CADH3_HUMAN
ID CADH3_HUMAN Reviewed; 829 AA.
AC P22223; B2R6F4; Q05DI6;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Cadherin-3;
DE AltName: Full=Placental cadherin;
DE Short=P-cadherin;
DE Flags: Precursor;
GN Name=CDH3; Synonyms=CDHP;
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 HIS-563.
RX PubMed=2793940; DOI=10.1083/jcb.109.4.1787;
RA Shimoyama Y., Yoshida T., Terada M., Shimosato Y., Abe O., Hirohashi S.;
RT "Molecular cloning of a human Ca2+-dependent cell-cell adhesion molecule
RT homologous to mouse placental cadherin: its low expression in human
RT placental tissues.";
RL J. Cell Biol. 109:1787-1794(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-563.
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], AND VARIANT HIS-563.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP MET-237.
RC TISSUE=Skin, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RC TISSUE=Fetal brain;
RX PubMed=9815605;
RA Jarrard D.F., Paul R., Van Bokhoven A., Nguyen S.H., Bova G.S.,
RA Wheelock M.J., Johnson K.R., Schalken J., Bussemakers M., Isaacs W.B.;
RT "P-cadherin is a basal cell-specific epithelial marker that is not
RT expressed in prostate cancer.";
RL Clin. Cancer Res. 3:2121-2128(1997).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=2702654;
RA Shimoyama Y., Hirohashi S., Hirano S., Noguchi M., Shimosato Y.,
RA Takeichi M., Abe O.;
RT "Cadherin cell-adhesion molecules in human epithelial tissues and
RT carcinomas.";
RL Cancer Res. 49:2128-2133(1989).
RN [7]
RP INTERACTION WITH CDCP1.
RX PubMed=16007225; DOI=10.1038/sj.onc.1208582;
RA Bhatt A.S., Erdjument-Bromage H., Tempst P., Craik C.S., Moasser M.M.;
RT "Adhesion signaling by a novel mitotic substrate of src kinases.";
RL Oncogene 24:5333-5343(2005).
RN [8]
RP INVOLVEMENT IN HJMD.
RX PubMed=11544476; DOI=10.1038/ng716;
RA Sprecher E., Bergman R., Richard G., Lurie R., Shalev S., Petronius D.,
RA Shalata A., Anbinder Y., Leibu R., Perlman I., Cohen N., Szargel R.;
RT "Hypotrichosis with juvenile macular dystrophy is caused by a mutation in
RT CDH3, encoding P-cadherin.";
RL Nat. Genet. 29:134-136(2001).
RN [9]
RP INTERACTION WITH CTNNB1.
RX PubMed=17052462; DOI=10.1016/j.molcel.2006.09.001;
RA Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.;
RT "Crystal structure of a beta-catenin/BCL9/Tcf4 complex.";
RL Mol. Cell 24:293-300(2006).
RN [10]
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 [11]
RP VARIANT HJMD HIS-503.
RX PubMed=12445216; DOI=10.1046/j.1523-1747.2002.19528.x;
RA Indelman M., Bergman R., Lurie R., Richard G., Miller B., Petronius D.,
RA Ciubutaro D., Leibu R., Sprecher E.;
RT "A missense mutation in CDH3, encoding P-cadherin, causes hypotrichosis
RT with juvenile macular dystrophy.";
RL J. Invest. Dermatol. 119:1210-1213(2002).
RN [12]
RP VARIANT EEMS ILE-322, AND VARIANT HIS-563.
RX PubMed=15805154; DOI=10.1136/jmg.2004.027821;
RA Kjaer K.W., Hansen L., Schwabe G.C., Marques-de-Faria A.P., Eiberg H.,
RA Mundlos S., Tommerup N., Rosenberg T.;
RT "Distinct CDH3 mutations cause ectodermal dysplasia, ectrodactyly, macular
RT dystrophy (EEM syndrome).";
RL J. Med. Genet. 42:292-298(2005).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells; cadherins may thus contribute to the sorting of
CC heterogeneous cell types.
CC -!- SUBUNIT: Interacts with CDCP1 and CTNNB1. {ECO:0000269|PubMed:16007225,
CC ECO:0000269|PubMed:17052462}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P22223-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P22223-2; Sequence=VSP_024820;
CC -!- TISSUE SPECIFICITY: Expressed in some normal epithelial tissues and in
CC some carcinoma cell lines. {ECO:0000269|PubMed:2702654}.
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: Hypotrichosis congenital with juvenile macular dystrophy
CC (HJMD) [MIM:601553]: A disorder characterized by congenital
CC hypotrichosis, early hair loss, and severe degenerative changes of the
CC retinal macula that culminate in blindness during the second to third
CC decade of life. {ECO:0000269|PubMed:11544476,
CC ECO:0000269|PubMed:12445216}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Ectodermal dysplasia, ectrodactyly, and macular dystrophy
CC syndrome (EEMS) [MIM:225280]: A form of ectodermal dysplasia, a
CC heterogeneous group of disorders due to abnormal development of two or
CC more ectodermal structures. It is an autosomal recessive condition
CC characterized by features of ectodermal dysplasia such as sparse
CC eyebrows and scalp hair, and selective tooth agenesis associated with
CC macular dystrophy and ectrodactyly. {ECO:0000269|PubMed:15805154}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- WEB RESOURCE: Name=Mutations of the CDH3 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/cdh3mut.htm";
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DR EMBL; X63629; CAA45177.1; -; mRNA.
DR EMBL; AK312554; BAG35451.1; -; mRNA.
DR EMBL; CH471092; EAW83238.1; -; Genomic_DNA.
DR EMBL; BC014462; AAH14462.1; -; mRNA.
DR EMBL; BC041846; AAH41846.1; -; mRNA.
DR EMBL; X95824; CAA65093.1; -; Genomic_DNA.
DR CCDS; CCDS10868.1; -. [P22223-1]
DR CCDS; CCDS82004.1; -. [P22223-2]
DR PIR; A33659; IJHUCP.
DR RefSeq; NP_001304124.1; NM_001317195.1. [P22223-2]
DR RefSeq; NP_001304125.1; NM_001317196.1.
DR RefSeq; NP_001784.2; NM_001793.5. [P22223-1]
DR PDB; 4OY9; X-ray; 1.62 A; A=108-320.
DR PDB; 4ZML; X-ray; 1.85 A; A=108-320.
DR PDB; 4ZMN; X-ray; 2.60 A; A=108-338.
DR PDB; 4ZMO; X-ray; 2.48 A; A=108-320.
DR PDB; 4ZMP; X-ray; 2.15 A; A=108-320.
DR PDB; 4ZMQ; X-ray; 2.20 A; A/B=108-320.
DR PDB; 4ZMT; X-ray; 2.70 A; A/B/C/D/E/F=108-338.
DR PDB; 4ZMV; X-ray; 2.40 A; A/B=108-320.
DR PDB; 4ZMW; X-ray; 2.30 A; A/B=108-320.
DR PDB; 4ZMX; X-ray; 3.10 A; A/B=108-320.
DR PDB; 4ZMY; X-ray; 1.50 A; A=108-320.
DR PDB; 4ZMZ; X-ray; 2.05 A; A=107-320.
DR PDB; 5JYL; X-ray; 2.55 A; A/C=108-207.
DR PDB; 5JYM; X-ray; 2.45 A; A/C=108-320.
DR PDB; 6ZTB; X-ray; 1.40 A; I=108-324.
DR PDB; 6ZTR; X-ray; 2.10 A; I/J=108-324.
DR PDB; 7CME; X-ray; 2.45 A; A/B=108-320.
DR PDB; 7CMF; X-ray; 2.30 A; A=107-320.
DR PDBsum; 4OY9; -.
DR PDBsum; 4ZML; -.
DR PDBsum; 4ZMN; -.
DR PDBsum; 4ZMO; -.
DR PDBsum; 4ZMP; -.
DR PDBsum; 4ZMQ; -.
DR PDBsum; 4ZMT; -.
DR PDBsum; 4ZMV; -.
DR PDBsum; 4ZMW; -.
DR PDBsum; 4ZMX; -.
DR PDBsum; 4ZMY; -.
DR PDBsum; 4ZMZ; -.
DR PDBsum; 5JYL; -.
DR PDBsum; 5JYM; -.
DR PDBsum; 6ZTB; -.
DR PDBsum; 6ZTR; -.
DR PDBsum; 7CME; -.
DR PDBsum; 7CMF; -.
DR AlphaFoldDB; P22223; -.
DR SMR; P22223; -.
DR BioGRID; 107436; 33.
DR IntAct; P22223; 11.
DR STRING; 9606.ENSP00000264012; -.
DR ChEMBL; CHEMBL3989384; -.
DR GlyGen; P22223; 2 sites.
DR iPTMnet; P22223; -.
DR PhosphoSitePlus; P22223; -.
DR BioMuta; CDH3; -.
DR DMDM; 146345382; -.
DR EPD; P22223; -.
DR jPOST; P22223; -.
DR MassIVE; P22223; -.
DR MaxQB; P22223; -.
DR PaxDb; P22223; -.
DR PeptideAtlas; P22223; -.
DR PRIDE; P22223; -.
DR ProteomicsDB; 53966; -. [P22223-1]
DR ProteomicsDB; 53967; -. [P22223-2]
DR ABCD; P22223; 42 sequenced antibodies.
DR Antibodypedia; 942; 927 antibodies from 41 providers.
DR DNASU; 1001; -.
DR Ensembl; ENST00000264012.9; ENSP00000264012.4; ENSG00000062038.15. [P22223-1]
DR Ensembl; ENST00000429102.6; ENSP00000398485.2; ENSG00000062038.15. [P22223-2]
DR GeneID; 1001; -.
DR KEGG; hsa:1001; -.
DR MANE-Select; ENST00000264012.9; ENSP00000264012.4; NM_001793.6; NP_001784.2.
DR UCSC; uc002ewf.3; human. [P22223-1]
DR CTD; 1001; -.
DR DisGeNET; 1001; -.
DR GeneCards; CDH3; -.
DR HGNC; HGNC:1762; CDH3.
DR HPA; ENSG00000062038; Tissue enhanced (choroid plexus, ovary).
DR MalaCards; CDH3; -.
DR MIM; 114021; gene.
DR MIM; 225280; phenotype.
DR MIM; 601553; phenotype.
DR neXtProt; NX_P22223; -.
DR OpenTargets; ENSG00000062038; -.
DR Orphanet; 1897; EEM syndrome.
DR Orphanet; 1573; Hypotrichosis with juvenile macular degeneration.
DR PharmGKB; PA26299; -.
DR VEuPathDB; HostDB:ENSG00000062038; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000154848; -.
DR HOGENOM; CLU_005284_2_0_1; -.
DR InParanoid; P22223; -.
DR OMA; EAQNQHT; -.
DR OrthoDB; 182239at2759; -.
DR PhylomeDB; P22223; -.
DR TreeFam; TF316817; -.
DR PathwayCommons; P22223; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR SignaLink; P22223; -.
DR SIGNOR; P22223; -.
DR BioGRID-ORCS; 1001; 9 hits in 1071 CRISPR screens.
DR ChiTaRS; CDH3; human.
DR GeneWiki; CDH3_(gene); -.
DR GenomeRNAi; 1001; -.
DR Pharos; P22223; Tbio.
DR PRO; PR:P22223; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P22223; protein.
DR Bgee; ENSG00000062038; Expressed in secondary oocyte and 138 other tissues.
DR ExpressionAtlas; P22223; baseline and differential.
DR Genevisible; P22223; HS.
DR GO; GO:0005912; C:adherens junction; IEA:Ensembl.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0022405; P:hair cycle process; IMP:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0031424; P:keratinization; IMP:UniProtKB.
DR GO; GO:0051796; P:negative regulation of timing of catagen; IMP:UniProtKB.
DR GO; GO:0032912; P:negative regulation of transforming growth factor beta2 production; IMP:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0010838; P:positive regulation of keratinocyte proliferation; IMP:UniProtKB.
DR GO; GO:0048023; P:positive regulation of melanin biosynthetic process; IMP:UniProtKB.
DR GO; GO:1902910; P:positive regulation of melanosome transport; IMP:UniProtKB.
DR GO; GO:0032773; P:positive regulation of tyrosinase activity; IMP:UniProtKB.
DR GO; GO:0060901; P:regulation of hair cycle by canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0001895; P:retina homeostasis; IMP:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR039808; Cadherin.
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; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 4.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Disease variant; Ectodermal dysplasia;
KW Glycoprotein; Hypotrichosis; Membrane; Metal-binding; Reference proteome;
KW Repeat; Sensory transduction; Signal; Transmembrane; Transmembrane helix;
KW Vision.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..107
FT /id="PRO_0000003745"
FT CHAIN 108..829
FT /note="Cadherin-3"
FT /id="PRO_0000003746"
FT TOPO_DOM 108..654
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..677
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 678..829
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 108..215
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 216..328
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 329..440
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 441..546
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 547..650
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 761..829
FT /note="NLKAANTDPTAPPYDTLLVFDYEGSGSDAASLSSLTSSASDQDQDYDYLNEW
FT GSRFKKLADMYGGGEDD -> GRGERGSQRGNGGLQLARGRTRRS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024820"
FT VARIANT 237
FT /note="V -> M (in dbSNP:rs17854171)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031929"
FT VARIANT 322
FT /note="N -> I (in EEMS; dbSNP:rs121434543)"
FT /evidence="ECO:0000269|PubMed:15805154"
FT /id="VAR_033010"
FT VARIANT 477
FT /note="R -> H (in dbSNP:rs34494880)"
FT /id="VAR_031930"
FT VARIANT 503
FT /note="R -> H (in HJMD; dbSNP:rs121434542)"
FT /evidence="ECO:0000269|PubMed:12445216"
FT /id="VAR_015422"
FT VARIANT 563
FT /note="Q -> H (in dbSNP:rs1126933)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15805154, ECO:0000269|PubMed:2793940,
FT ECO:0000269|Ref.3"
FT /id="VAR_031931"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:4ZMQ"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:6ZTB"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:6ZTB"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:6ZTB"
FT TURN 162..164
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:6ZTB"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 179..189
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:4ZMT"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 254..262
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:4ZMP"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:6ZTB"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:6ZTB"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:6ZTB"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:6ZTB"
FT STRAND 309..319
FT /evidence="ECO:0007829|PDB:6ZTB"
SQ SEQUENCE 829 AA; 91418 MW; 7C03C8536CD98C7B CRC64;
MGLPRGPLAS LLLLQVCWLQ CAASEPCRAV FREAEVTLEA GGAEQEPGQA LGKVFMGCPG
QEPALFSTDN DDFTVRNGET VQERRSLKER NPLKIFPSKR ILRRHKRDWV VAPISVPENG
KGPFPQRLNQ LKSNKDRDTK IFYSITGPGA DSPPEGVFAV EKETGWLLLN KPLDREEIAK
YELFGHAVSE NGASVEDPMN ISIIVTDQND HKPKFTQDTF RGSVLEGVLP GTSVMQVTAT
DEDDAIYTYN GVVAYSIHSQ EPKDPHDLMF TIHRSTGTIS VISSGLDREK VPEYTLTIQA
TDMDGDGSTT TAVAVVEILD ANDNAPMFDP QKYEAHVPEN AVGHEVQRLT VTDLDAPNSP
AWRATYLIMG GDDGDHFTIT THPESNQGIL TTRKGLDFEA KNQHTLYVEV TNEAPFVLKL
PTSTATIVVH VEDVNEAPVF VPPSKVVEVQ EGIPTGEPVC VYTAEDPDKE NQKISYRILR
DPAGWLAMDP DSGQVTAVGT LDREDEQFVR NNIYEVMVLA MDNGSPPTTG TGTLLLTLID
VNDHGPVPEP RQITICNQSP VRQVLNITDK DLSPHTSPFQ AQLTDDSDIY WTAEVNEEGD
TVVLSLKKFL KQDTYDVHLS LSDHGNKEQL TVIRATVCDC HGHVETCPGP WKGGFILPVL
GAVLALLFLL LVLLLLVRKK RKIKEPLLLP EDDTRDNVFY YGEEGGGEED QDYDITQLHR
GLEARPEVVL RNDVAPTIIP TPMYRPRPAN PDEIGNFIIE NLKAANTDPT APPYDTLLVF
DYEGSGSDAA SLSSLTSSAS DQDQDYDYLN EWGSRFKKLA DMYGGGEDD
