1EXU} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 24-290, FUNCTION, AND DISULFIDE RP BONDS. RX PubMed=10933786; DOI=10.1021/bi000749m; RA West A.P. Jr., Bjorkman P.J.; RT "Crystal structure and immunoglobulin G binding properties of the human RT major histocompatibility complex-related Fc receptor."; RL Biochemistry 39:9698-9708(2000). RN [15] {ECO:0007744|PDB:4N0F, ECO:0007744|PDB:4N0U} RP X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) OF 27-290, FUNCTION, INTERACTION RP WITH ALB, AND DISULFIDE BOND. RX PubMed=24469444; DOI=10.1074/jbc.m113.537563; RA Oganesyan V., Damschroder M.M., Cook K.E., Li Q., Gao C., Wu H., RA Dall'Acqua W.F.; RT "Structural insights into neonatal Fc receptor-based recycling RT mechanisms."; RL J. Biol. Chem. 289:7812-7824(2014). RN [16] {ECO:0007744|PDB:5BJT} RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 24-290, INTERACTION WITH ALB, RP FUNCTION, DISULFIDE BOND, AND TISSUE SPECIFICITY. RX PubMed=28330995; DOI=10.1073/pnas.1618291114; RA Pyzik M., Rath T., Kuo T.T., Win S., Baker K., Hubbard J.J., Grenha R., RA Gandhi A., Kraemer T.D., Mezo A.R., Taylor Z.S., McDonnell K., Nienaber V., RA Andersen J.T., Mizoguchi A., Blumberg L., Purohit S., Jones S.D., RA Christianson G., Lencer W.I., Sandlie I., Kaplowitz N., Roopenian D.C., RA Blumberg R.S.; RT "Hepatic FcRn regulates albumin homeostasis and susceptibility to liver RT injury."; RL Proc. Natl. Acad. Sci. U.S.A. 114:E2862-E2871(2017). CC -!- FUNCTION: Cell surface receptor that transfers passive humoral immunity CC from the mother to the newborn. Binds to the Fc region of monomeric CC immunoglobulin gamma and mediates its selective uptake from milk CC (PubMed:7964511, PubMed:10933786). IgG in the milk is bound at the CC apical surface of the intestinal epithelium. The resultant FcRn-IgG CC complexes are transcytosed across the intestinal epithelium and IgG is CC released from FcRn into blood or tissue fluids. Throughout life, CC contributes to effective humoral immunity by recycling IgG and CC extending its half-life in the circulation. Mechanistically, monomeric CC IgG binding to FcRn in acidic endosomes of endothelial and CC hematopoietic cells recycles IgG to the cell surface where it is CC released into the circulation (PubMed:10998088). In addition of IgG, CC regulates homeostasis of the other most abundant circulating protein CC albumin/ALB (PubMed:24469444, PubMed:28330995). CC {ECO:0000250|UniProtKB:P13599, ECO:0000269|PubMed:10933786, CC ECO:0000269|PubMed:10998088, ECO:0000269|PubMed:24469444, CC ECO:0000269|PubMed:28330995, ECO:0000269|PubMed:7964511}. CC -!- FUNCTION: (Microbial infection) Acts as an uncoating receptor for a CC panel of echoviruses including Echovirus 5, 6, 7, 9, 11, 13, 25 and 29. CC {ECO:0000269|PubMed:30808762, ECO:0000269|PubMed:31104841}. CC -!- SUBUNIT: FcRn complex consists of two subunits: p51, and p14 which is CC equivalent to beta-2-microglobulin. It forms an MHC class I-like CC heterodimer (By similarity). Interacts with albumin/ALB; this CC interaction regulates ALB homeostasis (PubMed:24469444, CC PubMed:28330995). {ECO:0000250|UniProtKB:P13599, CC ECO:0000269|PubMed:24469444, ECO:0000269|PubMed:28330995}. CC -!- SUBUNIT: (Microbial infection) Interacts with Echovirus 6, Echovirus 11 CC and Echovirus 30 capsid protein VP1. {ECO:0000269|PubMed:30808762, CC ECO:0000269|PubMed:31104841}. CC -!- INTERACTION: CC P55899; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-2833934, EBI-12256978; CC P55899; Q92520: FAM3C; NbExp=3; IntAct=EBI-2833934, EBI-2876774; CC P55899; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-2833934, EBI-10317425; CC P55899; Q01453: PMP22; NbExp=3; IntAct=EBI-2833934, EBI-2845982; CC P55899; O00526: UPK2; NbExp=3; IntAct=EBI-2833934, EBI-10179682; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P13599}; CC Single-pass type I membrane protein {ECO:0000255}. Endosome membrane CC {ECO:0000269|PubMed:31104841}. CC -!- TISSUE SPECIFICITY: Expressed in full-term placenta, heart, lung, CC liver, muscle, kidney, pancreas, and both fetal and adult small CC intestine. {ECO:0000269|PubMed:28330995, ECO:0000269|PubMed:7964511}. CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}. 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; U12255; AAA58958.1; -; mRNA. DR EMBL; AF220542; AAF72596.1; -; Genomic_DNA. DR EMBL; AF200220; AAG31421.1; -; Genomic_DNA. DR EMBL; AF200219; AAG31421.1; JOINED; Genomic_DNA. DR EMBL; BX647163; CAI46032.1; -; mRNA. DR EMBL; CH471177; EAW52498.1; -; Genomic_DNA. DR EMBL; BC008734; AAH08734.1; -; mRNA. DR CCDS; CCDS12770.1; -. DR PIR; I38720; I38720. DR RefSeq; NP_001129491.1; NM_001136019.2. DR RefSeq; NP_004098.1; NM_004107.4. DR PDB; 1EXU; X-ray; 2.70 A; A=24-290. DR PDB; 3M17; X-ray; 2.60 A; A/C/E/G=24-290. DR PDB; 3M1B; X-ray; 3.10 A; A/C/E/G=24-290. DR PDB; 4K71; X-ray; 2.40 A; B/E=24-297. DR PDB; 4N0F; X-ray; 3.02 A; A/E/H/K=27-297. DR PDB; 4N0U; X-ray; 3.80 A; A=27-290. DR PDB; 5BJT; X-ray; 3.20 A; A/C/E/G=24-290. DR PDB; 5BXF; X-ray; 2.85 A; A/C=1-290. DR PDB; 5WHK; X-ray; 2.50 A; A=1-297. DR PDB; 6C97; X-ray; 2.00 A; A/C=24-297. DR PDB; 6C98; X-ray; 1.85 A; A/C=24-297. DR PDB; 6C99; X-ray; 2.00 A; A/C=24-297. DR PDB; 6FGB; X-ray; 2.90 A; A=24-365. DR PDB; 6ILM; EM; 3.40 A; E=28-290. DR PDB; 6LA6; EM; 2.39 A; E=28-290. DR PDB; 6LA7; EM; 2.82 A; E=28-290. DR PDB; 6NHA; X-ray; 2.38 A; A=24-296. DR PDB; 6QIO; X-ray; 1.95 A; B=24-297. DR PDB; 6QIP; X-ray; 2.45 A; B=24-297. DR PDB; 6WNA; X-ray; 2.40 A; A=27-290. DR PDB; 6WOL; X-ray; 2.49 A; A=24-290. DR PDB; 7B5F; EM; 2.90 A; G=24-290. DR PDB; 7C9V; EM; 3.30 A; E=28-290. DR PDB; 7Q15; X-ray; 3.30 A; A/C=1-297. DR PDB; 7XXA; EM; 3.09 A; E=28-290. DR PDBsum; 1EXU; -. DR PDBsum; 3M17; -. DR PDBsum; 3M1B; -. DR PDBsum; 4K71; -. DR PDBsum; 4N0F; -. DR PDBsum; 4N0U; -. DR PDBsum; 5BJT; -. DR PDBsum; 5BXF; -. DR PDBsum; 5WHK; -. DR PDBsum; 6C97; -. DR PDBsum; 6C98; -. DR PDBsum; 6C99; -. DR PDBsum; 6FGB; -. DR PDBsum; 6ILM; -. DR PDBsum; 6LA6; -. DR PDBsum; 6LA7; -. DR PDBsum; 6NHA; -. DR PDBsum; 6QIO; -. DR PDBsum; 6QIP; -. DR PDBsum; 6WNA; -. DR PDBsum; 6WOL; -. DR PDBsum; 7B5F; -. DR PDBsum; 7C9V; -. DR PDBsum; 7Q15; -. DR PDBsum; 7XXA; -. DR AlphaFoldDB; P55899; -. DR EMDB; EMD-0857; -. DR EMDB; EMD-0858; -. DR EMDB; EMD-12028; -. DR EMDB; EMD-30318; -. DR EMDB; EMD-33499; -. DR EMDB; EMD-9687; -. DR SASBDB; P55899; -. DR SMR; P55899; -. DR BioGRID; 108511; 123. DR DIP; DIP-6165N; -. DR IntAct; P55899; 64. DR MINT; P55899; -. DR STRING; 9606.ENSP00000410798; -. DR BindingDB; P55899; -. DR ChEMBL; CHEMBL5966; -. DR DrugBank; DB15270; Efgartigimod alfa. DR GuidetoPHARMACOLOGY; 2985; -. DR TCDB; 9.A.75.1.4; the mhc ii receptor (mhc2r) family. DR GlyConnect; 1387; 2 N-Linked glycans (1 site). DR GlyCosmos; P55899; 2 sites, 2 glycans. DR GlyGen; P55899; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; P55899; -. DR PhosphoSitePlus; P55899; -. DR SwissPalm; P55899; -. DR BioMuta; FCGRT; -. DR DMDM; 2497331; -. DR EPD; P55899; -. DR jPOST; P55899; -. DR MassIVE; P55899; -. DR MaxQB; P55899; -. DR PaxDb; 9606-ENSP00000221466; -. DR PeptideAtlas; P55899; -. DR ProteomicsDB; 56878; -. DR ABCD; P55899; 8 sequenced antibodies. DR Antibodypedia; 1522; 429 antibodies from 31 providers. DR DNASU; 2217; -. DR Ensembl; ENST00000221466.10; ENSP00000221466.4; ENSG00000104870.13. DR Ensembl; ENST00000426395.7; ENSP00000410798.2; ENSG00000104870.13. DR GeneID; 2217; -. DR KEGG; hsa:2217; -. DR MANE-Select; ENST00000221466.10; ENSP00000221466.4; NM_001136019.3; NP_001129491.1. DR UCSC; uc002poe.3; human. DR AGR; HGNC:3621; -. DR CTD; 2217; -. DR DisGeNET; 2217; -. DR GeneCards; FCGRT; -. DR HGNC; HGNC:3621; FCGRT. DR HPA; ENSG00000104870; Low tissue specificity. DR MIM; 601437; gene. DR neXtProt; NX_P55899; -. DR OpenTargets; ENSG00000104870; -. DR PharmGKB; PA28067; -. DR VEuPathDB; HostDB:ENSG00000104870; -. DR eggNOG; ENOG502RTZ5; Eukaryota. DR GeneTree; ENSGT01100000263475; -. DR InParanoid; P55899; -. DR OMA; TWDGDWP; -. DR OrthoDB; 3840485at2759; -. DR PhylomeDB; P55899; -. DR TreeFam; TF336617; -. DR PathwayCommons; P55899; -. DR SignaLink; P55899; -. DR BioGRID-ORCS; 2217; 13 hits in 1147 CRISPR screens. DR ChiTaRS; FCGRT; human. DR EvolutionaryTrace; P55899; -. DR GeneWiki; FCGRT; -. DR GenomeRNAi; 2217; -. DR Pharos; P55899; Tclin. DR PRO; PR:P55899; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P55899; Protein. DR Bgee; ENSG00000104870; Expressed in mucosa of transverse colon and 175 other cell types or tissues. DR ExpressionAtlas; P55899; baseline and differential. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0030881; F:beta-2-microglobulin binding; IBA:GO_Central. DR GO; GO:0019864; F:IgG binding; IDA:UniProtKB. DR GO; GO:0002416; P:IgG immunoglobulin transcytosis in epithelial cells mediated by FcRn immunoglobulin receptor; NAS:UniProtKB. DR GO; GO:0006955; P:immune response; IBA:GO_Central. DR CDD; cd21011; IgC1_MHC-like_FcRn; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR Gene3D; 3.30.500.10; MHC class I-like antigen recognition-like; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011161; MHC_I-like_Ag-recog. DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR PANTHER; PTHR16675:SF3; IGG RECEPTOR FCRN LARGE SUBUNIT P51; 1. DR PANTHER; PTHR16675; MHC CLASS I-RELATED; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00129; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR SUPFAM; SSF54452; MHC antigen-recognition domain; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. DR Genevisible; P55899; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond; KW Endosome; Glycoprotein; IgG-binding protein; Immunoglobulin domain; KW Membrane; Phosphoprotein; Receptor; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..23 FT /evidence="ECO:0000269|PubMed:15340161" FT CHAIN 24..365 FT /note="IgG receptor FcRn large subunit p51" FT /evidence="ECO:0000269|PubMed:15340161" FT /id="PRO_0000015157" FT TOPO_DOM 24..297 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 298..321 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 322..365 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 202..289 FT /note="Ig-like C1-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT REGION 24..110 FT /note="Alpha-1" FT /evidence="ECO:0000269|PubMed:10933786, FT ECO:0007744|PDB:1EXU" FT REGION 111..200 FT /note="Alpha-2" FT /evidence="ECO:0000269|PubMed:10933786, FT ECO:0007744|PDB:1EXU" FT REGION 201..290 FT /note="Alpha-3" FT /evidence="ECO:0000269|PubMed:10933786, FT ECO:0007744|PDB:1EXU" FT REGION 291..297 FT /note="Connecting peptide" FT MOD_RES 334 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT CARBOHYD 125 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 119..182 FT /evidence="ECO:0000269|PubMed:10933786, FT ECO:0000269|PubMed:24469444, ECO:0000269|PubMed:28330995, FT ECO:0007744|PDB:1EXU, ECO:0007744|PDB:4N0F, FT ECO:0007744|PDB:4N0U, ECO:0007744|PDB:5BJT" FT DISULFID 221..275 FT /evidence="ECO:0000269|PubMed:10933786, FT ECO:0000269|PubMed:24469444, ECO:0000269|PubMed:28330995, FT ECO:0007744|PDB:1EXU, ECO:0007744|PDB:4N0F, FT ECO:0007744|PDB:4N0U, ECO:0007744|PDB:5BJT" FT CONFLICT 101..103 FT /note="Missing (in Ref. 3; AAG31421)" FT /evidence="ECO:0000305" FT CONFLICT 201 FT /note="E -> G (in Ref. 2; AAF72596)" FT /evidence="ECO:0000305" FT STRAND 29..39 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 46..53 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 56..62 FT /evidence="ECO:0007829|PDB:6C98" FT TURN 63..65 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:6ILM" FT HELIX 72..76 FT /evidence="ECO:0007829|PDB:6C98" FT TURN 80..82 FT /evidence="ECO:0007829|PDB:6LA6" FT HELIX 83..104 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 107..109 FT /evidence="ECO:0007829|PDB:6WNA" FT STRAND 112..121 FT /evidence="ECO:0007829|PDB:6C98" FT HELIX 123..125 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 127..135 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 138..144 FT /evidence="ECO:0007829|PDB:6C98" FT TURN 145..148 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:6C98" FT HELIX 155..166 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:6FGB" FT HELIX 170..179 FT /evidence="ECO:0007829|PDB:6C98" FT HELIX 181..192 FT /evidence="ECO:0007829|PDB:6C98" FT HELIX 194..197 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 204..211 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 213..215 FT /evidence="ECO:0007829|PDB:3M1B" FT STRAND 216..229 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 231..237 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 240..243 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 246..251 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 253..255 FT /evidence="ECO:0007829|PDB:6FGB" FT STRAND 257..266 FT /evidence="ECO:0007829|PDB:6C98" FT TURN 267..269 FT /evidence="ECO:0007829|PDB:5BJT" FT HELIX 270..272 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 273..279 FT /evidence="ECO:0007829|PDB:6C98" FT STRAND 282..284 FT /evidence="ECO:0007829|PDB:6C97" FT STRAND 286..288 FT /evidence="ECO:0007829|PDB:6C98" SQ SEQUENCE 365 AA; 39743 MW; C886C6A1F66A0D89 CRC64; MGVPRPQPWA LGLLLFLLPG SLGAESHLSL LYHLTAVSSP APGTPAFWVS GWLGPQQYLS YNSLRGEAEP CGAWVWENQV SWYWEKETTD LRIKEKLFLE AFKALGGKGP YTLQGLLGCE LGPDNTSVPT AKFALNGEEF MNFDLKQGTW GGDWPEALAI SQRWQQQDKA ANKELTFLLF SCPHRLREHL ERGRGNLEWK EPPSMRLKAR PSSPGFSVLT CSAFSFYPPE LQLRFLRNGL AAGTGQGDFG PNSDGSFHAS SSLTVKSGDE HHYCCIVQHA GLAQPLRVEL ESPAKSSVLV VGIVIGVLLL TAAAVGGALL WRRMRSGLPA PWISLRGDDT GVLLPTPGEA QDADLKDVNV IPATA //