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   02-OCT-2024, entry version 198.
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   PDB; 8HBC; X-ray; 3.35 A; A/B=31-627.
DR   PDB; 8K8H; X-ray; 2.79 A; A=32-627.
DR   PDBsum; 7JPT; -.
DR   PDBsum; 7JPU; -.
DR   PDBsum; 8HBC; -.
DR   PDBsum; 8K8H; -.
DR   AlphaFoldDB; O60449; -.
DR   EMDB; EMD-22422; -.
DR   EMDB; EMD-22423; -.
DR   EMDB; EMD-6333; -.
DR   SMR; O60449; -.
DR   IntAct; O60449; 4.
DR   STRING; 9606.ENSP00000263636; -.
DR   ChEMBL; CHEMBL4804258; -.
DR   CarbonylDB; O60449; -.
DR   GlyConnect; 1472; 1 N-Linked glycan (1 site).
DR   GlyCosmos; O60449; 16 sites, 2 glycans.
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   jPOST; O60449; -.
DR   MassIVE; O60449; -.
DR   PaxDb; 9606-ENSP00000263636; -.
DR   PeptideAtlas; 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; 606 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   AGR; HGNC:38828; -.
DR   AGR; HGNC:6729; -.
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; RMENIHC; -.
DR   OrthoDB; 4271106at2759; -.
DR   PhylomeDB; O60449; -.
DR   TreeFam; TF316663; -.
DR   PathwayCommons; O60449; -.
DR   SignaLink; O60449; -.
DR   BioGRID-ORCS; 100526664; 32 hits in 667 CRISPR screens.
DR   BioGRID-ORCS; 4065; 13 hits in 1094 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 166 other cell types or tissues.
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:0005886; C: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; cd00037; CLECT; 10.
DR   CDD; cd00062; FN2; 1.
DR   CDD; cd00161; RICIN; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 1.
DR   Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 10.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR050111; C-type_lectin/snaclec_domain.
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   PANTHER; PTHR22803:SF65; LYMPHOCYTE ANTIGEN 75; 1.
DR   PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
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; SSF56436; C-type lectin-like; 10.
DR   SUPFAM; SSF57440; Kringle-like; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 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; Proteomics identification; Receptor; Reference proteome;
KW   Repeat; Signal; 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          46..50
FT                   /evidence="ECO:0007829|PDB:8HBC"
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          103..105
FT                   /evidence="ECO:0007829|PDB:8HBC"
FT   STRAND          109..111
FT                   /evidence="ECO:0007829|PDB:8HBC"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:7JPT"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:7JPT"
FT   STRAND          122..126
FT                   /evidence="ECO:0007829|PDB:8HBC"
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          593..595
FT                   /evidence="ECO:0007829|PDB:8HBC"
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
//