CADH1_RAT
ID CADH1_RAT Reviewed; 886 AA.
AC Q9R0T4; O35794; Q9JIV9;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Cadherin-1;
DE AltName: Full=Epithelial cadherin;
DE Short=E-cadherin;
DE AltName: Full=Uvomorulin;
DE AltName: CD_antigen=CD324;
DE Contains:
DE RecName: Full=E-Cad/CTF1;
DE Contains:
DE RecName: Full=E-Cad/CTF2;
DE Contains:
DE RecName: Full=E-Cad/CTF3;
DE Flags: Precursor;
GN Name=Cdh1;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Jejunum;
RA Asai K., Tada T., Yamamoto M., Obayashi M., Mizuno M., Toda A., Eimoto T.,
RA Kato T.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 769-872.
RC STRAIN=Fischer 344; TISSUE=Testis;
RX PubMed=10650949; DOI=10.1210/endo.141.2.7334;
RA Johnson K.J., Patel S.R., Boekelheide K.;
RT "Multiple cadherin superfamily members with unique expression profiles are
RT produced in rat testis.";
RL Endocrinology 141:675-683(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 779-846.
RC TISSUE=Mammary tumor;
RA Gibbons K.L.;
RL Thesis (1997), University of Technology / Sydney, Australia.
RN [4]
RP INTERACTION WITH RAB8B.
RX PubMed=12639940; DOI=10.1210/en.2002-220893;
RA Lau A.S., Mruk D.D.;
RT "Rab8B GTPase and junction dynamics in the testis.";
RL Endocrinology 144:1549-1563(2003).
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. CDH1 is involved in mechanisms regulating
CC cell-cell adhesions, mobility and proliferation of epithelial cells.
CC Has a potent invasive suppressor role. It is a ligand for integrin
CC alpha-E/beta-7. {ECO:0000250|UniProtKB:P12830}.
CC -!- FUNCTION: E-Cad/CTF2 promotes non-amyloidogenic degradation of Abeta
CC precursors. Has a strong inhibitory effect on APP C99 and C83
CC production (By similarity). {ECO:0000250|UniProtKB:P12830}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Component of an
CC E-cadherin/ catenin adhesion complex composed of at least E-
CC cadherin/CDH1, beta-catenin/CTNNB1 or gamma-catenin/JUP, and
CC potentially alpha-catenin/CTNNA1; the complex is located to adherens
CC junctions (By similarity). Interacts with the TRPV4 and CTNNB1 complex
CC (By similarity). Interacts with CTNND1 (By similarity). The stable
CC association of CTNNA1 is controversial as CTNNA1 was shown not to bind
CC to F-actin when assembled in the complex (By similarity).
CC Alternatively, the CTNNA1-containing complex may be linked to F-actin
CC by other proteins such as LIMA1 (By similarity). Interaction with
CC PSEN1, cleaves CDH1 resulting in the disassociation of cadherin-based
CC adherens junctions (CAJs) (By similarity). Interacts with AJAP1 and
CC DLGAP5 (By similarity). Interacts with TBC1D2 (By similarity).
CC Interacts with LIMA1 (By similarity). Interacts with CAV1 (By
CC similarity). Interacts with PIP5K1C (By similarity). Interacts with
CC DDR1; this stabilizes CDH1 at the cell surface and inhibits its
CC internalization (By similarity). Interacts with RAPGEF2 (By
CC similarity). Interacts with RAB8B (PubMed:12639940). Interacts with
CC KLRG1 (By similarity). Forms a ternary complex composed of ADAM10,
CC CADH1 and EPHA4; within the complex, CADH1 is cleaved by ADAM10 which
CC disrupts adherens junctions (By similarity). Interacts with SPEF1 (By
CC similarity). {ECO:0000250|UniProtKB:P09803,
CC ECO:0000250|UniProtKB:P12830, ECO:0000269|PubMed:12639940}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:P12830}. Cell membrane; Single-pass type I
CC membrane protein. Endosome {ECO:0000250}. Golgi apparatus, trans-Golgi
CC network {ECO:0000250}. Note=Colocalizes with DLGAP5 at sites of cell-
CC cell contact in intestinal epithelial cells. Anchored to actin
CC microfilaments through association with alpha-, beta- and gamma-
CC catenin. Sequential proteolysis induced by apoptosis or calcium influx,
CC results in translocation from sites of cell-cell contact to the
CC cytoplasm. Colocalizes with RAB11A endosomes during its transport from
CC the Golgi apparatus to the plasma membrane (By similarity).
CC {ECO:0000250}.
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 -!- PTM: During apoptosis or with calcium influx, cleaved by a membrane-
CC bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3 (By
CC similarity). Processing by the metalloproteinase, induced by calcium
CC influx, causes disruption of cell-cell adhesion and the subsequent
CC release of beta-catenin into the cytoplasm (By similarity). The
CC residual membrane-tethered cleavage product is rapidly degraded via an
CC intracellular proteolytic pathway (By similarity). Cleavage by caspase-
CC 3 releases the cytoplasmic tail resulting in disintegration of the
CC actin microfilament system (By similarity). The gamma-secretase-
CC mediated cleavage promotes disassembly of adherens junctions (By
CC similarity). During development of the cochlear organ of Corti,
CC cleavage by ADAM10 at adherens junctions promotes pillar cell
CC separation (By similarity). {ECO:0000250|UniProtKB:P09803,
CC ECO:0000250|UniProtKB:P12830}.
CC -!- PTM: N-glycosylation at Asn-641 is essential for expression, folding
CC and trafficking. Addition of bisecting N-acetylglucosamine by MGAT3
CC modulates its cell membrane location (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P12830}.
CC -!- PTM: Ubiquitinated by a SCF complex containing SKP2, which requires
CC prior phosphorylation by CK1/CSNK1A1. Ubiquitinated by CBLL1/HAKAI,
CC requires prior phosphorylation at Tyr-758 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: O-glycosylated. O-manosylated by TMTC1, TMTC2, TMTC3 or TMTC4.
CC Ser-289 and Thr-513 are O-manosylated by TMTC2 or TMTC4 but not TMTC1
CC or TMTC3. {ECO:0000250|UniProtKB:P09803}.
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DR EMBL; AB017696; BAA84920.1; -; mRNA.
DR EMBL; AF177680; AAF87055.1; -; mRNA.
DR EMBL; AJ000540; CAA04173.1; -; mRNA.
DR RefSeq; NP_112624.1; NM_031334.1.
DR AlphaFoldDB; Q9R0T4; -.
DR SMR; Q9R0T4; -.
DR BioGRID; 249721; 3.
DR STRING; 10116.ENSRNOP00000027346; -.
DR GlyGen; Q9R0T4; 11 sites.
DR PhosphoSitePlus; Q9R0T4; -.
DR SwissPalm; Q9R0T4; -.
DR PaxDb; Q9R0T4; -.
DR PRIDE; Q9R0T4; -.
DR Ensembl; ENSRNOT00000027346; ENSRNOP00000027346; ENSRNOG00000020151.
DR GeneID; 83502; -.
DR KEGG; rno:83502; -.
DR UCSC; RGD:69279; rat.
DR CTD; 999; -.
DR RGD; 69279; Cdh1.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000157175; -.
DR HOGENOM; CLU_005284_2_1_1; -.
DR InParanoid; Q9R0T4; -.
DR OMA; DFCQKNP; -.
DR OrthoDB; 182239at2759; -.
DR PhylomeDB; Q9R0T4; -.
DR TreeFam; TF316817; -.
DR Reactome; R-RNO-1474228; Degradation of the extracellular matrix.
DR Reactome; R-RNO-216083; Integrin cell surface interactions.
DR Reactome; R-RNO-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-RNO-418990; Adherens junctions interactions.
DR Reactome; R-RNO-5626467; RHO GTPases activate IQGAPs.
DR PRO; PR:Q9R0T4; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000020151; Expressed in stomach and 18 other tissues.
DR Genevisible; Q9R0T4; RN.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0043296; C:apical junction complex; ISO:RGD.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0043679; C:axon terminus; 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; ISS:UniProtKB.
DR GO; GO:0071944; C:cell periphery; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016600; C:flotillin complex; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0030027; C:lamellipodium; ISO:RGD.
DR GO; GO:0043219; C:lateral loop; ISO:RGD.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
DR GO; GO:0033268; C:node of Ranvier; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; ISO:RGD.
DR GO; GO:0005802; C:trans-Golgi network; ISO:RGD.
DR GO; GO:0045294; F:alpha-catenin binding; ISO:RGD.
DR GO; GO:0030506; F:ankyrin 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; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:RGD.
DR GO; GO:0045295; F:gamma-catenin binding; ISO:RGD.
DR GO; GO:0032794; F:GTPase activating protein binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO: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:0031532; P:actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0034332; P:adherens junction organization; ISO:RGD.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:RGD.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:RGD.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISO:RGD.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
DR GO; GO:0071681; P:cellular response to indole-3-methanol; ISO:RGD.
DR GO; GO:0071285; P:cellular response to lithium ion; ISO:RGD.
DR GO; GO:0090102; P:cochlea development; ISO:RGD.
DR GO; GO:0046697; P:decidualization; ISO:RGD.
DR GO; GO:0007566; P:embryo implantation; ISO:RGD.
DR GO; GO:0003382; P:epithelial cell morphogenesis; ISO:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0060576; P:intestinal epithelial cell development; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISO:RGD.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:RGD.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0010955; P:negative regulation of protein processing; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IEP:RGD.
DR GO; GO:0021983; P:pituitary gland development; IEP:RGD.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:RGD.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0019538; P:protein metabolic process; ISO:RGD.
DR GO; GO:0060693; P:regulation of branching involved in salivary gland morphogenesis; ISO:RGD.
DR GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR GO; GO:2001222; P:regulation of neuron migration; ISO:RGD.
DR GO; GO:0099576; P:regulation of protein catabolic process at postsynapse, modulating synaptic transmission; IDA:SynGO.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; ISO:RGD.
DR GO; GO:0033561; P:regulation of water loss via skin; ISO:RGD.
DR GO; GO:0140459; P:response to Gram-positive bacterium; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0060662; P:salivary gland cavitation; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0007416; P:synapse assembly; IMP:RGD.
DR GO; GO:0001829; P:trophectodermal cell differentiation; ISO:RGD.
DR GO; GO:0035847; P:uterine epithelium development; ISO:RGD.
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; IPR030049; CDH1.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR PANTHER; PTHR24027:SF319; PTHR24027:SF319; 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; 4.
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; Disulfide bond; Endosome; Glycoprotein;
KW Golgi apparatus; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..158
FT /evidence="ECO:0000255"
FT /id="PRO_0000003719"
FT CHAIN 159..886
FT /note="Cadherin-1"
FT /id="PRO_0000003720"
FT CHAIN 705..886
FT /note="E-Cad/CTF1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000236073"
FT CHAIN 736..886
FT /note="E-Cad/CTF2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000236074"
FT CHAIN 755..886
FT /note="E-Cad/CTF3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000236075"
FT TOPO_DOM 24..713
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 735..886
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 159..266
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 267..379
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 380..490
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 491..597
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 598..701
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 751..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..773
FT /note="Required for binding CTNND1 and PSEN1"
FT /evidence="ECO:0000250"
FT REGION 815..886
FT /note="Required for binding alpha, beta and"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT SITE 704..705
FT /note="Cleavage; by a metalloproteinase"
FT /evidence="ECO:0000250"
FT SITE 735..736
FT /note="Cleavage; by gamma-secretase/PS1"
FT /evidence="ECO:0000250"
FT SITE 754..755
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 757
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P12830"
FT MOD_RES 758
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P12830"
FT MOD_RES 759
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:P12830"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12830"
FT MOD_RES 797
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12830"
FT MOD_RES 842
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09803"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09803"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09803"
FT CARBOHYD 284
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000250|UniProtKB:P09803"
FT CARBOHYD 289
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000250|UniProtKB:P09803"
FT CARBOHYD 362
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P09803"
FT CARBOHYD 474
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P09803"
FT CARBOHYD 476
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P09803"
FT CARBOHYD 513
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P09803"
FT CARBOHYD 562
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 580
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P09803"
FT CARBOHYD 582
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P09803"
FT CARBOHYD 584
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P09803"
FT CARBOHYD 641
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 886 AA; 98715 MW; A9AEE28EB797A547 CRC64;
MGARCRSFSA LLLLLQVSSW LCQQPESESD SCRPGFSSEV YTFLVPERHL ERGHILGRVK
FEGCTGRPRT AFFSEDSRFK VSTDGVITVK RHLKLHKLET SFLVHAWDSS YRKLSTKVTL
KSLGHHHHRH HHRDPVSESN PELLTFPSFH QGLRRQKRDW VIPPINCPEN QKGEFPQRLV
QIKSNRDKET TVFYSITGPG ADKPPVGVFI IERETGWLKV TQPLDREAID KYLLYSHAVS
SNGEAVEDPM EIVVTVTDQN DNRPEFIQEV FEGSVAEGAL PGTSVMQVSA TDADDDINTY
NAAIAYTILS QDPELPHKNM FTVNRDTGVI SVVTSGLDRE SYPTYTLVVQ AADLQGEGLS
TTAKAVITVK DINDNAPIFN PSTYQGQVLE NEVGARIATL KVTDDDAPNT PAWNAVYTVV
NDPDHQFTVI TDPKTNEGIL KTAKGLDFEA KQQYILHVTV ENEEPFEGSL VPSTATVTVD
VVDVNEAPIF VPAEKRVEVP EDFGVGLEIA SYTAREPDTF MEQKITYRIW RDTANWLEIN
PETGVISTRA EMDREDSEHV KNSTYTALII ATDDGSPIAT GTGTLLLVLS DVNDNAPIPE
PRNMQFCQRN PKPHVITILD PDLPPNTSPF TAELTHGASV NWTIEYNDAE QESLILQPRK
DLEIGEYKIN LKLSDNQNKD QVTTLEVHVC DCEGTVNNCM KAISLEAGLQ VPAILGILGG
ILALLILILL LLLFLRRRTV VKEPLLPPDD DTRDNVYYYD EEGGGEEDQD FDLSQLHRGL
DARPEVIRND VAPTLMSMPQ YRPRPANPDE IGNFIDENLK AADSDPTAPP YDSLLVFDYE
GSGSEAASLS SLNSSESDQD QDYDYLNEWG NRFKKLADMY GGGEED
