DSG1_HUMAN
ID DSG1_HUMAN Reviewed; 1049 AA.
AC Q02413; B7Z845;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Desmoglein-1;
DE AltName: Full=Cadherin family member 4;
DE AltName: Full=Desmosomal glycoprotein 1;
DE Short=DG1;
DE Short=DGI;
DE AltName: Full=Pemphigus foliaceus antigen;
DE Flags: Precursor;
GN Name=DSG1; Synonyms=CDHF4;
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] (ISOFORM 1), AND VARIANT VAL-11.
RC TISSUE=Keratinocyte;
RX PubMed=1711210; DOI=10.1073/pnas.88.11.4796;
RA Wheeler G.N., Parker A.E., Thomas C.L., Ataliotis P., Poynter D.,
RA Arnemann J., Rutman A.J., Pidsley S.C., Watt F.M., Rees D.A., Buxton R.S.,
RA Magee A.I.;
RT "Desmosomal glycoprotein DGI, a component of intercellular desmosome
RT junctions, is related to the cadherin family of cell adhesion molecules.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4796-4800(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-11.
RC TISSUE=Foreskin;
RX PubMed=1770008; DOI=10.1242/jcs.99.4.809;
RA Nilles L.A., Parry D.A., Powers E.E., Angst B.D., Wagner R.M., Green K.J.;
RT "Structural analysis and expression of human desmoglein: a cadherin-like
RT component of the desmosome.";
RL J. Cell Sci. 99:809-821(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [4]
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 [5]
RP INVOLVEMENT IN PPKS1.
RX PubMed=10332028; DOI=10.1093/hmg/8.6.971;
RA Rickman L., Simrak D., Stevens H.P., Hunt D.M., King I.A., Bryant S.P.,
RA Eady R.A.J., Leigh I.M., Arnemann J., Magee A.I., Kelsell D.P.,
RA Buxton R.S.;
RT "N-terminal deletion in a desmosomal cadherin causes the autosomal dominant
RT skin disease striate palmoplantar keratoderma.";
RL Hum. Mol. Genet. 8:971-976(1999).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110.
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 [7]
RP INTERACTION WITH JUP/PLAKOGLOBIN.
RX PubMed=19759396; DOI=10.1074/jbc.m109.047928;
RA Choi H.J., Gross J.C., Pokutta S., Weis W.I.;
RT "Interactions of plakoglobin and beta-catenin with desmosomal cadherins:
RT basis of selective exclusion of alpha- and beta-catenin from desmosomes.";
RL J. Biol. Chem. 284:31776-31788(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP INVOLVEMENT IN EPKHE.
RX PubMed=23974871; DOI=10.1038/ng.2739;
RA Samuelov L., Sarig O., Harmon R.M., Rapaport D., Ishida-Yamamoto A.,
RA Isakov O., Koetsier J.L., Gat A., Goldberg I., Bergman R., Spiegel R.,
RA Eytan O., Geller S., Peleg S., Shomron N., Goh C.S., Wilson N.J.,
RA Smith F.J., Pohler E., Simpson M.A., McLean W.H., Irvine A.D., Horowitz M.,
RA McGrath J.A., Green K.J., Sprecher E.;
RT "Desmoglein 1 deficiency results in severe dermatitis, multiple allergies
RT and metabolic wasting.";
RL Nat. Genet. 45:1244-1248(2013).
RN [11]
RP INTERACTION WITH STAPHYLOCOCCUS AUREUS PROTEIN SDRD (MICROBIAL INFECTION).
RX PubMed=26924733; DOI=10.1038/srep22134;
RA Askarian F., Ajayi C., Hanssen A.M., van Sorge N.M., Pettersen I.,
RA Diep D.B., Sollid J.U., Johannessen M.;
RT "The interaction between Staphylococcus aureus SdrD and desmoglein 1 is
RT important for adhesion to host cells.";
RL Sci. Rep. 6:22134-22134(2016).
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: Binds to JUP/plakoglobin.
CC -!- SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus
CC protein SdrD; this interaction increases S. aureus adherence to
CC keratinocytes. {ECO:0000269|PubMed:26924733}.
CC -!- INTERACTION:
CC Q02413; Q08554: DSC1; NbExp=2; IntAct=EBI-1045757, EBI-2371346;
CC Q02413; P15924: DSP; NbExp=2; IntAct=EBI-1045757, EBI-355041;
CC Q02413; P14923: JUP; NbExp=2; IntAct=EBI-1045757, EBI-702484;
CC Q02413; Q13835: PKP1; NbExp=2; IntAct=EBI-1045757, EBI-2513407;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell junction, desmosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q02413-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q02413-2; Sequence=VSP_055930;
CC -!- TISSUE SPECIFICITY: Epidermis, tongue, tonsil and esophagus.
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: Palmoplantar keratoderma 1, striate, focal, or diffuse (PPKS1)
CC [MIM:148700]: A dermatological disorder characterized by thickening of
CC the skin on the palms and soles, and longitudinal hyperkeratotic
CC lesions on the palms, running the length of each finger.
CC {ECO:0000269|PubMed:10332028}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Erythroderma, congenital, with palmoplantar keratoderma,
CC hypotrichosis, and hyper IgE (EPKHE) [MIM:615508]: A syndrome
CC characterized by severe dermatitis, multiple allergies and metabolic
CC wasting. Clinical features include erythroderma, yellowish papules and
CC plaques arranged at the periphery of the palms, along the fingers and
CC over weight-bearing areas of the feet, skin erosions and scaling, and
CC hypotrichosis. Additionally, patients manifest severe food allergies,
CC elevated immunoglobulin E (IgE) levels and recurrent infections with
CC marked metabolic wasting. {ECO:0000269|PubMed:23974871}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
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DR EMBL; X56654; CAA39976.1; -; mRNA.
DR EMBL; AF097935; AAC83817.1; -; mRNA.
DR EMBL; AK302888; BAH13831.1; -; mRNA.
DR EMBL; AC009717; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS11896.1; -. [Q02413-1]
DR PIR; S16906; IJHUG1.
DR RefSeq; NP_001933.2; NM_001942.3. [Q02413-1]
DR AlphaFoldDB; Q02413; -.
DR SMR; Q02413; -.
DR BioGRID; 108162; 154.
DR ELM; Q02413; -.
DR IntAct; Q02413; 60.
DR MINT; Q02413; -.
DR STRING; 9606.ENSP00000257192; -.
DR GlyGen; Q02413; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q02413; -.
DR PhosphoSitePlus; Q02413; -.
DR SwissPalm; Q02413; -.
DR BioMuta; DSG1; -.
DR DMDM; 292495005; -.
DR EPD; Q02413; -.
DR jPOST; Q02413; -.
DR MassIVE; Q02413; -.
DR MaxQB; Q02413; -.
DR PaxDb; Q02413; -.
DR PeptideAtlas; Q02413; -.
DR PRIDE; Q02413; -.
DR ProteomicsDB; 58089; -. [Q02413-1]
DR ABCD; Q02413; 44 sequenced antibodies.
DR Antibodypedia; 3998; 794 antibodies from 42 providers.
DR DNASU; 1828; -.
DR Ensembl; ENST00000257192.5; ENSP00000257192.4; ENSG00000134760.6. [Q02413-1]
DR GeneID; 1828; -.
DR KEGG; hsa:1828; -.
DR MANE-Select; ENST00000257192.5; ENSP00000257192.4; NM_001942.4; NP_001933.2.
DR UCSC; uc002kwp.4; human. [Q02413-1]
DR CTD; 1828; -.
DR DisGeNET; 1828; -.
DR GeneCards; DSG1; -.
DR HGNC; HGNC:3048; DSG1.
DR HPA; ENSG00000134760; Tissue enriched (skin).
DR MalaCards; DSG1; -.
DR MIM; 125670; gene.
DR MIM; 148700; phenotype.
DR MIM; 615508; phenotype.
DR neXtProt; NX_Q02413; -.
DR OpenTargets; ENSG00000134760; -.
DR Orphanet; 369999; Diffuse palmoplantar keratoderma with painful fissures.
DR Orphanet; 370002; Focal palmoplantar keratoderma with joint keratoses.
DR Orphanet; 369992; Severe dermatitis-multiple allergies-metabolic wasting syndrome.
DR Orphanet; 50942; Striate palmoplantar keratoderma.
DR PharmGKB; PA27501; -.
DR VEuPathDB; HostDB:ENSG00000134760; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT01030000234624; -.
DR HOGENOM; CLU_005284_0_0_1; -.
DR InParanoid; Q02413; -.
DR OMA; MDWRFFR; -.
DR OrthoDB; 250139at2759; -.
DR PhylomeDB; Q02413; -.
DR TreeFam; TF331809; -.
DR PathwayCommons; Q02413; -.
DR Reactome; R-HSA-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR SignaLink; Q02413; -.
DR BioGRID-ORCS; 1828; 7 hits in 1074 CRISPR screens.
DR ChiTaRS; DSG1; human.
DR GeneWiki; Desmoglein_1; -.
DR GenomeRNAi; 1828; -.
DR Pharos; Q02413; Tbio.
DR PRO; PR:Q02413; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q02413; protein.
DR Bgee; ENSG00000134760; Expressed in upper arm skin and 101 other tissues.
DR Genevisible; Q02413; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0001533; C:cornified envelope; TAS:Reactome.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030057; C:desmosome; IBA:GO_Central.
DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0045295; F:gamma-catenin binding; IPI:BHF-UCL.
DR GO; GO:0015643; F:toxic substance binding; NAS:UniProtKB.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; NAS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; NAS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR DisProt; DP01476; -.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR009123; Desmoglein.
DR InterPro; IPR009122; Desmosomal_cadherin.
DR Pfam; PF00028; Cadherin; 3.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR01818; DESMOCADHERN.
DR PRINTS; PR01819; DESMOGLEIN.
DR SMART; SM00112; CA; 4.
DR SUPFAM; SSF49313; SSF49313; 4.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Hypotrichosis; Membrane;
KW Metal-binding; Palmoplantar keratoderma; Phosphoprotein;
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_0000003837"
FT CHAIN 50..1049
FT /note="Desmoglein-1"
FT /id="PRO_0000003838"
FT TOPO_DOM 50..548
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 549..569
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 570..1049
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..270
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 271..385
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 386..497
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 813..839
FT /note="Desmoglein repeat 1"
FT REPEAT 840..869
FT /note="Desmoglein repeat 2"
FT REPEAT 870..899
FT /note="Desmoglein repeat 3"
FT REPEAT 900..927
FT /note="Desmoglein repeat 4"
FT REPEAT 928..956
FT /note="Desmoglein repeat 5"
FT REGION 485..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16740002"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..641
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055930"
FT VARIANT 11
FT /note="M -> V (in dbSNP:rs1426310)"
FT /evidence="ECO:0000269|PubMed:1711210,
FT ECO:0000269|PubMed:1770008"
FT /id="VAR_060248"
FT VARIANT 395
FT /note="T -> S (in dbSNP:rs16961655)"
FT /id="VAR_055573"
FT VARIANT 493
FT /note="N -> T (in dbSNP:rs8091003)"
FT /id="VAR_024385"
FT VARIANT 498
FT /note="T -> N (in dbSNP:rs8091117)"
FT /id="VAR_024386"
FT VARIANT 528
FT /note="Y -> S (in dbSNP:rs16961689)"
FT /id="VAR_055574"
FT VARIANT 538
FT /note="D -> N (in dbSNP:rs34302455)"
FT /id="VAR_055575"
FT VARIANT 665
FT /note="M -> I (in dbSNP:rs35360042)"
FT /id="VAR_055576"
FT VARIANT 821
FT /note="L -> Q (in dbSNP:rs16961692)"
FT /id="VAR_055577"
FT VARIANT 828
FT /note="D -> N (in dbSNP:rs3752094)"
FT /id="VAR_060249"
FT VARIANT 841
FT /note="Y -> F (in dbSNP:rs3752095)"
FT /id="VAR_020364"
SQ SEQUENCE 1049 AA; 113748 MW; FEA471244B9D67AE CRC64;
MDWSFFRVVA MLFIFLVVVE VNSEFRIQVR DYNTKNGTIK WHSIRRQKRE WIKFAAACRE
GEDNSKRNPI AKIHSDCAAN QQVTYRISGV GIDQPPYGIF VINQKTGEIN ITSIVDREVT
PFFIIYCRAL NSMGQDLERP LELRVRVLDI NDNPPVFSMA TFAGQIEENS NANTLVMILN
ATDADEPNNL NSKIAFKIIR QEPSDSPMFI INRNTGEIRT MNNFLDREQY GQYALAVRGS
DRDGGADGMS AECECNIKIL DVNDNIPYME QSSYTIEIQE NTLNSNLLEI RVIDLDEEFS
ANWMAVIFFI SGNEGNWFEI EMNERTNVGI LKVVKPLDYE AMQSLQLSIG VRNKAEFHHS
IMSQYKLKAS AISVTVLNVI EGPVFRPGSK TYVVTGNMGS NDKVGDFVAT DLDTGRPSTT
VRYVMGNNPA DLLAVDSRTG KLTLKNKVTK EQYNMLGGKY QGTILSIDDN LQRTCTGTIN
INIQSFGNDD RTNTEPNTKI TTNTGRQEST SSTNYDTSTT STDSSQVYSS EPGNGAKDLL
SDNVHFGPAG IGLLIMGFLV LGLVPFLMIC CDCGGAPRSA AGFEPVPECS DGAIHSWAVE
GPQPEPRDIT TVIPQIPPDN ANIIECIDNS GVYTNEYGGR EMQDLGGGER MTGFELTEGV
KTSGMPEICQ EYSGTLRRNS MRECREGGLN MNFMESYFCQ KAYAYADEDE GRPSNDCLLI
YDIEGVGSPA GSVGCCSFIG EDLDDSFLDT LGPKFKKLAD ISLGKESYPD LDPSWPPQST
EPVCLPQETE PVVSGHPPIS PHFGTTTVIS ESTYPSGPGV LHPKPILDPL GYGNVTVTES
YTTSDTLKPS VHVHDNRPAS NVVVTERVVG PISGADLHGM LEMPDLRDGS NVIVTERVIA
PSSSLPTSLT IHHPRESSNV VVTERVIQPT SGMIGSLSMH PELANAHNVI VTERVVSGAG
VTGISGTTGI SGGIGSSGLV GTSMGAGSGA LSGAGISGGG IGLSSLGGTA SIGHMRSSSD
HHFNQTIGSA SPSTARSRIT KYSTVQYSK
