ID   PCD16_HUMAN             Reviewed;        3298 AA.
AC   Q96JQ0; O15098;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Protocadherin-16;
DE   AltName: Full=Cadherin-19;
DE   AltName: Full=Cadherin-25;
DE   AltName: Full=Fibroblast cadherin-1;
DE   AltName: Full=Protein dachsous homolog 1;
DE   Flags: Precursor;
GN   Name=DCHS1; Synonyms=CDH19, CDH25, FIB1, KIAA1773, PCDH16;
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].
RC   TISSUE=Brain;
RX   PubMed=11597768; DOI=10.1016/s0169-328x(01)00218-2;
RA   Nakajima D., Nakayama M., Kikuno R., Hirosawa M., Nagase T., Ohara O.;
RT   "Identification of three novel non-classical cadherin genes through
RT   comprehensive analysis of large cDNAs.";
RL   Brain Res. Mol. Brain Res. 94:85-95(2001).
RN   [2]
RP   SEQUENCE REVISION.
RA   Nakajima D., Nakayama M., Kikuno R., Nagase T., Ohara O.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 434-570, AND TISSUE SPECIFICITY.
RX   PubMed=9199196; DOI=10.1006/bbrc.1997.6707;
RA   Matsuyoshi N., Imamura S.;
RT   "Multiple cadherins are expressed in human fibroblasts.";
RL   Biochem. Biophys. Res. Commun. 235:355-358(1997).
RN   [4]
RP   FUNCTION, INVOLVEMENT IN MVP2, VARIANTS MVP2 LEU-197; CYS-2330 AND
RP   HIS-2513, AND CHARACTERIZATION OF VARIANTS MVP2 LEU-197; CYS-2330 AND
RP   HIS-2513.
RX   PubMed=26258302; DOI=10.1038/nature14670;
RA   Durst R., Sauls K., Peal D.S., deVlaming A., Toomer K., Leyne M.,
RA   Salani M., Talkowski M.E., Brand H., Perrocheau M., Simpson C., Jett C.,
RA   Stone M.R., Charles F., Chiang C., Lynch S.N., Bouatia-Naji N.,
RA   Delling F.N., Freed L.A., Tribouilloy C., Le Tourneau T., LeMarec H.,
RA   Fernandez-Friera L., Solis J., Trujillano D., Ossowski S., Estivill X.,
RA   Dina C., Bruneval P., Chester A., Schott J.J., Irvine K.D., Mao Y.,
RA   Wessels A., Motiwala T., Puceat M., Tsukasaki Y., Menick D.R.,
RA   Kasiganesan H., Nie X., Broome A.M., Williams K., Johnson A.,
RA   Markwald R.R., Jeunemaitre X., Hagege A., Levine R.A., Milan D.J.,
RA   Norris R.A., Slaugenhaupt S.A.;
RT   "Mutations in DCHS1 cause mitral valve prolapse.";
RL   Nature 525:109-113(2015).
RN   [5]
RP   VARIANT [LARGE SCALE ANALYSIS] TRP-1583.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [6]
RP   VARIANT VMLDS1 ILE-2370.
RX   PubMed=24056717; DOI=10.1038/ng.2765;
RA   Cappello S., Gray M.J., Badouel C., Lange S., Einsiedler M., Srour M.,
RA   Chitayat D., Hamdan F.F., Jenkins Z.A., Morgan T., Preitner N., Uster T.,
RA   Thomas J., Shannon P., Morrison V., Di Donato N., Van Maldergem L.,
RA   Neuhann T., Newbury-Ecob R., Swinkells M., Terhal P., Wilson L.C.,
RA   Zwijnenburg P.J., Sutherland-Smith A.J., Black M.A., Markie D.,
RA   Michaud J.L., Simpson M.A., Mansour S., McNeill H., Goetz M.,
RA   Robertson S.P.;
RT   "Mutations in genes encoding the cadherin receptor-ligand pair DCHS1 and
RT   FAT4 disrupt cerebral cortical development.";
RL   Nat. Genet. 45:1300-1308(2013).
CC   -!- FUNCTION: Calcium-dependent cell-adhesion protein. Mediates functions
CC       in neuroprogenitor cell proliferation and differentiation. In the
CC       heart, has a critical role for proper morphogenesis of the mitral
CC       valve, acting in the regulation of cell migration involved in valve
CC       formation (PubMed:26258302). {ECO:0000269|PubMed:26258302}.
CC   -!- SUBUNIT: Heterophilic interaction with FAT4; this interaction affects
CC       their respective protein levels. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. Note=In the embryonic cortex, FAT4 and
CC       DCHS1 accumulated at the cell-cell boundaries located apical to the
CC       adherens junction. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in fibroblasts but not in melanocytes or
CC       keratinocytes. {ECO:0000269|PubMed:9199196}.
CC   -!- DISEASE: Van Maldergem syndrome 1 (VMLDS1) [MIM:601390]: An autosomal
CC       recessive disorder characterized by intellectual disability, typical
CC       craniofacial features, auditory malformations resulting in hearing
CC       loss, and skeletal and limb malformations. Some patients have renal
CC       hypoplasia. Brain MRI typically shows periventricular nodular
CC       heterotopia. {ECO:0000269|PubMed:24056717}. Note=The disease is caused
CC       by variants affecting the gene represented in this entry.
CC   -!- DISEASE: Mitral valve prolapse 2 (MVP2) [MIM:607829]: A form of mitral
CC       valve prolapse, a valvular heart disease characterized by abnormally
CC       elongated and thickened mitral valve leaflets, that typically show
CC       myxomatous degeneration with increased leaflet compliance. It is
CC       associated with mitral regurgitation. Myxomatous mitral valves have an
CC       abnormal layered architecture characterized by loose collagen in
CC       fibrosa, expanded spongiosa strongly positive for proteoglycans, and
CC       disrupted elastin in atrialis. In classic mitral valve prolapse,
CC       leaflets are at least 5 mm thick, whereas in the non-classic form, they
CC       are less than 5 mm thick. Severe classic mitral valve prolapse is
CC       strongly associated with arrhythmias, endocarditis, heart failure, and
CC       need for valve surgery. MVP2 inheritance is autosomal dominant.
CC       {ECO:0000269|PubMed:26258302}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB61903.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB053446; BAB61903.2; ALT_INIT; mRNA.
DR   EMBL; AB000895; BAA21133.1; -; mRNA.
DR   CCDS; CCDS7771.1; -.
DR   PIR; PC4297; PC4297.
DR   RefSeq; NP_003728.1; NM_003737.3.
DR   PDB; 8EGW; X-ray; 2.30 A; A=43-356.
DR   PDB; 8EGX; X-ray; 3.69 A; A=43-462.
DR   PDBsum; 8EGW; -.
DR   PDBsum; 8EGX; -.
DR   SMR; Q96JQ0; -.
DR   BioGRID; 114194; 16.
DR   IntAct; Q96JQ0; 6.
DR   MINT; Q96JQ0; -.
DR   STRING; 9606.ENSP00000299441; -.
DR   GlyCosmos; Q96JQ0; 14 sites, No reported glycans.
DR   GlyGen; Q96JQ0; 14 sites.
DR   iPTMnet; Q96JQ0; -.
DR   PhosphoSitePlus; Q96JQ0; -.
DR   BioMuta; DCHS1; -.
DR   DMDM; 20139065; -.
DR   jPOST; Q96JQ0; -.
DR   MassIVE; Q96JQ0; -.
DR   PaxDb; 9606-ENSP00000299441; -.
DR   PeptideAtlas; Q96JQ0; -.
DR   ProteomicsDB; 77003; -.
DR   Antibodypedia; 64000; 76 antibodies from 16 providers.
DR   DNASU; 8642; -.
DR   Ensembl; ENST00000299441.5; ENSP00000299441.3; ENSG00000166341.9.
DR   GeneID; 8642; -.
DR   KEGG; hsa:8642; -.
DR   MANE-Select; ENST00000299441.5; ENSP00000299441.3; NM_003737.4; NP_003728.1.
DR   UCSC; uc001mem.3; human.
DR   AGR; HGNC:13681; -.
DR   CTD; 8642; -.
DR   DisGeNET; 8642; -.
DR   GeneCards; DCHS1; -.
DR   HGNC; HGNC:13681; DCHS1.
DR   HPA; ENSG00000166341; Low tissue specificity.
DR   MalaCards; DCHS1; -.
DR   MIM; 601390; phenotype.
DR   MIM; 603057; gene.
DR   MIM; 607829; phenotype.
DR   neXtProt; NX_Q96JQ0; -.
DR   OpenTargets; ENSG00000166341; -.
DR   Orphanet; 314679; Cerebrofacioarticular syndrome.
DR   Orphanet; 741; Familial mitral valve prolapse.
DR   PharmGKB; PA33000; -.
DR   VEuPathDB; HostDB:ENSG00000166341; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000161822; -.
DR   HOGENOM; CLU_000265_2_0_1; -.
DR   InParanoid; Q96JQ0; -.
DR   OMA; QPKDYTF; -.
DR   OrthoDB; 2961370at2759; -.
DR   PhylomeDB; Q96JQ0; -.
DR   TreeFam; TF316403; -.
DR   PathwayCommons; Q96JQ0; -.
DR   SignaLink; Q96JQ0; -.
DR   BioGRID-ORCS; 8642; 11 hits in 1146 CRISPR screens.
DR   ChiTaRS; DCHS1; human.
DR   GeneWiki; DCHS1; -.
DR   GenomeRNAi; 8642; -.
DR   Pharos; Q96JQ0; Tbio.
DR   PRO; PR:Q96JQ0; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q96JQ0; Protein.
DR   Bgee; ENSG00000166341; Expressed in tendon of biceps brachii and 185 other cell types or tissues.
DR   GO; GO:0045177; C:apical part of cell; IEA:Ensembl.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; NAS: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:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; NAS:UniProtKB.
DR   GO; GO:0003273; P:cell migration involved in endocardial cushion formation; IMP:UniProtKB.
DR   GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR   GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR   GO; GO:0072137; P:condensed mesenchymal cell proliferation; IEA:Ensembl.
DR   GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR   GO; GO:0035329; P:hippo signaling; ISS:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0003192; P:mitral valve formation; IMP:UniProtKB.
DR   GO; GO:0021915; P:neural tube development; IEA:Ensembl.
DR   GO; GO:0022008; P:neurogenesis; ISS:UniProtKB.
DR   GO; GO:0043931; P:ossification involved in bone maturation; IEA:Ensembl.
DR   GO; GO:0007389; P:pattern specification process; IEA:Ensembl.
DR   GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR   CDD; cd11304; Cadherin_repeat; 27.
DR   Gene3D; 2.60.40.60; Cadherins; 27.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   PANTHER; PTHR24028; CADHERIN-87A; 1.
DR   PANTHER; PTHR24028:SF310; STARRY NIGHT; 1.
DR   Pfam; PF00028; Cadherin; 24.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 27.
DR   SUPFAM; SSF49313; Cadherin-like; 27.
DR   PROSITE; PS00232; CADHERIN_1; 18.
DR   PROSITE; PS50268; CADHERIN_2; 27.
DR   Genevisible; Q96JQ0; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell adhesion; Cell membrane; Deafness;
KW   Disease variant; Glycoprotein; Intellectual disability; Membrane;
KW   Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..42
FT                   /evidence="ECO:0000255"
FT   CHAIN           43..3298
FT                   /note="Protocadherin-16"
FT                   /id="PRO_0000004000"
FT   TOPO_DOM        43..2940
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        2941..2961
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        2962..3298
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          43..143
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          144..255
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          256..362
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          367..472
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          474..578
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          579..685
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          686..790
FT                   /note="Cadherin 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          791..894
FT                   /note="Cadherin 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          895..1000
FT                   /note="Cadherin 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1001..1111
FT                   /note="Cadherin 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1112..1211
FT                   /note="Cadherin 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1218..1324
FT                   /note="Cadherin 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1333..1436
FT                   /note="Cadherin 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1437..1546
FT                   /note="Cadherin 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1547..1649
FT                   /note="Cadherin 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1650..1751
FT                   /note="Cadherin 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1752..1855
FT                   /note="Cadherin 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1856..1960
FT                   /note="Cadherin 18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          1965..2068
FT                   /note="Cadherin 19"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          2069..2171
FT                   /note="Cadherin 20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          2172..2277
FT                   /note="Cadherin 21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          2278..2376
FT                   /note="Cadherin 22"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          2377..2482
FT                   /note="Cadherin 23"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          2483..2602
FT                   /note="Cadherin 24"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          2603..2706
FT                   /note="Cadherin 25"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          2707..2813
FT                   /note="Cadherin 26"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          2814..2933
FT                   /note="Cadherin 27"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REGION          2065..2094
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2986..3040
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3062..3082
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3233..3298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3239..3262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         3055
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:E9PVD3"
FT   CARBOHYD        217
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        402
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        584
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1521
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1718
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1996
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2361
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2428
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2569
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2761
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2792
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        2862
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         197
FT                   /note="P -> L (in MVP2; uncertain significance; has no
FT                   significant effect on protein levels; dbSNP:rs145099391)"
FT                   /evidence="ECO:0000269|PubMed:26258302"
FT                   /id="VAR_075048"
FT   VARIANT         1583
FT                   /note="R -> W (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs148882462)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036110"
FT   VARIANT         1949
FT                   /note="T -> M (in dbSNP:rs4758443)"
FT                   /id="VAR_048577"
FT   VARIANT         2172
FT                   /note="L -> Q (in dbSNP:rs56920123)"
FT                   /id="VAR_061074"
FT   VARIANT         2330
FT                   /note="R -> C (in MVP2; loss-of-function mutation; results
FT                   in reduced protein levels; results in increased protein
FT                   degradation; dbSNP:rs768737101)"
FT                   /evidence="ECO:0000269|PubMed:26258302"
FT                   /id="VAR_075049"
FT   VARIANT         2331
FT                   /note="V -> I (in dbSNP:rs7924553)"
FT                   /id="VAR_048578"
FT   VARIANT         2359
FT                   /note="R -> C (in dbSNP:rs2659875)"
FT                   /id="VAR_048579"
FT   VARIANT         2370
FT                   /note="N -> I (in VMLDS1; dbSNP:rs483352919)"
FT                   /evidence="ECO:0000269|PubMed:24056717"
FT                   /id="VAR_070928"
FT   VARIANT         2513
FT                   /note="R -> H (in MVP2; uncertain significance;
FT                   loss-of-function mutation; results in reduced protein
FT                   levels; results in increased protein degradation;
FT                   dbSNP:rs201457110)"
FT                   /evidence="ECO:0000269|PubMed:26258302"
FT                   /id="VAR_075050"
FT   STRAND          44..52
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   HELIX           64..67
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   HELIX           88..91
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   TURN            96..98
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          100..105
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   TURN            109..111
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          114..120
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          126..134
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          146..153
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   HELIX           173..175
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          176..184
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   TURN            188..190
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          191..197
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   HELIX           199..201
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          203..209
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   TURN            215..217
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          220..229
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          231..233
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          236..246
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          254..256
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          258..265
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          273..276
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   HELIX           285..288
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          291..294
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   TURN            296..298
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          305..307
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   TURN            309..311
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          313..316
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   TURN            322..324
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          326..335
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          338..340
FT                   /evidence="ECO:0007829|PDB:8EGW"
FT   STRAND          343..353
FT                   /evidence="ECO:0007829|PDB:8EGW"
SQ   SEQUENCE   3298 AA;  346181 MW;  6EE8D28BEF0795DB CRC64;
     MQKELGIVPS CPGMKSPRPH LLLPLLLLLL LLLGAGVPGA WGQAGSLDLQ IDEEQPAGTL
     IGDISAGLPA GTAAPLMYFI SAQEGSGVGT DLAIDEHSGV VRTARVLDRE QRDRYRFTAV
     TPDGATVEVT VRVADINDHA PAFPQARAAL QVPEHTAFGT RYPLEPARDA DAGRLGTQGY
     ALSGDGAGET FRLETRPGPD GTPVPELVVT GELDRENRSH YMLQLEAYDG GSPPRRAQAL
     LDVTLLDIND HAPAFNQSRY HAVVSESLAP GSPVLQVFAS DADAGVNGAV TYEINRRQSE
     GDGPFSIDAH TGLLQLERPL DFEQRRVHEL VVQARDGGAH PELGSAFVTV HVRDANDNQP
     SMTVIFLSAD GSPQVSEAAP PGQLVARISV SDPDDGDFAH VNVSLEGGEG HFALSTQDSV
     IYLVCVARRL DREERDAYNL RVTATDSGSP PLRAEAAFVL HVTDVNDNAP AFDRQLYRPE
     PLPEVALPGS FVVRVTARDP DQGTNGQVTY SLAPGAHTHW FSIDPTSGII TTAASLDYEL
     EPQPQLIVVA TDGGLPPLAS SATVSVALQD VNDNEPQFQR TFYNASLPEG TQPGTCFLQV
     TATDADSGPF GLLSYSLGAG LGSSGSPPFR IDAHSGDVCT TRTLDRDQGP SSFDFTVTAV
     DGGGLKSMVY VKVFLSDEND NPPQFYPREY AASISAQSPP GTAVLRLRAH DPDQGSHGRL
     SYHILAGNSP PLFTLDEQSG LLTVAWPLAR RANSVVQLEI GAEDGGGLQA EPSARVDISI
     VPGTPTPPIF EQLQYVFSVP EDVAPGTSVG IVQAHNPPGR LAPVTLSLSG GDPRGLFSLD
     AVSGLLQTLR PLDRELLGPV LELEVRAGSG VPPAFAVARV RVLLDDVNDN SPAFPAPEDT
     VLLPPNTAPG TPIYTLRALD PDSGVNSRVT FTLLAGGGGA FTVDPTTGHV RLMRPLGPSG
     GPAHELELEA RDGGSPPRTS HFRLRVVVQD VGTRGLAPRF NSPTYRVDLP SGTTAGTQVL
     QVQAQAPDGG PITYHLAAEG ASSPFGLEPQ SGWLWVRAAL DREAQELYIL KVMAVSGSKA
     ELGQQTGTAT VRVSILNQNE HSPRLSEDPT FLAVAENQPP GTSVGRVFAT DRDSGPNGRL
     TYSLQQLSED SKAFRIHPQT GEVTTLQTLD REQQSSYQLL VQVQDGGSPP RSTTGTVHVA
     VLDLNDNSPT FLQASGAAGG GLPIQVPDRV PPGTLVTTLQ AKDPDEGENG TILYTLTGPG
     SELFSLHPHS GELLTAAPLI RAERPHYVLT LSAHDQGSPP RSASLQLLVQ VLPSARLAEP
     PPDLAERDPA APVPVVLTVT AAEGLRPGSL LGSVAAPEPA GVGALTYTLV GGADPEGTFA
     LDAASGRLYL ARPLDFEAGP PWRALTVRAE GPGGAGARLL RVQVQVQDEN EHAPAFARDP
     LALALPENPE PGAALYTFRA SDADGPGPNS DVRYRLLRQE PPVPALRLDA RTGALSAPRG
     LDRETTPALL LLVEATDRPA NASRRRAARV SARVFVTDEN DNAPVFASPS RVRLPEDQPP
     GPAALHVVAR DPDLGEAARV SYRLASGGDG HFRLHSSTGA LSVVRPLDRE QRAEHVLTVV
     ASDHGSPPRS ATQVLTVSVA DVNDEAPTFQ QQEYSVLLRE NNPPGTSLLT LRATDPDVGA
     NGQVTYGGVS SESFSLDPDT GVLTTLRALD REEQEEINLT VYAQDRGSPP QLTHVTVRVA
     VEDENDHAPT FGSAHLSLEV PEGQDPQTLT MLRASDPDVG ANGQLQYRIL DGDPSGAFVL
     DLASGEFGTM RPLDREVEPA FQLRIEARDG GQPALSATLL LTVTVLDAND HAPAFPVPAY
     SVEVPEDVPA GTLLLQLQAH DPDAGANGHV TYYLGAGTAG AFLLEPSSGE LRTAAALDRE
     QCPSYTFSVS AVDGAAAGPL STTVSVTITV RDVNDHAPTF PTSPLRLRLP RPGPSFSTPT
     LALATLRAED RDAGANASIL YRLAGTPPPG TTVDSYTGEI RVARSPVALG PRDRVLFIVA
     TDLGRPARSA TGVIIVGLQG EAERGPRFPR ASSEATIREN APPGTPIVSP RAVHAGGTNG
     PITYSILSGN EKGTFSIQPS TGAITVRSAE GLDFEVSPRL RLVLQAESGG AFAFTVLTLT
     LQDANDNAPR FLRPHYVAFL PESRPLEGPL LQVEADDLDQ GSGGQISYSL AASQPARGLF
     HVDPTTGTIT TTAILDREIW AETRLVLMAT DRGSPALVGS ATLTVMVIDT NDNRPTIPQP
     WELRVSEDAL LGSEIAQVTG NDVDSGPVLW YVLSPSGPQD PFSVGRYGGR VSLTGPLDFE
     QCDRYQLQLL AHDGPHEGRA NLTVLVEDVN DNAPAFSQSL YQVMLLEHTP PGSAILSVSA
     TDRDSGANGH ISYHLASPAD GFSVDPNNGT LFTIVGTVAL GHDGSGAVDV VLEARDHGAP
     GRAARATVHV QLQDQNDHAP SFTLSHYRVA VTEDLPPGST LLTLEATDAD GSRSHAAVDY
     SIISGNWGRV FQLEPRLAEA GESAGPGPRA LGCLVLLEPL DFESLTQYNL TVAAADRGQP
     PQSSVVPVTV TVLDVNDNPP VFTRASYRVT VPEDTPVGAE LLHVEASDAD PGPHGLVRFT
     VSSGDPSGLF ELDESSGTLR LAHALDCETQ ARHQLVVQAA DPAGAHFALA PVTIEVQDVN
     DHGPAFPLNL LSTSVAENQP PGTLVTTLHA IDGDAGAFGR LRYSLLEAGP GPEGREAFAL
     NSSTGELRAR VPFDYEHTES FRLLVGAADA GNLSASVTVS VLVTGEDEYD PVFLAPAFHF
     QVPEGARRGH SLGHVQATDE DGGADGLVLY SLATSSPYFG INQTTGALYL RVDSRAPGSG
     TATSGGGGRT RREAPRELRL EVIARGPLPG SRSATVPVTV DITHTALGLA PDLNLLLVGA
     VAASLGVVVV LALAALVLGL VRARSRKAEA APGPMSQAAP LASDSLQKLG REPPSPPPSE
     HLYHQTLPSY GGPGAGGPYP RGGSLDPSHS SGRGSAEAAE DDEIRMINEF PRVASVASSL
     AARGPDSGIQ QDADGLSDTS CEPPAPDTWY KGRKAGLLLP GAGATLYREE GPPATATAFL
     GGCGLSPAPT GDYGFPADGK PCVAGALTAI VAGEEELRGS YNWDYLLSWC PQFQPLASVF
     TEIARLKDEA RPCPPAPRID PPPLITAVAH PGAKSVPPKP ANTAAARAIF PPASHRSPIS
     HEGSLSSAAM SPSFSPSLSP LAARSPVVSP FGVAQGPSAS ALSAESGLEP PDDTELHI
//