AFAD_RAT
ID AFAD_RAT Reviewed; 1829 AA.
AC O35889; O35890;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Afadin;
DE AltName: Full=Afadin adherens junction formation factor {ECO:0000312|RGD:708561};
DE AltName: Full=Protein Af-6;
GN Name=Afdn {ECO:0000312|RGD:708561}; Synonyms=Af6, Mllt4;
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] (ISOFORMS 1 AND 2), PARTIAL PROTEIN SEQUENCE,
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP F-ACTIN.
RC TISSUE=Brain;
RX PubMed=9334353; DOI=10.1083/jcb.139.2.517;
RA Mandai K., Nakanishi H., Satoh A., Obaishi H., Wada M., Nishioka H.,
RA Itoh M., Mizoguchi A., Aoki T., Fujimoto T., Matsuda Y., Tsukita S.,
RA Takai Y.;
RT "Afadin: a novel actin filament-binding protein with one PDZ domain
RT localized at cadherin-based cell-to-cell adherens junction.";
RL J. Cell Biol. 139:517-528(1997).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-512; SER-1090;
RP SER-1114; SER-1147; SER-1150; SER-1189; SER-1282; SER-1506; SER-1517;
RP SER-1726; SER-1779 AND SER-1804, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP INTERACTION WITH ADAM10.
RX PubMed=30463011; DOI=10.1016/j.celrep.2018.10.088;
RA Shah J., Rouaud F., Guerrera D., Vasileva E., Popov L.M., Kelley W.L.,
RA Rubinstein E., Carette J.E., Amieva M.R., Citi S.;
RT "A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to
RT Promote alpha-Toxin Cytotoxicity.";
RL Cell Rep. 25:2132-2147(2018).
CC -!- FUNCTION: Belongs to an adhesion system, probably together with the E-
CC cadherin-catenin system, which plays a role in the organization of
CC homotypic, interneuronal and heterotypic cell-cell adherens junctions
CC (AJs) (PubMed:9334353). Nectin- and actin-filament-binding protein that
CC connects nectin to the actin cytoskeleton (PubMed:9334353). May play a
CC key role in the organization of epithelial structures of the embryonic
CC ectoderm (By similarity). Essential for the organization of adherens
CC junctions (By similarity). {ECO:0000250|UniProtKB:P55196,
CC ECO:0000250|UniProtKB:Q9QZQ1, ECO:0000269|PubMed:9334353}.
CC -!- SUBUNIT: Homodimer. Interacts with F-actin, nectin and NECTIN3.
CC Essential for the association of nectin and E-cadherin. Isoform 2/s-
CC afadin does not interact with F-actin. Interacts with ZO-1 and
CC occludin, but probably in an indirect manner. Interacts with RIT1,
CC RIT2, NRXN1 and BCR (By similarity). Interacts with ADAM10; the
CC interaction locks ADAM10 at adherens junctions following ADAM10
CC recruitment to adherens junctions by TSPAN33 (PubMed:30463011).
CC {ECO:0000250, ECO:0000269|PubMed:30463011}.
CC -!- INTERACTION:
CC O35889; P26231: Ctnna1; Xeno; NbExp=2; IntAct=EBI-6654073, EBI-647895;
CC O35889; Q16643: DBN1; Xeno; NbExp=3; IntAct=EBI-6654073, EBI-351394;
CC O35889; Q8VC66: Ssx2ip; Xeno; NbExp=4; IntAct=EBI-6654073, EBI-6654049;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:9334353}. Note=Not found at cell-matrix AJs.
CC {ECO:0000269|PubMed:9334353}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=l-afadin, p205;
CC IsoId=O35889-1; Sequence=Displayed;
CC Name=2; Synonyms=s-afadin, p190;
CC IsoId=O35889-2; Sequence=VSP_011726, VSP_011727, VSP_011728,
CC VSP_011729;
CC -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed, including in heart,
CC brain, spleen, lung, liver, skeletal muscle, kidney and testis. Isoform
CC 2 is mainly expressed in the brain. {ECO:0000269|PubMed:9334353}.
CC -!- MISCELLANEOUS: Isoform 1 increases the viscosity of F-actin in a dose-
CC dependent manner. Isoform 1 causes F-actin to associate into bundles
CC and meshworks.
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DR EMBL; U83231; AAC53391.1; -; mRNA.
DR EMBL; U83230; AAC53390.1; -; mRNA.
DR PIR; T41751; T41751.
DR PIR; T42092; T42092.
DR RefSeq; NP_037349.1; NM_013217.2. [O35889-1]
DR AlphaFoldDB; O35889; -.
DR BMRB; O35889; -.
DR SMR; O35889; -.
DR BioGRID; 247803; 2.
DR ELM; O35889; -.
DR IntAct; O35889; 15.
DR MINT; O35889; -.
DR STRING; 10116.ENSRNOP00000029044; -.
DR iPTMnet; O35889; -.
DR PhosphoSitePlus; O35889; -.
DR jPOST; O35889; -.
DR PRIDE; O35889; -.
DR Ensembl; ENSRNOT00000106034; ENSRNOP00000088861; ENSRNOG00000023753. [O35889-1]
DR GeneID; 26955; -.
DR KEGG; rno:26955; -.
DR CTD; 4301; -.
DR RGD; 708561; Afdn.
DR eggNOG; KOG1892; Eukaryota.
DR GeneTree; ENSGT00940000155237; -.
DR InParanoid; O35889; -.
DR OrthoDB; 23029at2759; -.
DR PhylomeDB; O35889; -.
DR Reactome; R-RNO-418990; Adherens junctions interactions.
DR PRO; PR:O35889; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005912; C:adherens junction; IDA: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; IDA:RGD.
DR GO; GO:0030054; C:cell junction; ISO:RGD.
DR GO; GO:0044291; C:cell-cell contact zone; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0046930; C:pore complex; ISO:RGD.
DR GO; GO:0036477; C:somatodendritic compartment; IDA:RGD.
DR GO; GO:0070160; C:tight junction; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
DR GO; GO:0030274; F:LIM domain binding; IPI:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISO:RGD.
DR GO; GO:0034334; P:adherens junction maintenance; ISO:RGD.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISO:RGD.
DR GO; GO:0048854; P:brain morphogenesis; ISO:RGD.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISO:RGD.
DR GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
DR GO; GO:0140059; P:dendrite arborization; IMP:RGD.
DR GO; GO:0090557; P:establishment of endothelial intestinal barrier; ISO:RGD.
DR GO; GO:0061951; P:establishment of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0048872; P:homeostasis of number of cells; ISO:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:0060563; P:neuroepithelial cell differentiation; ISO:RGD.
DR GO; GO:0046931; P:pore complex assembly; ISO:RGD.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:RGD.
DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; ISO:RGD.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IMP:RGD.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:RGD.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:0061885; P:positive regulation of mini excitatory postsynaptic potential; IMP:RGD.
DR GO; GO:1902414; P:protein localization to cell junction; ISO:RGD.
DR GO; GO:0060019; P:radial glial cell differentiation; ISO:RGD.
DR GO; GO:0070445; P:regulation of oligodendrocyte progenitor proliferation; ISO:RGD.
DR GO; GO:0032880; P:regulation of protein localization; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0021537; P:telencephalon development; ISO:RGD.
DR CDD; cd00060; FHA; 1.
DR CDD; cd15471; Myo5p-like_CBD_afadin; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR037977; CBD_Afadin.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00788; RA; 2.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00240; FHA; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00314; RA; 2.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50200; RA; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell adhesion; Cell junction;
KW Coiled coil; Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1829
FT /note="Afadin"
FT /id="PRO_0000215920"
FT DOMAIN 39..133
FT /note="Ras-associating 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 246..348
FT /note="Ras-associating 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 441..507
FT /note="FHA"
FT DOMAIN 668..915
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT DOMAIN 1014..1100
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 129..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1300..1533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1574..1724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1742..1829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 146..186
FT /evidence="ECO:0000255"
FT COILED 1417..1454
FT /evidence="ECO:0000255"
FT COILED 1530..1564
FT /evidence="ECO:0000255"
FT COILED 1600..1672
FT /evidence="ECO:0000255"
FT COMPBIAS 143..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1137..1154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1382
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1519..1533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1685
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1687..1716
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1751..1765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1811..1829
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 589
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1090
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZQ1"
FT MOD_RES 1147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZQ1"
FT MOD_RES 1180
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1218
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1239
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1337
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1506
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55196"
FT MOD_RES 1726
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1779
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1804
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1812
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9QZQ1"
FT VAR_SEQ 679..685
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9334353"
FT /id="VSP_011726"
FT VAR_SEQ 1609
FT /note="R -> RQTAMPAISVLDL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9334353"
FT /id="VSP_011727"
FT VAR_SEQ 1655..1658
FT /note="RRQE -> VMVL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9334353"
FT /id="VSP_011728"
FT VAR_SEQ 1659..1829
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9334353"
FT /id="VSP_011729"
SQ SEQUENCE 1829 AA; 207678 MW; 45C597A82F109D6F CRC64;
MSAGGRDEER RKLADIIHHW NANRLDLFEI SQPTEDLEFH GVMRFYFQDK AAGNFATKCI
RVSSTATTQD VIETLAEKFR PDMRMLSSPK YSLYEVHVSG ERRLDIDEKP LVVQLNWNKD
DREGRFVLKN ENDAIPAKKA QSNGPEKQEK EGVIQNFKRT LSKKEKKEKK KREKEALRQA
SDKEERPSQG DDSENSRLAA EVYKDMPETS FTRTISNPEV VMKRRRQQKL EKRMQEFRSS
DGRPDSGGTL RIYADSLKPN IPYKTILLST TDPADFAVAE SLEKYGLEKE NPKDYCIARV
MLPPGAQHSD ERGAKEIILD DDECPLQIFR EWPSDKGILV FQLKRRPPDY IPKKMKKHVE
GKPLKGKDRA DGSGYGSALP PEKLPYLVEL SPGRRNHFAY YSYHTYEDGS DSRDKPKLYR
LQLSVTEVGT EKFDDNSIQL FGPGIQPHHC DLTNMDGVVT VTPRSMDAET YVDGQRISET
TMLQSGMRLQ FGTSHVFKFV DPIQDHVLSK RSVDGGLMVK GPRHKPGAVQ ETTFELGGDI
HSGTALPASR STTRLDSDRV SSASSTAERG MVKPMIRLDQ EQDYRRRESR TQDAAGPELM
LPASIEFRES SEDSFLSAII NYTNSSTVHF KLSPTYVLYM ACRYVLSSQH RPDISPTERT
HKAIAVVNKM VSMMEGVIQE VDQVDQKQKN IAGALAFWMA NASELLNFIK QDRDLSRITL
DAQDVLAHLV QMAFKYLVHC LQSELNNYMP AFLDDPEENS LQRPKIDDVL HTLTGAMSLL
RRCRVNAALT IQLFSQLFHF INMWLFNRLV TDPDSGLCSH YWGAIIRQQL GHIEAWAEKQ
GLELAADCHL SRIVQATTLL TMDKYVPDDI PNINSTCFKL NSLQLQALLQ NYHCAPDEPF
IPTDLIENVV AVAENTADEL ARSDGRDVQL EEDPDLQLPF LLPEDGYSCD VVRNIPNGLQ
EFLDPLCQRG FCRLVPHTRS PGTWTIYFEG ADYESHLMRE NTELTQPLRK EPEVITVTLK
KQNGMGLSIV AAKGAGQDKL GIYVKSVVKG GAADVDGRLA AGDQLLSVDG RSLVGLSQER
AAELMTRTSS VVTLEVAKQG AIYHGLATLL NQPSPMMQRI SDRRGSGKPR PKSEGFELYN
NSAQNGSPES PQMPWTEYSE PKKLPGDDRL MKNRADHRSS PNVANQPPSP GGKSPYTSGT
AAKITSVSTG NLCTEEQTPP PRPEAYPIPT QTYTREYFTF PASKSQDRMA PVQNQWPNYE
EKPHMHTESD HASIAIQRVT RSQEELREEK VYQLERHRVE SGMDRKCDSD MWINQSSSVE
SSTSSQEHLN HSSKSVTPAS TLTKSGPGRW KTPAAVLPTP VAVSQPIRTD LPPPPPPPPA
HYTSDFDGIS MDLPLPPPPA NQAAPQSAQV AAAERKKREE HQRWYEKEKA RLEEERERKR
REQERKLGQM RTQSLNPASF SPLATQAKPE KPSTLQRPQE TVIRELQPQQ QPRTIERRDL
QYITISKEEL SSGDSLSPDP WKRDAREKLE KQQQMHIVDM LSKEIHELQN KGDRTAEESD
RLRKLMLEWQ FQKRLQESKQ KDEDDDEEED DDVDTMLIMQ RLEAERRARL QDEERRRQQQ
LEEMRKREVE DRVRQEEDGR HQEEERVKRD AEEKRRQEEG YYSRLEAERR RQHEEAARRL
LEPEEPGLSR PPLPQDYEPP SQSSAPSAPP PPPQRNASYL KTQVLSPDSL FTAKFVAYDD
DDEEENYVPA GPNSYSGSAG TTAGTYDAPR DTREKLSRSQ DADLPGSSGA PENLTFRERQ
RLFSQGQDVS DKVKASRKLT ELENELNTK
