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Cadherin EGF LAG seven-pass G-type receptor 3 (Cadherin family member 11) (Epidermal growth factor-like protein 1) (EGF-like protein 1) (Flamingo homolog 1) (hFmi1) (Multiple epidermal growth factor-like domains protein 2) (Multiple EGF-like domains protein 2)

 CELR3_HUMAN             Reviewed;        3312 AA.
Q9NYQ7; O75092;
02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 2.
28-MAR-2018, entry version 170.
RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 3;
AltName: Full=Cadherin family member 11;
AltName: Full=Epidermal growth factor-like protein 1;
Short=EGF-like protein 1;
AltName: Full=Flamingo homolog 1;
Short=hFmi1;
AltName: Full=Multiple epidermal growth factor-like domains protein 2;
Short=Multiple EGF-like domains protein 2;
Flags: Precursor;
Name=CELSR3; Synonyms=CDHF11, EGFL1, FMI1, KIAA0812, MEGF2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10716726; DOI=10.1073/pnas.97.7.3124;
Wu Q., Maniatis T.;
"Large exons encoding multiple ectodomains are a characteristic
feature of protocadherin genes.";
Proc. Natl. Acad. Sci. U.S.A. 97:3124-3129(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1954-3312 (ISOFORM 2).
TISSUE=Brain;
PubMed=9693030; DOI=10.1006/geno.1998.5341;
Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
"Identification of high-molecular-weight proteins with multiple EGF-
like motifs by motif-trap screening.";
Genomics 51:27-34(1998).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
-!- FUNCTION: Receptor that may have an important role in cell/cell
signaling during nervous system formation.
-!- INTERACTION:
P16333:NCK1; NbExp=2; IntAct=EBI-308417, EBI-389883;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NYQ7-1; Sequence=Displayed;
Name=2;
IsoId=Q9NYQ7-2; Sequence=VSP_037125;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
LN-TM7 subfamily. {ECO:0000305}.
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EMBL; AF231023; AAF61929.1; -; mRNA.
EMBL; AC121252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB011536; BAA32464.1; -; mRNA.
CCDS; CCDS2775.1; -. [Q9NYQ7-1]
PIR; T00250; T00250.
RefSeq; NP_001398.2; NM_001407.2. [Q9NYQ7-1]
UniGene; Hs.631926; -.
ProteinModelPortal; Q9NYQ7; -.
SMR; Q9NYQ7; -.
BioGrid; 108271; 19.
IntAct; Q9NYQ7; 18.
STRING; 9606.ENSP00000164024; -.
iPTMnet; Q9NYQ7; -.
PhosphoSitePlus; Q9NYQ7; -.
BioMuta; CELSR3; -.
DMDM; 229462826; -.
EPD; Q9NYQ7; -.
MaxQB; Q9NYQ7; -.
PaxDb; Q9NYQ7; -.
PeptideAtlas; Q9NYQ7; -.
PRIDE; Q9NYQ7; -.
Ensembl; ENST00000164024; ENSP00000164024; ENSG00000008300. [Q9NYQ7-1]
GeneID; 1951; -.
KEGG; hsa:1951; -.
UCSC; uc003cul.4; human. [Q9NYQ7-1]
CTD; 1951; -.
DisGeNET; 1951; -.
EuPathDB; HostDB:ENSG00000008300.14; -.
GeneCards; CELSR3; -.
H-InvDB; HIX0200467; -.
HGNC; HGNC:3230; CELSR3.
HPA; HPA062866; -.
MIM; 604264; gene.
neXtProt; NX_Q9NYQ7; -.
OpenTargets; ENSG00000008300; -.
PharmGKB; PA26395; -.
eggNOG; KOG4289; Eukaryota.
eggNOG; ENOG410XTGH; LUCA.
GeneTree; ENSGT00760000118805; -.
HOGENOM; HOG000231346; -.
HOVERGEN; HBG050887; -.
InParanoid; Q9NYQ7; -.
KO; K04602; -.
OMA; ANRHPQF; -.
OrthoDB; EOG091G0039; -.
PhylomeDB; Q9NYQ7; -.
TreeFam; TF323983; -.
SignaLink; Q9NYQ7; -.
ChiTaRS; CELSR3; human.
GeneWiki; CELSR3; -.
GenomeRNAi; 1951; -.
PRO; PR:Q9NYQ7; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000008300; -.
CleanEx; HS_CELSR3; -.
Genevisible; Q9NYQ7; HS.
GO; GO:0016021; C:integral component of membrane; TAS:GDB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004930; F:G-protein coupled receptor activity; TAS:GDB.
GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl.
GO; GO:0060271; P:cilium assembly; IEA:Ensembl.
GO; GO:0036514; P:dopaminergic neuron axon guidance; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:GDB.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:1904938; P:planar cell polarity pathway involved in axon guidance; IEA:Ensembl.
GO; GO:0032880; P:regulation of protein localization; IEA:Ensembl.
GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0036515; P:serotonergic neuron axon guidance; IEA:Ensembl.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
Gene3D; 4.10.1240.10; -; 1.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR032471; GAIN_dom_N.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR036445; GPCR_2_extracell_dom_sf.
InterPro; IPR001879; GPCR_2_extracellular_dom.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR017983; GPCR_2_secretin-like_CS.
InterPro; IPR000203; GPS.
InterPro; IPR002049; Laminin_EGF.
InterPro; IPR001791; Laminin_G.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF00028; Cadherin; 8.
Pfam; PF00008; EGF; 2.
Pfam; PF16489; GAIN; 1.
Pfam; PF01825; GPS; 1.
Pfam; PF00053; Laminin_EGF; 1.
Pfam; PF02210; Laminin_G_2; 2.
PRINTS; PR00205; CADHERIN.
PRINTS; PR00249; GPCRSECRETIN.
SMART; SM00112; CA; 9.
SMART; SM00181; EGF; 6.
SMART; SM00179; EGF_CA; 5.
SMART; SM00180; EGF_Lam; 1.
SMART; SM00303; GPS; 1.
SMART; SM00008; HormR; 1.
SMART; SM00282; LamG; 2.
SUPFAM; SSF49313; SSF49313; 9.
SUPFAM; SSF49899; SSF49899; 2.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00232; CADHERIN_1; 7.
PROSITE; PS50268; CADHERIN_2; 8.
PROSITE; PS00022; EGF_1; 6.
PROSITE; PS01186; EGF_2; 4.
PROSITE; PS50026; EGF_3; 6.
PROSITE; PS01248; EGF_LAM_1; 1.
PROSITE; PS50027; EGF_LAM_2; 1.
PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PROSITE; PS50221; GPS; 1.
PROSITE; PS50025; LAM_G_DOMAIN; 2.
1: Evidence at protein level;
Alternative splicing; Calcium; Cell membrane; Complete proteome;
Developmental protein; Disulfide bond; EGF-like domain;
G-protein coupled receptor; Glycoprotein; Hydroxylation;
Laminin EGF-like domain; Membrane; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Repeat; Signal; Transducer;
Transmembrane; Transmembrane helix.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 3312 Cadherin EGF LAG seven-pass G-type
receptor 3.
/FTId=PRO_0000012918.
TOPO_DOM 33 2540 Extracellular. {ECO:0000255}.
TRANSMEM 2541 2561 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 2562 2572 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2573 2593 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 2594 2601 Extracellular. {ECO:0000255}.
TRANSMEM 2602 2622 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 2623 2643 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2644 2664 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 2665 2681 Extracellular. {ECO:0000255}.
TRANSMEM 2682 2702 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 2703 2725 Cytoplasmic. {ECO:0000255}.
TRANSMEM 2726 2746 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 2747 2753 Extracellular. {ECO:0000255}.
TRANSMEM 2754 2774 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 2775 3312 Cytoplasmic. {ECO:0000255}.
DOMAIN 326 433 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 434 545 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 546 651 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 652 756 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 757 858 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 859 961 Cadherin 6. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 962 1067 Cadherin 7. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1068 1169 Cadherin 8. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1170 1265 Cadherin 9. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1375 1433 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1435 1471 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1475 1514 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1515 1719 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1722 1758 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1764 1944 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1946 1982 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1983 2020 EGF-like 6; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2021 2053 EGF-like 7; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2055 2090 EGF-like 8; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2077 2124 Laminin EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00460}.
DOMAIN 2477 2529 GPS. {ECO:0000255|PROSITE-
ProRule:PRU00098}.
MOD_RES 1963 1963 (3R)-3-hydroxyaspartate. {ECO:0000255}.
MOD_RES 2126 2126 Phosphotyrosine.
{ECO:0000250|UniProtKB:O88278}.
MOD_RES 3051 3051 Phosphotyrosine.
{ECO:0000250|UniProtKB:O88278}.
MOD_RES 3097 3097 Phosphoserine.
{ECO:0000250|UniProtKB:O88278}.
CARBOHYD 632 632 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 847 847 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1182 1182 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1222 1222 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1317 1317 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1327 1327 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1649 1649 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1713 1713 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1770 1770 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2053 2053 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2177 2177 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2196 2196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2386 2386 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2474 2474 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2506 2506 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 1379 1390 {ECO:0000250}.
DISULFID 1384 1421 {ECO:0000250}.
DISULFID 1423 1432 {ECO:0000250}.
DISULFID 1439 1450 {ECO:0000250}.
DISULFID 1444 1459 {ECO:0000250}.
DISULFID 1461 1470 {ECO:0000250}.
DISULFID 1479 1490 {ECO:0000250}.
DISULFID 1484 1500 {ECO:0000250}.
DISULFID 1502 1513 {ECO:0000250}.
DISULFID 1693 1719 {ECO:0000250}.
DISULFID 1726 1737 {ECO:0000250}.
DISULFID 1731 1746 {ECO:0000250}.
DISULFID 1748 1757 {ECO:0000250}.
DISULFID 1915 1944 {ECO:0000250}.
DISULFID 1950 1961 {ECO:0000250}.
DISULFID 1955 1970 {ECO:0000250}.
DISULFID 1972 1981 {ECO:0000250}.
DISULFID 1985 1996 {ECO:0000250}.
DISULFID 1990 2008 {ECO:0000250}.
DISULFID 2010 2019 {ECO:0000250}.
DISULFID 2027 2040 {ECO:0000250}.
DISULFID 2042 2052 {ECO:0000250}.
DISULFID 2059 2074 {ECO:0000250}.
DISULFID 2061 2077 {ECO:0000250}.
DISULFID 2079 2089 {ECO:0000250}.
DISULFID 2098 2107 {ECO:0000250}.
DISULFID 2110 2122 {ECO:0000250}.
VAR_SEQ 2158 2158 G -> GLRGAG (in isoform 2).
{ECO:0000303|PubMed:9693030}.
/FTId=VSP_037125.
VARIANT 157 157 A -> P (in dbSNP:rs3733085).
/FTId=VAR_020022.
VARIANT 805 805 S -> T (in dbSNP:rs3821875).
/FTId=VAR_020023.
VARIANT 1758 1758 Q -> R (in dbSNP:rs12107252).
/FTId=VAR_055101.
CONFLICT 13 13 G -> E (in Ref. 1; AAF61929).
{ECO:0000305}.
SEQUENCE 3312 AA; 358185 MW; 9E6B37787A9F0348 CRC64;
MMARRPPWRG LGGRSTPILL LLLLSLFPLS QEELGGGGHQ GWDPGLAATT GPRAHIGGGA
LALCPESSGV REDGGPGLGV REPIFVGLRG RRQSARNSRG PPEQPNEELG IEHGVQPLGS
RERETGQGPG SVLYWRPEVS SCGRTGPLQR GSLSPGALSS GVPGSGNSSP LPSDFLIRHH
GPKPVSSQRN AGTGSRKRVG TARCCGELWA TGSKGQGERA TTSGAERTAP RRNCLPGASG
SGPELDSAPR TARTAPASGS APRESRTAPE PAPKRMRSRG LFRCRFLPQR PGPRPPGLPA
RPEARKVTSA NRARFRRAAN RHPQFPQYNY QTLVPENEAA GTAVLRVVAQ DPDAGEAGRL
VYSLAALMNS RSLELFSIDP QSGLIRTAAA LDRESMERHY LRVTAQDHGS PRLSATTMVA
VTVADRNDHS PVFEQAQYRE TLRENVEEGY PILQLRATDG DAPPNANLRY RFVGPPAARA
AAAAAFEIDP RSGLISTSGR VDREHMESYE LVVEASDQGQ EPGPRSATVR VHITVLDEND
NAPQFSEKRY VAQVREDVRP HTVVLRVTAT DRDKDANGLV HYNIISGNSR GHFAIDSLTG
EIQVVAPLDF EAEREYALRI RAQDAGRPPL SNNTGLASIQ VVDINDHIPI FVSTPFQVSV
LENAPLGHSV IHIQAVDADH GENARLEYSL TGVAPDTPFV INSATGWVSV SGPLDRESVE
HYFFGVEARD HGSPPLSASA SVTVTVLDVN DNRPEFTMKE YHLRLNEDAA VGTSVVSVTA
VDRDANSAIS YQITGGNTRN RFAISTQGGV GLVTLALPLD YKQERYFKLV LTASDRALHD
HCYVHINITD ANTHRPVFQS AHYSVSVNED RPMGSTIVVI SASDDDVGEN ARITYLLEDN
LPQFRIDADS GAITLQAPLD YEDQVTYTLA ITARDNGIPQ KADTTYVEVM VNDVNDNAPQ
FVASHYTGLV SEDAPPFTSV LQISATDRDA HANGRVQYTF QNGEDGDGDF TIEPTSGIVR
TVRRLDREAV SVYELTAYAV DRGVPPLRTP VSIQVMVQDV NDNAPVFPAE EFEVRVKENS
IVGSVVAQIT AVDPDEGPNA HIMYQIVEGN IPELFQMDIF SGELTALIDL DYEARQEYVI
VVQATSAPLV SRATVHVRLV DQNDNSPVLN NFQILFNNYV SNRSDTFPSG IIGRIPAYDP
DVSDHLFYSF ERGNELQLLV VNQTSGELRL SRKLDNNRPL VASMLVTVTD GLHSVTAQCV
LRVVIITEEL LANSLTVRLE NMWQERFLSP LLGRFLEGVA AVLATPAEDV FIFNIQNDTD
VGGTVLNVSF SALAPRGAGA GAAGPWFSSE ELQEQLYVRR AALAARSLLD VLPFDDNVCL
REPCENYMKC VSVLRFDSSA PFLASASTLF RPIQPIAGLR CRCPPGFTGD FCETELDLCY
SNPCRNGGAC ARREGGYTCV CRPRFTGEDC ELDTEAGRCV PGVCRNGGTC TDAPNGGFRC
QCPAGGAFEG PRCEVAARSF PPSSFVMFRG LRQRFHLTLS LSFATVQQSG LLFYNGRLNE
KHDFLALELV AGQVRLTYST GESNTVVSPT VPGGLSDGQW HTVHLRYYNK PRTDALGGAQ
GPSKDKVAVL SVDDCDVAVA LQFGAEIGNY SCAAAGVQTS SKKSLDLTGP LLLGGVPNLP
ENFPVSHKDF IGCMRDLHID GRRVDMAAFV ANNGTMAGCQ AKLHFCDSGP CKNSGFCSER
WGSFSCDCPV GFGGKDCQLT MAHPHHFRGN GTLSWNFGSD MAVSVPWYLG LAFRTRATQG
VLMQVQAGPH STLLCQLDRG LLSVTVTRGS GRASHLLLDQ VTVSDGRWHD LRLELQEEPG
GRRGHHVLMV SLDFSLFQDT MAVGSELQGL KVKQLHVGGL PPGSAEEAPQ GLVGCIQGVW
LGSTPSGSPA LLPPSHRVNA EPGCVVTNAC ASGPCPPHAD CRDLWQTFSC TCQPGYYGPG
CVDACLLNPC QNQGSCRHLP GAPHGYTCDC VGGYFGHHCE HRMDQQCPRG WWGSPTCGPC
NCDVHKGFDP NCNKTNGQCH CKEFHYRPRG SDSCLPCDCY PVGSTSRSCA PHSGQCPCRP
GALGRQCNSC DSPFAEVTAS GCRVLYDACP KSLRSGVWWP QTKFGVLATV PCPRGALGAA
VRLCDEAQGW LEPDLFNCTS PAFRELSLLL DGLELNKTAL DTMEAKKLAQ RLREVTGHTD
HYFSQDVRVT ARLLAHLLAF ESHQQGFGLT ATQDAHFNEN LLWAGSALLA PETGDLWAAL
GQRAPGGSPG SAGLVRHLEE YAATLARNME LTYLNPMGLV TPNIMLSIDR MEHPSSPRGA
RRYPRYHSNL FRGQDAWDPH THVLLPSQSP RPSPSEVLPT SSSIENSTTS SVVPPPAPPE
PEPGISIIIL LVYRTLGGLL PAQFQAERRG ARLPQNPVMN SPVVSVAVFH GRNFLRGILE
SPISLEFRLL QTANRSKAIC VQWDPPGLAE QHGVWTARDC ELVHRNGSHA RCRCSRTGTF
GVLMDASPRE RLEGDLELLA VFTHVVVAVS VAALVLTAAI LLSLRSLKSN VRGIHANVAA
ALGVAELLFL LGIHRTHNQL VCTAVAILLH YFFLSTFAWL FVQGLHLYRM QVEPRNVDRG
AMRFYHALGW GVPAVLLGLA VGLDPEGYGN PDFCWISVHE PLIWSFAGPV VLVIVMNGTM
FLLAARTSCS TGQREAKKTS ALTLRSSFLL LLLVSASWLF GLLAVNHSIL AFHYLHAGLC
GLQGLAVLLL FCVLNADARA AWMPACLGRK AAPEEARPAP GLGPGAYNNT ALFEESGLIR
ITLGASTVSS VSSARSGRTQ DQDSQRGRSY LRDNVLVRHG SAADHTDHSL QAHAGPTDLD
VAMFHRDAGA DSDSDSDLSL EEERSLSIPS SESEDNGRTR GRFQRPLCRA AQSERLLTHP
KDVDGNDLLS YWPALGECEA APCALQTWGS ERRLGLDTSK DAANNNQPDP ALTSGDETSL
GRAQRQRKGI LKNRLQYPLV PQTRGAPELS WCRAATLGHR AVPAASYGRI YAGGGTGSLS
QPASRYSSRE QLDLLLRRQL SRERLEEAPA PVLRPLSRPG SQECMDAAPG RLEPKDRGST
LPRRQPPRDY PGAMAGRFGS RDALDLGAPR EWLSTLPPPR RTRDLDPQPP PLPLSPQRQL
SRDPLLPSRP LDSLSRSSNS REQLDQVPSR HPSREALGPL PQLLRAREDS VSGPSHGPST
EQLDILSSIL ASFNSSALSS VQSSSTPLGP HTTATPSATA SVLGPSTPRS ATSHSISELS
PDSEVPRSEG HS


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