ID   DSG3_HUMAN              Reviewed;         999 AA.
AC   P32926; A8K2V2;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   24-JAN-2024, entry version 191.
DE   RecName: Full=Desmoglein-3 {ECO:0000305};
DE   AltName: Full=130 kDa pemphigus vulgaris antigen;
DE            Short=PVA;
DE   AltName: Full=Cadherin family member 6;
DE   Flags: Precursor;
GN   Name=DSG3 {ECO:0000312|HGNC:HGNC:3050}; Synonyms=CDHF6;
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], INVOLVEMENT IN PEMPHIGUS VULGARIS, AND VARIANT
RP   ALA-912.
RX   PubMed=1720352; DOI=10.1016/0092-8674(91)90360-b;
RA   Amagai M., Klaus-Kovtun V., Stanley J.R.;
RT   "Autoantibodies against a novel epithelial cadherin in pemphigus vulgaris,
RT   a disease of cell adhesion.";
RL   Cell 67:869-877(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-912.
RC   TISSUE=Tongue;
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=16177791; DOI=10.1038/nature03983;
RA   Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA   Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA   Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA   Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA   Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA   Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA   Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA   Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 18.";
RL   Nature 437:551-555(2005).
RN   [4]
RP   INTERACTION WITH PKP2.
RX   PubMed=11790773; DOI=10.1074/jbc.m108765200;
RA   Chen X., Bonne S., Hatzfeld M., van Roy F., Green K.J.;
RT   "Protein binding and functional characterization of plakophilin 2. Evidence
RT   for its diverse roles in desmosomes and beta -catenin signaling.";
RL   J. Biol. Chem. 277:10512-10522(2002).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-459 AND ASN-545.
RC   TISSUE=Saliva;
RX   PubMed=16740002; DOI=10.1021/pr050492k;
RA   Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.;
RT   "Identification of N-linked glycoproteins in human saliva by glycoprotein
RT   capture and mass spectrometry.";
RL   J. Proteome Res. 5:1493-1503(2006).
RN   [6]
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   [7]
RP   VARIANT ABOLM 287-ARG--ILE-999 DEL, CHARACTERIZATION OF VARIANT ABOLM
RP   287-ARG--ILE-999 DEL, AND TISSUE SPECIFICITY.
RX   PubMed=30528827; DOI=10.1016/j.jid.2018.09.038;
RA   Kim J.H., Kim S.E., Park H.S., Lee S.H., Lee S.E., Kim S.C.;
RT   "A Homozygous Nonsense Mutation in the DSG3 Gene Causes Acantholytic
RT   Blisters in the Oral and Laryngeal Mucosa.";
RL   J. Invest. Dermatol. 139:1187-1190(2019).
CC   -!- FUNCTION: Component of intercellular desmosome junctions. Involved in
CC       the interaction of plaque proteins and intermediate filaments mediating
CC       cell-cell adhesion.
CC   -!- SUBUNIT: Interacts with PKP2. {ECO:0000269|PubMed:11790773}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000255}. Cell junction, desmosome {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Epidermis, tongue, tonsil, esophagus and
CC       carcinomas. Expressed in skin and mucosa (at protein level)
CC       (PubMed:30528827). {ECO:0000269|PubMed:30528827}.
CC   -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC       cadherin domain and rigidify the connections, imparting a strong
CC       curvature to the full-length ectodomain. {ECO:0000250}.
CC   -!- DISEASE: Blistering, acantholytic, of oral and laryngeal mucosa (ABOLM)
CC       [MIM:619226]: An autosomal recessive disorder characterized by
CC       recurrent, suprabasal acantholytic blisters in the oral and laryngeal
CC       mucosa. Skin, conjunctival and genital mucosa, nail folds, and nails
CC       are unaffected. Normal structure is observed in the scalp epidermis and
CC       hair follicle. {ECO:0000269|PubMed:30528827}. Note=The disease may be
CC       caused by variants affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: Pemphigus vulgaris (PV) is a potentially lethal skin
CC       disease in which epidermal blisters occur as the result of the loss of
CC       cell-cell adhesion caused by the action of autoantibodies against
CC       desmoglein 3. {ECO:0000269|PubMed:1720352}.
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DR   EMBL; M76482; AAA60230.1; -; mRNA.
DR   EMBL; AK290367; BAF83056.1; -; mRNA.
DR   EMBL; AC021549; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS11898.1; -.
DR   PIR; A41088; IJHUG3.
DR   RefSeq; NP_001935.2; NM_001944.2.
DR   PDB; 5EQX; X-ray; 3.05 A; A=50-598.
DR   PDBsum; 5EQX; -.
DR   AlphaFoldDB; P32926; -.
DR   SMR; P32926; -.
DR   BioGRID; 108164; 43.
DR   ELM; P32926; -.
DR   IntAct; P32926; 2.
DR   STRING; 9606.ENSP00000257189; -.
DR   Allergome; 8248; Hom s DSG3.
DR   GlyCosmos; P32926; 4 sites, No reported glycans.
DR   GlyGen; P32926; 10 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P32926; -.
DR   PhosphoSitePlus; P32926; -.
DR   SwissPalm; P32926; -.
DR   BioMuta; DSG3; -.
DR   DMDM; 239938621; -.
DR   CPTAC; CPTAC-62; -.
DR   CPTAC; CPTAC-63; -.
DR   EPD; P32926; -.
DR   jPOST; P32926; -.
DR   MassIVE; P32926; -.
DR   MaxQB; P32926; -.
DR   PaxDb; 9606-ENSP00000257189; -.
DR   PeptideAtlas; P32926; -.
DR   PRIDE; P32926; -.
DR   ProteomicsDB; 54887; -.
DR   ABCD; P32926; 49 sequenced antibodies.
DR   Antibodypedia; 3464; 826 antibodies from 36 providers.
DR   DNASU; 1830; -.
DR   Ensembl; ENST00000257189.5; ENSP00000257189.4; ENSG00000134757.5.
DR   GeneID; 1830; -.
DR   KEGG; hsa:1830; -.
DR   MANE-Select; ENST00000257189.5; ENSP00000257189.4; NM_001944.3; NP_001935.2.
DR   UCSC; uc002kws.4; human.
DR   AGR; HGNC:3050; -.
DR   CTD; 1830; -.
DR   DisGeNET; 1830; -.
DR   GeneCards; DSG3; -.
DR   HGNC; HGNC:3050; DSG3.
DR   HPA; ENSG00000134757; Tissue enhanced (esophagus, vagina).
DR   MalaCards; DSG3; -.
DR   MIM; 169615; gene.
DR   MIM; 619226; phenotype.
DR   neXtProt; NX_P32926; -.
DR   OpenTargets; ENSG00000134757; -.
DR   PharmGKB; PA27503; -.
DR   VEuPathDB; HostDB:ENSG00000134757; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT01030000234624; -.
DR   HOGENOM; CLU_005284_0_0_1; -.
DR   InParanoid; P32926; -.
DR   OMA; CQCDNRD; -.
DR   OrthoDB; 5314152at2759; -.
DR   PhylomeDB; P32926; -.
DR   TreeFam; TF331809; -.
DR   PathwayCommons; P32926; -.
DR   Reactome; R-HSA-351906; Apoptotic cleavage of cell adhesion proteins.
DR   Reactome; R-HSA-6805567; Keratinization.
DR   Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR   SignaLink; P32926; -.
DR   BioGRID-ORCS; 1830; 10 hits in 1141 CRISPR screens.
DR   ChiTaRS; DSG3; human.
DR   GeneWiki; Desmoglein_3; -.
DR   GenomeRNAi; 1830; -.
DR   Pharos; P32926; Tbio.
DR   PRO; PR:P32926; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; P32926; Protein.
DR   Bgee; ENSG00000134757; Expressed in gingiva and 102 other cell types or tissues.
DR   GO; GO:0001533; C:cornified envelope; TAS:Reactome.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0030057; C:desmosome; IBA:GO_Central.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   CDD; cd11304; Cadherin_repeat; 4.
DR   Gene3D; 2.60.40.60; Cadherins; 5.
DR   Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   InterPro; IPR009122; Desmosomal_cadherin.
DR   PANTHER; PTHR24025; DESMOGLEIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR24025:SF3; DESMOGLEIN-3; 1.
DR   Pfam; PF00028; Cadherin; 3.
DR   PRINTS; PR00205; CADHERIN.
DR   PRINTS; PR01818; DESMOCADHERN.
DR   PRINTS; PR01819; DESMOGLEIN.
DR   SMART; SM00112; CA; 4.
DR   SUPFAM; SSF49313; Cadherin-like; 4.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 4.
DR   Genevisible; P32926; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW   Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..49
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003851"
FT   CHAIN           50..999
FT                   /note="Desmoglein-3"
FT                   /id="PRO_0000003852"
FT   TOPO_DOM        50..615
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        616..640
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        641..999
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          50..158
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          159..268
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          269..383
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          386..499
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REPEAT          910..935
FT                   /note="Desmoglein repeat 1"
FT   REPEAT          936..966
FT                   /note="Desmoglein repeat 2"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        459
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16740002"
FT   CARBOHYD        545
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16740002"
FT   VARIANT         287..999
FT                   /note="Missing (in ABOLM; uncertain significance; loss of
FT                   expression in skin and mucosa)"
FT                   /evidence="ECO:0000269|PubMed:30528827"
FT                   /id="VAR_085271"
FT   VARIANT         509
FT                   /note="V -> M (in dbSNP:rs16961975)"
FT                   /id="VAR_055578"
FT   VARIANT         912
FT                   /note="T -> A (in dbSNP:rs1380866)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:1720352"
FT                   /id="VAR_059178"
FT   CONFLICT        110
FT                   /note="N -> D (in Ref. 2; BAF83056)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        298
FT                   /note="T -> A (in Ref. 2; BAF83056)"
FT                   /evidence="ECO:0000305"
FT   TURN            65..67
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          70..72
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   HELIX           76..78
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          84..89
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          93..96
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          98..102
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   TURN            104..106
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   TURN            117..119
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          121..130
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          141..148
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          156..158
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          160..166
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          175..178
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          187..189
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   TURN            190..192
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          198..201
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          209..211
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   TURN            213..215
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          217..220
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   TURN            227..229
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          231..241
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   HELIX           242..244
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          248..257
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          266..270
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          272..277
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          282..288
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   TURN            299..301
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          303..310
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          316..320
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   TURN            322..324
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          327..331
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   TURN            337..339
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          341..353
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   TURN            357..359
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   HELIX           360..362
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          368..375
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          384..391
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          394..396
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          412..419
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          422..429
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   HELIX           431..433
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          435..437
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   TURN            439..441
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          443..446
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   TURN            453..456
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          459..470
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   TURN            471..473
FT                   /evidence="ECO:0007829|PDB:5EQX"
FT   STRAND          477..484
FT                   /evidence="ECO:0007829|PDB:5EQX"
SQ   SEQUENCE   999 AA;  107533 MW;  7553CC917E8719BA CRC64;
     MMGLFPRTTG ALAIFVVVIL VHGELRIETK GQYDEEEMTM QQAKRRQKRE WVKFAKPCRE
     GEDNSKRNPI AKITSDYQAT QKITYRISGV GIDQPPFGIF VVDKNTGDIN ITAIVDREET
     PSFLITCRAL NAQGLDVEKP LILTVKILDI NDNPPVFSQQ IFMGEIEENS ASNSLVMILN
     ATDADEPNHL NSKIAFKIVS QEPAGTPMFL LSRNTGEVRT LTNSLDREQA SSYRLVVSGA
     DKDGEGLSTQ CECNIKVKDV NDNFPMFRDS QYSARIEENI LSSELLRFQV TDLDEEYTDN
     WLAVYFFTSG NEGNWFEIQT DPRTNEGILK VVKALDYEQL QSVKLSIAVK NKAEFHQSVI
     SRYRVQSTPV TIQVINVREG IAFRPASKTF TVQKGISSKK LVDYILGTYQ AIDEDTNKAA
     SNVKYVMGRN DGGYLMIDSK TAEIKFVKNM NRDSTFIVNK TITAEVLAID EYTGKTSTGT
     VYVRVPDFND NCPTAVLEKD AVCSSSPSVV VSARTLNNRY TGPYTFALED QPVKLPAVWS
     ITTLNATSAL LRAQEQIPPG VYHISLVLTD SQNNRCEMPR SLTLEVCQCD NRGICGTSYP
     TTSPGTRYGR PHSGRLGPAA IGLLLLGLLL LLLAPLLLLT CDCGAGSTGG VTGGFIPVPD
     GSEGTIHQWG IEGAHPEDKE ITNICVPPVT ANGADFMESS EVCTNTYARG TAVEGTSGME
     MTTKLGAATE SGGAAGFATG TVSGAASGFG AATGVGICSS GQSGTMRTRH STGGTNKDYA
     DGAISMNFLD SYFSQKAFAC AEEDDGQEAN DCLLIYDNEG ADATGSPVGS VGCCSFIADD
     LDDSFLDSLG PKFKKLAEIS LGVDGEGKEV QPPSKDSGYG IESCGHPIEV QQTGFVKCQT
     LSGSQGASAL STSGSVQPAV SIPDPLQHGN YLVTETYSAS GSLVQPSTAG FDPLLTQNVI
     VTERVICPIS SVPGNLAGPT QLRGSHTMLC TEDPCSRLI
//