LY75_HUMAN
ID LY75_HUMAN Reviewed; 1722 AA.
AC O60449; O75913; Q53R46; Q53TF5; Q7Z575; Q7Z577;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Lymphocyte antigen 75;
DE Short=Ly-75;
DE AltName: Full=C-type lectin domain family 13 member B;
DE AltName: Full=DEC-205;
DE AltName: Full=gp200-MR6;
DE AltName: CD_antigen=CD205;
DE Flags: Precursor;
GN Name=LY75; Synonyms=CD205, CLEC13B;
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 {ECO:0000312|EMBL:AAC17636.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), PARTIAL PROTEIN SEQUENCE, TISSUE
RP SPECIFICITY, GLYCOSYLATION, AND VARIANTS ASP-268 AND GLU-807.
RC TISSUE=Thymus;
RX PubMed=9862343;
RX DOI=10.1002/(sici)1521-4141(199812)28:12<4071::aid-immu4071>3.0.co;2-o;
RA McKay P.F., Imami N., Johns M., Taylor-Fishwick D.A., Sedibane L.M.,
RA Totty N.F., Hsuan J.J., Palmer D.B., George A.J.T., Foxwell B.M.J.,
RA Ritter M.A.;
RT "The gp200-MR6 molecule which is functionally associated with the IL-4
RT receptor modulates B cell phenotype and is a novel member of the human
RT macrophage mannose receptor family.";
RL Eur. J. Immunol. 28:4071-4083(1998).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT ASN-1321.
RX PubMed=9553150; DOI=10.1007/s002510050381;
RA Kato M., Neil T.K., Clark G.J., Morris C.M., Sorg R.V., Hart D.N.J.;
RT "cDNA cloning of human DEC-205, a putative antigen-uptake receptor on
RT dendritic cells.";
RL Immunogenetics 47:442-450(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY, AND
RP VARIANT ASN-1321.
RX PubMed=12824192; DOI=10.1074/jbc.m303112200;
RA Kato M., Khan S., Gonzalez N., O'Neill B.P., McDonald K.J., Cooper B.J.,
RA Angel N.Z., Hart D.N.J.;
RT "Hodgkin's lymphoma cell lines express a fusion protein encoded by
RT intergenically spliced mRNA for the multilectin receptor DEC-205 (CD205)
RT and a novel C-type lectin receptor DCL-1.";
RL J. Biol. Chem. 278:34035-34041(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-933, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC -!- FUNCTION: Acts as an endocytic receptor to direct captured antigens
CC from the extracellular space to a specialized antigen-processing
CC compartment (By similarity). Causes reduced proliferation of B-
CC lymphocytes. {ECO:0000250}.
CC -!- INTERACTION:
CC O60449-3; Q969F0: FATE1; NbExp=3; IntAct=EBI-10186753, EBI-743099;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=4;
CC IsoId=O60449-1; Sequence=Displayed;
CC Name=2; Synonyms=Fusion protein variant V34-2;
CC IsoId=O60449-2; Sequence=VSP_020909;
CC Name=5;
CC IsoId=Q8IX05-2; Sequence=External;
CC Name=3; Synonyms=Fusion protein variant V33-2;
CC IsoId=O60449-3; Sequence=VSP_020908;
CC Name=1;
CC IsoId=Q8IX05-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Expressed in spleen, thymus, colon and peripheral
CC blood lymphocytes. Detected in myeloid and B-lymphoid cell lines.
CC Isoform 2 and isoform 3 are expressed in malignant Hodgkin lymphoma
CC cells called Hodgkin and Reed-Sternberg (HRS) cells.
CC {ECO:0000269|PubMed:12824192, ECO:0000269|PubMed:9862343}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9862343}.
CC -!- MISCELLANEOUS: Isoform 2 and isoform 3 are produced in HRS cells by a
CC transcriptional control mechanism which cotranscribe an mRNA containing
CC LY75 and CD302 prior to generating the intergenically spliced mRNA to
CC produce LY75/CD302 fusion proteins.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by intergenic splicing of LY75 and
CC CD302. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by intergenic splicing of LY75 and
CC CD302. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=DEC-205;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_250";
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DR EMBL; AF064827; AAC62622.1; -; mRNA.
DR EMBL; AF011333; AAC17636.1; -; mRNA.
DR EMBL; AY184222; AAN85434.1; -; mRNA.
DR EMBL; AY314006; AAP79899.1; -; mRNA.
DR EMBL; AC009961; AAY14943.1; -; Genomic_DNA.
DR EMBL; AC093873; AAY24189.1; -; Genomic_DNA.
DR CCDS; CCDS2211.1; -. [O60449-1]
DR RefSeq; NP_001185688.1; NM_001198759.1. [O60449-2]
DR RefSeq; NP_001185689.1; NM_001198760.1. [O60449-3]
DR RefSeq; NP_002340.2; NM_002349.3. [O60449-1]
DR PDB; 7JPT; EM; 3.20 A; A=30-1722.
DR PDB; 7JPU; EM; 5.00 A; A/B/C/D=1-1722.
DR PDBsum; 7JPT; -.
DR PDBsum; 7JPU; -.
DR AlphaFoldDB; O60449; -.
DR SMR; O60449; -.
DR IntAct; O60449; 3.
DR STRING; 9606.ENSP00000263636; -.
DR CarbonylDB; O60449; -.
DR GlyConnect; 1472; 1 N-Linked glycan (1 site).
DR GlyGen; O60449; 21 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; O60449; -.
DR PhosphoSitePlus; O60449; -.
DR BioMuta; LY75; -.
DR EPD; O60449; -.
DR jPOST; O60449; -.
DR MassIVE; O60449; -.
DR MaxQB; O60449; -.
DR PaxDb; O60449; -.
DR PeptideAtlas; O60449; -.
DR PRIDE; O60449; -.
DR ProteomicsDB; 49406; -. [O60449-1]
DR ProteomicsDB; 49407; -. [O60449-2]
DR ProteomicsDB; 49408; -. [O60449-3]
DR ABCD; O60449; 1 sequenced antibody.
DR Antibodypedia; 3669; 561 antibodies from 41 providers.
DR CPTC; O60449; 1 antibody.
DR DNASU; 4065; -.
DR Ensembl; ENST00000263636.5; ENSP00000263636.4; ENSG00000054219.11. [O60449-1]
DR GeneID; 100526664; -.
DR GeneID; 4065; -.
DR KEGG; hsa:100526664; -.
DR KEGG; hsa:4065; -.
DR MANE-Select; ENST00000263636.5; ENSP00000263636.4; NM_002349.4; NP_002340.2.
DR UCSC; uc002ubc.6; human. [O60449-1]
DR CTD; 100526664; -.
DR CTD; 4065; -.
DR DisGeNET; 100526664; -.
DR DisGeNET; 4065; -.
DR GeneCards; LY75; -.
DR HGNC; HGNC:6729; LY75.
DR HPA; ENSG00000054219; Tissue enriched (lymphoid).
DR MIM; 604524; gene.
DR neXtProt; NX_O60449; -.
DR OpenTargets; ENSG00000054219; -.
DR OpenTargets; ENSG00000248672; -.
DR PharmGKB; PA30493; -.
DR VEuPathDB; HostDB:ENSG00000054219; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT01050000244842; -.
DR HOGENOM; CLU_002069_2_0_1; -.
DR InParanoid; O60449; -.
DR OMA; KTADCND; -.
DR OrthoDB; 29241at2759; -.
DR PhylomeDB; O60449; -.
DR TreeFam; TF316663; -.
DR PathwayCommons; O60449; -.
DR SignaLink; O60449; -.
DR BioGRID-ORCS; 100526664; 32 hits in 618 CRISPR screens.
DR BioGRID-ORCS; 4065; 12 hits in 1017 CRISPR screens.
DR GeneWiki; LY75; -.
DR Pharos; O60449; Tbio.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O60449; protein.
DR Bgee; ENSG00000054219; Expressed in thymus and 164 other tissues.
DR Genevisible; O60449; HS.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.10.10.10; -; 1.
DR Gene3D; 3.10.100.10; -; 10.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00059; Lectin_C; 10.
DR SMART; SM00034; CLECT; 10.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF56436; SSF56436; 10.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 10.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Endocytosis; Glycoprotein; Lectin; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:9862343"
FT CHAIN 28..1722
FT /note="Lymphocyte antigen 75"
FT /id="PRO_0000017552"
FT TOPO_DOM 28..1666
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1667..1691
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1692..1722
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..156
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 164..211
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 225..341
FT /note="C-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 368..486
FT /note="C-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 493..625
FT /note="C-type lectin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 652..778
FT /note="C-type lectin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 818..931
FT /note="C-type lectin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 958..1091
FT /note="C-type lectin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1110..1222
FT /note="C-type lectin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1251..1374
FT /note="C-type lectin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1401..1513
FT /note="C-type lectin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 1542..1661
FT /note="C-type lectin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOD_RES 933
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1703
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60767"
FT MOD_RES 1719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q60767"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 843
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 865
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 934
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1076
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1392
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 169..194
FT /evidence="ECO:0000250"
FT DISULFID 183..209
FT /evidence="ECO:0000250"
FT DISULFID 247..340
FT /evidence="ECO:0000250"
FT DISULFID 317..332
FT /evidence="ECO:0000250"
FT DISULFID 389..485
FT /evidence="ECO:0000250"
FT DISULFID 462..477
FT /evidence="ECO:0000250"
FT DISULFID 597..614
FT /evidence="ECO:0000250"
FT DISULFID 840..930
FT /evidence="ECO:0000250"
FT DISULFID 904..922
FT /evidence="ECO:0000250"
FT DISULFID 1060..1080
FT /evidence="ECO:0000250"
FT DISULFID 1197..1211
FT /evidence="ECO:0000250"
FT DISULFID 1488..1502
FT /evidence="ECO:0000250"
FT DISULFID 1635..1650
FT /evidence="ECO:0000250"
FT VAR_SEQ 1608..1722
FT /note="DQSWSWLDGSEVTFVKWENKSKSGVGRCSMLIASNETWKKVECEHGFGRVVC
FT KVPLGPDYTAIAIIVATLSILVLMGGLIWFLFQRHRLHLAGFSSVRYAQGVNEDEIMLP
FT SFHD -> DCPSSTWIQFQDSCYIFLQEAIKVESIEDVRNQCTDHGADMISIHNEEENA
FT FILDTLKKQWKGPDDILLGMFYDTDDASFKWFDNSNMTFDKWTDQDDDEDLVDTCAFLH
FT IKTGEWKKGNCEVSSVEGTLCKTAIPYKRKYLSDNHILISALVIASTVILTVLGAIIWF
FT LYKKHSDSRFTTVFSTAPQSPYNEDCVLVVGEENEYPVQFD (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12824192"
FT /id="VSP_020908"
FT VAR_SEQ 1664..1722
FT /note="GPDYTAIAIIVATLSILVLMGGLIWFLFQRHRLHLAGFSSVRYAQGVNEDEI
FT MLPSFHD -> DCPSSTWIQFQDSCYIFLQEAIKVESIEDVRNQCTDHGADMISIHNEE
FT ENAFILDTLKKQWKGPDDILLGMFYDTDDASFKWFDNSNMTFDKWTDQDDDEDLVDTCA
FT FLHIKTGEWKKGNCEVSSVEGTLCKTAIPYKRKYLSDNHILISALVIASTVILTVLGAI
FT IWFLYKKHSDSRFTTVFSTAPQSPYNEDCVLVVGEENEYPVQFD (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12824192"
FT /id="VSP_020909"
FT VARIANT 20
FT /note="W -> R (in dbSNP:rs35284483)"
FT /id="VAR_056156"
FT VARIANT 268
FT /note="E -> D (in dbSNP:rs2271381)"
FT /evidence="ECO:0000269|PubMed:9862343"
FT /id="VAR_027824"
FT VARIANT 486
FT /note="K -> M (in dbSNP:rs2729709)"
FT /id="VAR_027825"
FT VARIANT 666
FT /note="V -> A (in dbSNP:rs34020639)"
FT /id="VAR_056157"
FT VARIANT 692
FT /note="D -> N (in dbSNP:rs1397706)"
FT /id="VAR_024522"
FT VARIANT 807
FT /note="D -> E (in dbSNP:rs3951216)"
FT /evidence="ECO:0000269|PubMed:9862343"
FT /id="VAR_027826"
FT VARIANT 884
FT /note="D -> A (in dbSNP:rs3815875)"
FT /id="VAR_027827"
FT VARIANT 1202
FT /note="T -> S (in dbSNP:rs2303549)"
FT /id="VAR_027828"
FT VARIANT 1321
FT /note="K -> N (in dbSNP:rs12692566)"
FT /evidence="ECO:0000269|PubMed:12824192,
FT ECO:0000269|PubMed:9553150"
FT /id="VAR_027829"
FT VARIANT 1347
FT /note="K -> R (in dbSNP:rs17827158)"
FT /id="VAR_027830"
FT VARIANT 1391
FT /note="Y -> H (in dbSNP:rs2059696)"
FT /id="VAR_027831"
FT VARIANT 1393
FT /note="T -> I (in dbSNP:rs35941588)"
FT /id="VAR_056158"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:7JPT"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 200..203
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 227..238
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 240..249
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:7JPT"
FT TURN 322..325
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 371..380
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 383..390
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 402..410
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 412..416
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 421..427
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:7JPT"
FT TURN 467..470
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 471..475
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 481..488
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 503..505
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 506..508
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 535..548
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 550..553
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 556..561
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 574..576
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 609..612
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 614..616
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 622..625
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 629..632
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 653..660
FT /evidence="ECO:0007829|PDB:7JPT"
FT TURN 662..664
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 671..680
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 691..701
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 711..716
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 720..722
FT /evidence="ECO:0007829|PDB:7JPT"
FT TURN 745..749
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 752..755
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 769..772
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 780..788
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 793..796
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 797..799
FT /evidence="ECO:0007829|PDB:7JPT"
FT TURN 800..804
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 805..812
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 823..831
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 833..840
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 842..847
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 853..866
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 872..874
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 907..911
FT /evidence="ECO:0007829|PDB:7JPT"
FT TURN 912..916
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 926..932
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 945..948
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 956..958
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 961..964
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 970..972
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 973..982
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 983..987
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 993..1002
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 1003..1005
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1008..1010
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1015..1020
FT /evidence="ECO:0007829|PDB:7JPT"
FT TURN 1025..1027
FT /evidence="ECO:0007829|PDB:7JPT"
FT TURN 1038..1040
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1058..1064
FT /evidence="ECO:0007829|PDB:7JPT"
FT TURN 1070..1073
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1075..1078
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1082..1085
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1089..1091
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1108..1110
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1113..1118
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 1124..1133
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 1144..1157
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1164..1167
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1169..1172
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1174..1176
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1187..1189
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1195..1200
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1206..1209
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1211..1213
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1218..1222
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 1269..1280
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1281..1283
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 1293..1303
FT /evidence="ECO:0007829|PDB:7JPT"
FT TURN 1304..1308
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1310..1313
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 1319..1321
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1324..1328
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1336..1339
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1348..1352
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1358..1362
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 1366..1368
FT /evidence="ECO:0007829|PDB:7JPT"
FT HELIX 1370..1374
FT /evidence="ECO:0007829|PDB:7JPT"
FT STRAND 1376..1379
FT /evidence="ECO:0007829|PDB:7JPT"
SQ SEQUENCE 1722 AA; 198311 MW; 4BC17EC646BF016F CRC64;
MRTGWATPRR PAGLLMLLFW FFDLAEPSGR AANDPFTIVH GNTGKCIKPV YGWIVADDCD
ETEDKLWKWV SQHRLFHLHS QKCLGLDITK SVNELRMFSC DSSAMLWWKC EHHSLYGAAR
YRLALKDGHG TAISNASDVW KKGGSEESLC DQPYHEIYTR DGNSYGRPCE FPFLIDGTWH
HDCILDEDHS GPWCATTLNY EYDRKWGICL KPENGCEDNW EKNEQFGSCY QFNTQTALSW
KEAYVSCQNQ GADLLSINSA AELTYLKEKE GIAKIFWIGL NQLYSARGWE WSDHKPLNFL
NWDPDRPSAP TIGGSSCARM DAESGLWQSF SCEAQLPYVC RKPLNNTVEL TDVWTYSDTR
CDAGWLPNNG FCYLLVNESN SWDKAHAKCK AFSSDLISIH SLADVEVVVT KLHNEDIKEE
VWIGLKNINI PTLFQWSDGT EVTLTYWDEN EPNVPYNKTP NCVSYLGELG QWKVQSCEEK
LKYVCKRKGE KLNDASSDKM CPPDEGWKRH GETCYKIYED EVPFGTNCNL TITSRFEQEY
LNDLMKKYDK SLRKYFWTGL RDVDSCGEYN WATVGGRRRA VTFSNWNFLE PASPGGCVAM
STGKSVGKWE VKDCRSFKAL SICKKMSGPL GPEEASPKPD DPCPEGWQSF PASLSCYKVF
HAERIVRKRN WEEAERFCQA LGAHLSSFSH VDEIKEFLHF LTDQFSGQHW LWIGLNKRSP
DLQGSWQWSD RTPVSTIIMP NEFQQDYDIR DCAAVKVFHR PWRRGWHFYD DREFIYLRPF
ACDTKLEWVC QIPKGRTPKT PDWYNPDRAG IHGPPLIIEG SEYWFVADLH LNYEEAVLYC
ASNHSFLATI TSFVGLKAIK NKIANISGDG QKWWIRISEW PIDDHFTYSR YPWHRFPVTF
GEECLYMSAK TWLIDLGKPT DCSTKLPFIC EKYNVSSLEK YSPDSAAKVQ CSEQWIPFQN
KCFLKIKPVS LTFSQASDTC HSYGGTLPSV LSQIEQDFIT SLLPDMEATL WIGLRWTAYE
KINKWTDNRE LTYSNFHPLL VSGRLRIPEN FFEEESRYHC ALILNLQKSP FTGTWNFTSC
SERHFVSLCQ KYSEVKSRQT LQNASETVKY LNNLYKIIPK TLTWHSAKRE CLKSNMQLVS
ITDPYQQAFL SVQALLHNSS LWIGLFSQDD ELNFGWSDGK RLHFSRWAET NGQLEDCVVL
DTDGFWKTVD CNDNQPGAIC YYSGNETEKE VKPVDSVKCP SPVLNTPWIP FQNCCYNFII
TKNRHMATTQ DEVHTKCQKL NPKSHILSIR DEKENNFVLE QLLYFNYMAS WVMLGITYRN
KSLMWFDKTP LSYTHWRAGR PTIKNEKFLA GLSTDGFWDI QTFKVIEEAV YFHQHSILAC
KIEMVDYKEE YNTTLPQFMP YEDGIYSVIQ KKVTWYEALN MCSQSGGHLA SVHNQNGQLF
LEDIVKRDGF PLWVGLSSHD GSESSFEWSD GSTFDYIPWK GQTSPGNCVL LDPKGTWKHE
KCNSVKDGAI CYKPTKSKKL SRLTYSSRCP AAKENGSRWI QYKGHCYKSD QALHSFSEAK
KLCSKHDHSA TIVSIKDEDE NKFVSRLMRE NNNITMRVWL GLSQHSVDQS WSWLDGSEVT
FVKWENKSKS GVGRCSMLIA SNETWKKVEC EHGFGRVVCK VPLGPDYTAI AIIVATLSIL
VLMGGLIWFL FQRHRLHLAG FSSVRYAQGV NEDEIMLPSF HD
