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 18-JUL-2018, entry version 181. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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., RA Hirohashi S.; RT "Molecular cloning of a human Ca2+-dependent cell-cell adhesion RT molecule homologous to mouse placental cadherin: its low expression in RT human placental tissues."; RL J. Cell Biol. 109:1787-1794(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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., RA Petronius D., Shalata A., Anbinder Y., Leibu R., Perlman I., Cohen N., RA Szargel R.; RT "Hypotrichosis with juvenile macular dystrophy is caused by a mutation RT in 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., RA Buerckstuemmer T., 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., RA Petronius D., Ciubutaro D., Leibu R., Sprecher E.; RT "A missense mutation in CDH3, encoding P-cadherin, causes RT hypotrichosis 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, RT macular dystrophy (EEM syndrome)."; RL J. Med. Genet. 42:292-298(2005). CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. CC They preferentially interact with themselves in a homophilic CC manner in connecting cells; cadherins may thus contribute to the CC sorting of heterogeneous cell types. CC -!- SUBUNIT: Interacts with CDCP1 and CTNNB1. CC {ECO:0000269|PubMed:16007225, 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 Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Expressed in some normal epithelial tissues CC and in some carcinoma cell lines. {ECO:0000269|PubMed:2702654}. CC -!- DOMAIN: Three calcium ions are usually bound at the interface of CC each cadherin domain and rigidify the connections, imparting a CC strong 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 CC the retinal macula that culminate in blindness during the second CC to third decade of life. {ECO:0000269|PubMed:11544476, CC ECO:0000269|PubMed:12445216}. Note=The disease is caused by CC mutations 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 CC two or more ectodermal structures. It is an autosomal recessive CC condition characterized by features of ectodermal dysplasia such CC as sparse eyebrows and scalp hair, and selective tooth agenesis CC associated with macular dystrophy and ectrodactyly. CC {ECO:0000269|PubMed:15805154}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- WEB RESOURCE: Name=Mutations of the CDH3 gene; Note=Retina CC International's Scientific Newsletter; CC URL="http://www.retina-international.org/files/sci-news/cdh3mut.htm"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Hs.191842; -. 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 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 ProteinModelPortal; P22223; -. DR SMR; P22223; -. DR BioGrid; 107436; 10. DR IntAct; P22223; 5. DR STRING; 9606.ENSP00000264012; -. DR ChEMBL; CHEMBL3989384; -. DR iPTMnet; P22223; -. DR PhosphoSitePlus; P22223; -. DR BioMuta; CDH3; -. DR DMDM; 146345382; -. DR EPD; P22223; -. DR MaxQB; P22223; -. DR PaxDb; P22223; -. DR PeptideAtlas; P22223; -. DR PRIDE; P22223; -. DR ProteomicsDB; 53966; -. DR ProteomicsDB; 53967; -. [P22223-2] DR DNASU; 1001; -. DR Ensembl; ENST00000264012; ENSP00000264012; ENSG00000062038. [P22223-1] DR Ensembl; ENST00000429102; ENSP00000398485; ENSG00000062038. [P22223-2] DR GeneID; 1001; -. DR KEGG; hsa:1001; -. DR UCSC; uc002ewf.3; human. [P22223-1] DR CTD; 1001; -. DR DisGeNET; 1001; -. DR EuPathDB; HostDB:ENSG00000062038.13; -. DR GeneCards; CDH3; -. DR H-InvDB; HIX0026973; -. DR HGNC; HGNC:1762; CDH3. DR HPA; CAB002487; -. DR HPA; HPA001767; -. 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 eggNOG; KOG3594; Eukaryota. DR eggNOG; ENOG410XQHI; LUCA. DR GeneTree; ENSGT00760000118906; -. DR HOGENOM; HOG000231254; -. DR HOVERGEN; HBG106438; -. DR InParanoid; P22223; -. DR KO; K06796; -. DR OMA; AGWLAMD; -. DR OrthoDB; EOG091G05OA; -. DR PhylomeDB; P22223; -. DR TreeFam; TF316817; -. DR Reactome; R-HSA-418990; Adherens junctions interactions. DR SIGNOR; P22223; -. DR ChiTaRS; CDH3; human. DR GeneWiki; CDH3_(gene); -. DR GenomeRNAi; 1001; -. DR PRO; PR:P22223; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000062038; -. DR CleanEx; HS_CDH3; -. DR ExpressionAtlas; P22223; baseline and differential. DR Genevisible; P22223; HS. DR GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0034332; P:adherens junction organization; TAS:Reactome. DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:UniProtKB. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. 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: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 monophenol monooxygenase activity; IMP:UniProtKB. DR GO; GO:0060901; P:regulation of hair cycle by canonical Wnt signaling pathway; IMP:UniProtKB. DR GO; GO:0042493; P:response to drug; 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; IPR002126; Cadherin. DR InterPro; IPR015919; Cadherin-like. DR InterPro; IPR020894; Cadherin_CS. DR InterPro; IPR000233; Cadherin_cytoplasmic-dom. DR InterPro; IPR014868; Cadherin_pro_dom. DR InterPro; IPR027397; Catenin_binding_dom_sf. 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; KW Cell membrane; Cleavage on pair of basic residues; Complete proteome; KW Disease mutation; Ectodermal dysplasia; Glycoprotein; Hypotrichosis; KW Membrane; Metal-binding; Polymorphism; Reference proteome; Repeat; KW Sensory transduction; Signal; Transmembrane; Transmembrane helix; KW Vision. FT SIGNAL 1 24 {ECO:0000255}. FT PROPEP 25 107 FT /FTId=PRO_0000003745. FT CHAIN 108 829 Cadherin-3. FT /FTId=PRO_0000003746. FT TOPO_DOM 108 654 Extracellular. {ECO:0000255}. FT TRANSMEM 655 677 Helical. {ECO:0000255}. FT TOPO_DOM 678 829 Cytoplasmic. {ECO:0000255}. FT DOMAIN 108 215 Cadherin 1. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 216 328 Cadherin 2. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 329 440 Cadherin 3. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 441 546 Cadherin 4. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT DOMAIN 547 650 Cadherin 5. {ECO:0000255|PROSITE- FT ProRule:PRU00043}. FT COMPBIAS 785 800 Ser-rich. FT CARBOHYD 200 200 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 566 566 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT VAR_SEQ 761 829 NLKAANTDPTAPPYDTLLVFDYEGSGSDAASLSSLTSSASD FT QDQDYDYLNEWGSRFKKLADMYGGGEDD -> GRGERGSQR FT GNGGLQLARGRTRRS (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_024820. FT VARIANT 237 237 V -> M (in dbSNP:rs17854171). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_031929. FT VARIANT 322 322 N -> I (in EEMS; dbSNP:rs121434543). FT {ECO:0000269|PubMed:15805154}. FT /FTId=VAR_033010. FT VARIANT 477 477 R -> H (in dbSNP:rs34494880). FT /FTId=VAR_031930. FT VARIANT 503 503 R -> H (in HJMD; dbSNP:rs121434542). FT {ECO:0000269|PubMed:12445216}. FT /FTId=VAR_015422. FT VARIANT 563 563 Q -> H (in dbSNP:rs1126933). FT {ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15805154, FT ECO:0000269|PubMed:2793940, FT ECO:0000269|Ref.3}. FT /FTId=VAR_031931. FT STRAND 108 110 {ECO:0000244|PDB:4ZMQ}. FT STRAND 114 119 {ECO:0000244|PDB:4ZMY}. FT STRAND 124 130 {ECO:0000244|PDB:4ZMY}. FT HELIX 134 137 {ECO:0000244|PDB:4ZMY}. FT STRAND 141 148 {ECO:0000244|PDB:4ZMY}. FT TURN 149 151 {ECO:0000244|PDB:4ZMY}. FT STRAND 152 154 {ECO:0000244|PDB:4ZMY}. FT STRAND 157 160 {ECO:0000244|PDB:4ZMY}. FT TURN 162 164 {ECO:0000244|PDB:4ZMY}. FT STRAND 166 169 {ECO:0000244|PDB:4ZMY}. FT TURN 175 177 {ECO:0000244|PDB:4ZMY}. FT STRAND 179 189 {ECO:0000244|PDB:4ZMY}. FT STRAND 194 196 {ECO:0000244|PDB:4ZMT}. FT STRAND 199 206 {ECO:0000244|PDB:4ZMY}. FT STRAND 214 216 {ECO:0000244|PDB:4ZMY}. FT STRAND 218 225 {ECO:0000244|PDB:4ZMY}. FT STRAND 232 236 {ECO:0000244|PDB:4ZMY}. FT STRAND 246 249 {ECO:0000244|PDB:4ZMY}. FT STRAND 254 262 {ECO:0000244|PDB:4ZMY}. FT STRAND 265 267 {ECO:0000244|PDB:4ZMP}. FT STRAND 270 272 {ECO:0000244|PDB:4ZMY}. FT TURN 274 276 {ECO:0000244|PDB:4ZMY}. FT STRAND 278 281 {ECO:0000244|PDB:4ZMY}. FT TURN 288 290 {ECO:0000244|PDB:4ZMY}. FT STRAND 293 301 {ECO:0000244|PDB:4ZMY}. FT HELIX 303 305 {ECO:0000244|PDB:4ZMY}. FT STRAND 309 319 {ECO:0000244|PDB:4ZMY}. 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 //