CD180_HUMAN
ID CD180_HUMAN Reviewed; 661 AA.
AC Q99467; B2R7Z7; Q32MM5;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=CD180 antigen;
DE AltName: Full=Lymphocyte antigen 64;
DE AltName: Full=Radioprotective 105 kDa protein;
DE AltName: CD_antigen=CD180;
DE Flags: Precursor;
GN Name=CD180; Synonyms=LY64, RP105;
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].
RC TISSUE=B-cell lymphoma;
RX PubMed=8975706; DOI=10.1006/geno.1996.0632;
RA Miura Y., Miyake K., Yamashita Y., Shimazu R., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Inazawa J., Abe T., Kimoto M.;
RT "Molecular cloning of a human RP105 homologue and chromosomal localization
RT of the mouse and human RP105 genes (Ly64 and LY64).";
RL Genomics 38:299-304(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
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 [7]
RP INTERACTION WITH LY86.
RX PubMed=9763566;
RA Miura Y., Shimazu R., Miyake K., Akashi S., Ogata H., Yamashita Y.,
RA Narisawa Y., Kimoto M.;
RT "RP105 is associated with MD-1 and transmits an activation signal in human
RT B cells.";
RL Blood 92:2815-2822(1998).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78.
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 multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 24-626 IN COMPLEX WITH LY86,
RP SUBUNIT, AND GLYCOSYLATION AT ASN-402 AND ASN-451.
RX PubMed=21959264; DOI=10.1016/j.jmb.2011.09.020;
RA Ohto U., Miyake K., Shimizu T.;
RT "Crystal structures of mouse and human RP105/MD-1 complexes reveal unique
RT dimer organization of the toll-like receptor family.";
RL J. Mol. Biol. 413:815-825(2011).
CC -!- FUNCTION: May cooperate with MD-1 and TLR4 to mediate the innate immune
CC response to bacterial lipopolysaccharide (LPS) in B-cells. Leads to NF-
CC kappa-B activation. Also involved in the life/death decision of B-cells
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: M-shaped tetramer of two CD180-LY86 heterodimers.
CC {ECO:0000269|PubMed:21959264}.
CC -!- INTERACTION:
CC Q99467; O95711: LY86; NbExp=3; IntAct=EBI-15940363, EBI-12203791;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Expressed mainly on mature peripherical B cells.
CC Detected in spleen, lymph node and appendix. Not detected in pre-B and
CC -T cells.
CC -!- SIMILARITY: Belongs to the Toll-like receptor family. {ECO:0000305}.
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DR EMBL; D83597; BAA12019.1; -; mRNA.
DR EMBL; AK313177; BAG35994.1; -; mRNA.
DR EMBL; AC026445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471137; EAW51318.1; -; Genomic_DNA.
DR EMBL; BC109069; AAI09070.1; -; mRNA.
DR EMBL; BC109070; AAI09071.1; -; mRNA.
DR CCDS; CCDS3992.1; -.
DR RefSeq; NP_005573.2; NM_005582.2.
DR PDB; 3B2D; X-ray; 2.80 A; A/B=24-626.
DR PDBsum; 3B2D; -.
DR AlphaFoldDB; Q99467; -.
DR SMR; Q99467; -.
DR BioGRID; 110242; 1.
DR DIP; DIP-59104N; -.
DR IntAct; Q99467; 1.
DR STRING; 9606.ENSP00000256447; -.
DR GlyGen; Q99467; 11 sites.
DR iPTMnet; Q99467; -.
DR PhosphoSitePlus; Q99467; -.
DR BioMuta; CD180; -.
DR DMDM; 296434437; -.
DR EPD; Q99467; -.
DR jPOST; Q99467; -.
DR MassIVE; Q99467; -.
DR MaxQB; Q99467; -.
DR PaxDb; Q99467; -.
DR PeptideAtlas; Q99467; -.
DR PRIDE; Q99467; -.
DR ProteomicsDB; 78284; -.
DR Antibodypedia; 1122; 436 antibodies from 38 providers.
DR DNASU; 4064; -.
DR Ensembl; ENST00000256447.5; ENSP00000256447.4; ENSG00000134061.5.
DR GeneID; 4064; -.
DR KEGG; hsa:4064; -.
DR MANE-Select; ENST00000256447.5; ENSP00000256447.4; NM_005582.3; NP_005573.2.
DR UCSC; uc003juy.3; human.
DR CTD; 4064; -.
DR DisGeNET; 4064; -.
DR GeneCards; CD180; -.
DR HGNC; HGNC:6726; CD180.
DR HPA; ENSG00000134061; Tissue enhanced (lymphoid).
DR MIM; 602226; gene.
DR neXtProt; NX_Q99467; -.
DR OpenTargets; ENSG00000134061; -.
DR PharmGKB; PA30490; -.
DR VEuPathDB; HostDB:ENSG00000134061; -.
DR eggNOG; KOG4641; Eukaryota.
DR GeneTree; ENSGT00940000161183; -.
DR HOGENOM; CLU_006000_5_1_1; -.
DR InParanoid; Q99467; -.
DR OMA; MCTEKEA; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q99467; -.
DR TreeFam; TF351113; -.
DR PathwayCommons; Q99467; -.
DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR SignaLink; Q99467; -.
DR BioGRID-ORCS; 4064; 9 hits in 1065 CRISPR screens.
DR ChiTaRS; CD180; human.
DR GeneWiki; CD180; -.
DR GenomeRNAi; 4064; -.
DR Pharos; Q99467; Tbio.
DR PRO; PR:Q99467; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q99467; protein.
DR Bgee; ENSG00000134061; Expressed in pancreatic ductal cell and 116 other tissues.
DR Genevisible; Q99467; HS.
DR GO; GO:0031012; C:extracellular matrix; 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:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0002322; P:B cell proliferation involved in immune response; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IGI:MGI.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR041281; LRR_11.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF18831; LRR_11; 1.
DR Pfam; PF13855; LRR_8; 3.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00082; LRRCT; 1.
DR PROSITE; PS51450; LRR; 12.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Glycoprotein;
KW Immunity; Inflammatory response; Innate immunity; Leucine-rich repeat;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 24..661
FT /note="CD180 antigen"
FT /id="PRO_0000034741"
FT TOPO_DOM 24..626
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 627..650
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 651..661
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..53
FT /note="LRRNT"
FT REPEAT 54..75
FT /note="LRR 1"
FT REPEAT 78..99
FT /note="LRR 2"
FT REPEAT 102..123
FT /note="LRR 3"
FT REPEAT 126..147
FT /note="LRR 4"
FT REPEAT 150..171
FT /note="LRR 5"
FT REPEAT 174..195
FT /note="LRR 6"
FT REPEAT 201..221
FT /note="LRR 7"
FT REPEAT 275..296
FT /note="LRR 8"
FT REPEAT 299..320
FT /note="LRR 9"
FT REPEAT 322..343
FT /note="LRR 10"
FT REPEAT 346..366
FT /note="LRR 11"
FT REPEAT 371..391
FT /note="LRR 12"
FT REPEAT 397..418
FT /note="LRR 13"
FT REPEAT 421..442
FT /note="LRR 14"
FT REPEAT 446..466
FT /note="LRR 15"
FT REPEAT 470..493
FT /note="LRR 16"
FT REPEAT 497..518
FT /note="LRR 17"
FT REPEAT 521..544
FT /note="LRR 18"
FT REPEAT 546..564
FT /note="LRR 19"
FT DOMAIN 577..627
FT /note="LRRCT"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21959264"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:21959264"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 20
FT /note="V -> L (in dbSNP:rs5744463)"
FT /id="VAR_057298"
FT VARIANT 53
FT /note="N -> K (in dbSNP:rs16875312)"
FT /id="VAR_021978"
FT VARIANT 99
FT /note="S -> R (in dbSNP:rs2230520)"
FT /id="VAR_021979"
FT VARIANT 259
FT /note="D -> N (in dbSNP:rs5744525)"
FT /id="VAR_057299"
FT VARIANT 356
FT /note="V -> M (in dbSNP:rs56752081)"
FT /id="VAR_061859"
FT VARIANT 430
FT /note="T -> A (in dbSNP:rs2230523)"
FT /id="VAR_057300"
FT VARIANT 648
FT /note="F -> L (in dbSNP:rs2230524)"
FT /id="VAR_057301"
FT CONFLICT 223
FT /note="I -> V (in Ref. 1; BAA12019, 2; BAG35994, 4;
FT EAW51318 and 5; AAI09070/AAI09071)"
FT /evidence="ECO:0000305"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 70..75
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 94..99
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:3B2D"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3B2D"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 195..198
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 200..205
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 216..221
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:3B2D"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:3B2D"
FT HELIX 269..273
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 291..294
FT /evidence="ECO:0007829|PDB:3B2D"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:3B2D"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:3B2D"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 365..368
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 384..388
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 400..402
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 413..418
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 440..443
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 462..467
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:3B2D"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:3B2D"
FT HELIX 491..494
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 513..518
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:3B2D"
FT HELIX 534..540
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:3B2D"
FT HELIX 563..567
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:3B2D"
FT HELIX 583..585
FT /evidence="ECO:0007829|PDB:3B2D"
FT HELIX 586..594
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:3B2D"
FT STRAND 607..613
FT /evidence="ECO:0007829|PDB:3B2D"
FT TURN 618..620
FT /evidence="ECO:0007829|PDB:3B2D"
SQ SEQUENCE 661 AA; 74179 MW; 93DE3178594B3383 CRC64;
MAFDVSCFFW VVLFSAGCKV ITSWDQMCIE KEANKTYNCE NLGLSEIPDT LPNTTEFLEF
SFNFLPTIHN RTFSRLMNLT FLDLTRCQIN WIHEDTFQSH HQLSTLVLTG NPLIFMAETS
LNGPKSLKHL FLIQTGISNL EFIPVHNLEN LESLYLGSNH ISSIKFPKDF PARNLKVLDF
QNNAIHYISR EDMRSLEQAI NLSLNFNGNN VKGIELGAFD STIFQSLNFG GTPNLSVIFN
GLQNSTTQSL WLGTFEDIDD EDISSAMLKG LCEMSVESLN LQEHRFSDIS STTFQCFTQL
QELDLTATHL KGLPSGMKGL NLLKKLVLSV NHFDQLCQIS AANFPSLTHL YIRGNVKKLH
LGVGCLEKLG NLQTLDLSHN DIEASDCCSL QLKNLSHLQT LNLSHNEPLG LQSQAFKECP
QLELLDLAFT RLHINAPQSP FQNLHFLQVL NLTYCFLDTS NQHLLAGLPV LRHLNLKGNH
FQDGTITKTN LLQTVGSLEV LILSSCGLLS IDQQAFHSLG KMSHVDLSHN SLTCDSIDSL
SHLKGIYLNL AANSINIISP RLLPILSQQS TINLSHNPLD CTCSNIHFLT WYKENLHKLE
GSEETTCANP PSLRGVKLSD VKLSCGITAI GIFFLIVFLL LLAILLFFAV KYLLRWKYQH
I
