FCGRN_HUMAN
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 03-AUG-2022, entry version 188.
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}.
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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 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 AlphaFoldDB; P55899; -.
DR SASBDB; P55899; -.
DR SMR; P55899; -.
DR BioGRID; 108511; 121.
DR DIP; DIP-6165N; -.
DR IntAct; P55899; 64.
DR MINT; P55899; -.
DR STRING; 9606.ENSP00000221466; -.
DR BindingDB; P55899; -.
DR ChEMBL; CHEMBL5966; -.
DR DrugBank; DB15270; Efgartigimod alfa.
DR GuidetoPHARMACOLOGY; 2985; -.
DR GlyConnect; 1387; 2 N-Linked glycans (1 site).
DR GlyGen; P55899; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P55899; -.
DR PhosphoSitePlus; P55899; -.
DR BioMuta; FCGRT; -.
DR DMDM; 2497331; -.
DR EPD; P55899; -.
DR jPOST; P55899; -.
DR MassIVE; P55899; -.
DR MaxQB; P55899; -.
DR PaxDb; P55899; -.
DR PeptideAtlas; P55899; -.
DR PRIDE; P55899; -.
DR ProteomicsDB; 56878; -.
DR ABCD; P55899; 8 sequenced antibodies.
DR Antibodypedia; 1522; 314 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 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; ENSGT01040000240396; -.
DR InParanoid; P55899; -.
DR OMA; EGGFGPN; -.
DR OrthoDB; 912212at2759; -.
DR PhylomeDB; P55899; -.
DR TreeFam; TF336617; -.
DR PathwayCommons; P55899; -.
DR SignaLink; P55899; -.
DR BioGRID-ORCS; 2217; 12 hits in 1069 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 173 other tissues.
DR ExpressionAtlas; P55899; baseline and differential.
DR Genevisible; P55899; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 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 Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 1.
DR SMART; SM00407; IGc1; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00290; IG_MHC; 1.
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:6QIO"
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
