CADH2_RAT
ID CADH2_RAT Reviewed; 906 AA.
AC Q9Z1Y3; Q9R0T5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Cadherin-2;
DE AltName: Full=Neural cadherin;
DE Short=N-cadherin;
DE AltName: CD_antigen=CD325;
DE Flags: Precursor;
GN Name=Cdh2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Testis;
RX PubMed=9528971; DOI=10.1210/endo.139.4.5958;
RA Chung S.S., Mo M.Y., Silvestrini B., Lee W.M., Cheng C.Y.;
RT "Rat testicular N-cadherin: its complementary deoxyribonucleic acid cloning
RT and regulation.";
RL Endocrinology 139:1853-1862(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Asai K., Tada T., Yamamoto M., Tada A., Mizuno M., Eimoto T., Kato T.;
RT "Rat N-cadherin cDNA.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH PCDH8, AND MUTAGENESIS OF LEU-740 AND MET-741.
RX PubMed=17988630; DOI=10.1016/j.neuron.2007.08.020;
RA Yasuda S., Tanaka H., Sugiura H., Okamura K., Sakaguchi T., Tran U.,
RA Takemiya T., Mizoguchi A., Yagita Y., Sakurai T., De Robertis E.M.,
RA Yamagata K.;
RT "Activity-induced protocadherin arcadlin regulates dendritic spine number
RT by triggering N-cadherin endocytosis via TAO2beta and p38 MAP kinases.";
RL Neuron 56:456-471(2007).
CC -!- FUNCTION: Calcium-dependent cell adhesion protein; preferentially
CC mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain
CC from another cell. Cadherins may thus contribute to the sorting of
CC heterogeneous cell types. Acts as a regulator of neural stem cells
CC quiescence by mediating anchorage of neural stem cells to ependymocytes
CC in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated
CC anchorage is affected, leading to modulate neural stem cell quiescence.
CC Plays a role in cell-to-cell junction formation between pancreatic beta
CC cells and neural crest stem (NCS) cells, promoting the formation of
CC processes by NCS cells (By similarity). CDH2 may be involved in
CC neuronal recognition mechanism. In hippocampal neurons, may regulate
CC dendritic spine density. {ECO:0000250|UniProtKB:P15116}.
CC -!- SUBUNIT: Homodimer (via extracellular region). Can also form
CC heterodimers with other cadherins (via extracellular region).
CC Dimerization occurs in trans, i.e. with a cadherin chain from another
CC cell (By similarity). Interacts with PCDH8; this complex may also
CC include TAOK2 (PubMed:17988630). The interaction with PCDH8 may lead to
CC internalization through TAOK2/p38 MAPK pathway (PubMed:17988630).
CC Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2,
CC SRC, SHC1, GAP43 and CTTN. May interact with OBSCN (via protein kinase
CC domain 2) (By similarity). {ECO:0000250|UniProtKB:P15116,
CC ECO:0000250|UniProtKB:P19022, ECO:0000269|PubMed:17988630}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15116};
CC Single-pass type I membrane protein {ECO:0000255}. Cell membrane,
CC sarcolemma {ECO:0000250|UniProtKB:P15116}. Cell junction
CC {ECO:0000250|UniProtKB:P19022}. Cell surface
CC {ECO:0000250|UniProtKB:P15116}. Note=Colocalizes with TMEM65 at the
CC intercalated disk in cardiomyocytes (By similarity). Colocalizes with
CC OBSCN at the intercalated disk and sarcolemma in cardiomyocytes (By
CC similarity). {ECO:0000250|UniProtKB:P15116}.
CC -!- TISSUE SPECIFICITY: In testis, expressed in Sertoli and germ cells.
CC {ECO:0000269|PubMed:9528971}.
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. Calcium-binding sites are
CC occupied sequentially in the order of site 3, then site 2 and site 1.
CC {ECO:0000250|UniProtKB:P15116}.
CC -!- PTM: Cleaved by MMP24. Ectodomain cleavage leads to the generation of a
CC soluble 90 kDa N-terminal soluble fragment and a 45 kDa membrane-bound
CC C-terminal fragment 1 (CTF1), which is further cleaved by gamma-
CC secretase into a 35 kDa (By similarity). Cleavage in neural stem cells
CC by MMP24 affects CDH2-mediated anchorage of neural stem cells to
CC ependymocytes in the adult subependymal zone, leading to modulate
CC neural stem cell quiescence (By similarity).
CC {ECO:0000250|UniProtKB:P15116}.
CC -!- PTM: May be phosphorylated by OBSCN. {ECO:0000250|UniProtKB:P15116}.
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DR EMBL; AF097593; AAC83818.1; -; mRNA.
DR EMBL; AB017695; BAA84919.1; -; mRNA.
DR RefSeq; NP_112623.1; NM_031333.1.
DR AlphaFoldDB; Q9Z1Y3; -.
DR SMR; Q9Z1Y3; -.
DR BioGRID; 249720; 5.
DR CORUM; Q9Z1Y3; -.
DR DIP; DIP-48902N; -.
DR IntAct; Q9Z1Y3; 2.
DR STRING; 10116.ENSRNOP00000021170; -.
DR GlyGen; Q9Z1Y3; 8 sites, 4 N-linked glycans (1 site).
DR iPTMnet; Q9Z1Y3; -.
DR PhosphoSitePlus; Q9Z1Y3; -.
DR SwissPalm; Q9Z1Y3; -.
DR PaxDb; Q9Z1Y3; -.
DR PRIDE; Q9Z1Y3; -.
DR GeneID; 83501; -.
DR KEGG; rno:83501; -.
DR CTD; 1000; -.
DR RGD; 69280; Cdh2.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q9Z1Y3; -.
DR OrthoDB; 191117at2759; -.
DR PhylomeDB; Q9Z1Y3; -.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-418990; Adherens junctions interactions.
DR Reactome; R-RNO-525793; Myogenesis.
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q9Z1Y3; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005912; C:adherens junction; IDA:RGD.
DR GO; GO:0045177; C:apical part of cell; IBA:GO_Central.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0016327; C:apicolateral plasma membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0016342; C:catenin complex; ISO:RGD.
DR GO; GO:0030054; C:cell junction; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005916; C:fascia adherens; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; EXP:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IDA:SynGO.
DR GO; GO:0014704; C:intercalated disc; IDA:BHF-UCL.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0044853; C:plasma membrane raft; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:BHF-UCL.
DR GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
DR GO; GO:0045294; F:alpha-catenin binding; ISO:RGD.
DR GO; GO:0008013; F:beta-catenin binding; IPI:RGD.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0045295; F:gamma-catenin binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0048514; P:blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0048854; P:brain morphogenesis; ISO:RGD.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IMP:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:RGD.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISS:UniProtKB.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; ISS:UniProtKB.
DR GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
DR GO; GO:0010001; P:glial cell differentiation; ISS:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
DR GO; GO:0048872; P:homeostasis of number of cells; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:RGD.
DR GO; GO:0090497; P:mesenchymal cell migration; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; EXP:SynGO.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0014032; P:neural crest cell development; ISS:UniProtKB.
DR GO; GO:0060563; P:neuroepithelial cell differentiation; ISO:RGD.
DR GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; ISO:RGD.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0060019; P:radial glial cell differentiation; ISO:RGD.
DR GO; GO:0050770; P:regulation of axonogenesis; IMP:RGD.
DR GO; GO:0031641; P:regulation of myelination; IMP:RGD.
DR GO; GO:0070445; P:regulation of oligodendrocyte progenitor proliferation; ISO:RGD.
DR GO; GO:1902897; P:regulation of postsynaptic density protein 95 clustering; ISO:RGD.
DR GO; GO:0032880; P:regulation of protein localization; IMP:RGD.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IMP:RGD.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:SynGO.
DR GO; GO:0051146; P:striated muscle cell differentiation; ISO:RGD.
DR GO; GO:0007416; P:synapse assembly; IMP:RGD.
DR GO; GO:0099560; P:synaptic membrane adhesion; IC:SynGO.
DR GO; GO:0021537; P:telencephalon development; ISO:RGD.
DR GO; GO:0003323; P:type B pancreatic cell development; ISS:UniProtKB.
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 InterPro; IPR030051; CDH2.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR PANTHER; PTHR24027:SF79; PTHR24027:SF79; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF01049; Cadherin_C; 1.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..159
FT /evidence="ECO:0000255"
FT /id="PRO_0000003735"
FT CHAIN 160..906
FT /note="Cadherin-2"
FT /id="PRO_0000003736"
FT TOPO_DOM 160..724
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 725..745
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 746..906
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 160..267
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 268..382
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 383..497
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 498..603
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 604..717
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 863..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19022"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
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 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 740
FT /note="L->P: Decrease in PCDH8-binding; alone or when
FT associated with G-741."
FT /evidence="ECO:0000269|PubMed:17988630"
FT MUTAGEN 741
FT /note="M->G: Decrease in PCDH8-binding; when associated
FT with P-740."
FT /evidence="ECO:0000269|PubMed:17988630"
FT CONFLICT 7
FT /note="G -> A (in Ref. 2; BAA84919)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="T -> D (in Ref. 2; BAA84919)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="A -> R (in Ref. 2; BAA84919)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="A -> V (in Ref. 2; BAA84919)"
FT /evidence="ECO:0000305"
FT CONFLICT 658
FT /note="N -> K (in Ref. 2; BAA84919)"
FT /evidence="ECO:0000305"
FT CONFLICT 724
FT /note="T -> A (in Ref. 2; BAA84919)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 906 AA; 99686 MW; 97D9937FD8D1F8B5 CRC64;
MCRIAGGPRT LLPLLAALLQ ASLEASGELA LCKTGFPEDV YSAVLPKTVH EGQPLLNVKF
SNCNRKRKVQ YESSEPADFK VDEDGTVYAV RSFPLSAEQA KFLIYAQDKE TQEKWQVAVN
LSLEPSLTEE PMKEPHEIEE IVFPRQLAKH SGALQRQKRD WVIPPINLPE NSRGPFPQEL
VRIRSDRDKN LSLRYSVTGP GADQPPTGIF IINPISGQLS VTKPLDRELI ARFHLRAHAV
DINGNQVENP IDIVINVIDM NDNRPEFLHQ VWNGSVPEGS KPGTYVMTVT AIDADDPNAL
NGMLRYRILS QAPSTPSPNM FTINNETGDI ITVAAGLDRE KVQQYTLIIQ ATDMEGNPTY
GLSNTATAVI TVTDVNDNPP EFTAMTFYGE VPENRVDVIV ANLTVTDKDQ PHTPAWNAAY
RISGGDPTGR FAILTDPNSN DGLVTVVKPI DFETNRMFVL TVAAENQVPL AKGIQHPPQS
TATVSVTVID VNENPYFAPN PKIIRQEEGL HAGTMLTTLT AQDPDRYMQQ NIRYTKLSDP
ANWLKIDPVN GQITTIAVLD RESPNVKNNI YNATFLASDN GIPPMSGTGT LQIYLLDIND
NAPQVLPQEA ETCETPEPNS INITALDYDI DPNAGPFAFD LPLSPATIKR NWTITRLNGD
FAQLNLKIKF LEAGIYEVPI VITDSGNPPK SNISILRVKV CQCDSNGDCT DVDRIVGAGL
GTGTIIAILL CIIILLILVL MFVVWMKRRD KERQAKQLLI DPEDDVRDNI LKYDEEGGGE
EDQDYDLSQL QQPDTVEPDA IKPVGIRRLD ERPIHAEPQY PVRSAAPHPG DIGDFINEGL
KAADNDPTAP PYDSLLVFDY EGSGSTAGSL SSLNSSSSGG DQDYDYLNDW GPRFKKLADM
YGGGDD
