GENTAUR Molecular Products.

 SLIT3_HUMAN             Reviewed;        1523 AA.
 O75094; A6H8U9; J3KNP3; O95804; Q9UFH5;
 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
 02-NOV-2010, sequence version 3.
 12-SEP-2018, entry version 168.
 RecName: Full=Slit homolog 3 protein;
          Short=Slit-3;
 AltName: Full=Multiple epidermal growth factor-like domains protein 5;
          Short=Multiple EGF-like domains protein 5;
 Flags: Precursor;
 Name=SLIT3; Synonyms=KIAA0814, MEGF5, SLIL2; ORFNames=UNQ691/PRO1336;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY,
 AND VARIANT ALA-371.
 PubMed=9813312; DOI=10.1016/S0169-328X(98)00224-1;
 Itoh A., Miyabayashi T., Ohno M., Sakano S.;
 "Cloning and expressions of three mammalian homologues of Drosophila
 slit suggest possible roles for Slit in the formation and maintenance
 of the nervous system.";
 Brain Res. Mol. Brain Res. 62:175-186(1998).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-371.
 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).
 [3]
 SEQUENCE REVISION.
 Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.;
 Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
 ALA-371 AND SER-618.
 PubMed=12975309; DOI=10.1101/gr.1293003;
 Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
 Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
 Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
 Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
 Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
 Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
 Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
 Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
 Wood W.I., Godowski P.J., Gray A.M.;
 "The secreted protein discovery initiative (SPDI), a large-scale
 effort to identify novel human secreted and transmembrane proteins: a
 bioinformatics assessment.";
 Genome Res. 13:2265-2270(2003).
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=15372022; DOI=10.1038/nature02919;
 Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
 Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
 She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
 Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
 Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
 Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
 Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
 Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
 Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
 Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
 Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
 Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
 Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
 Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
 "The DNA sequence and comparative analysis of human chromosome 5.";
 Nature 431:268-274(2004).
 [6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
 ALA-371.
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [7]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-657, AND VARIANT
 ALA-371.
 TISSUE=Testis;
 PubMed=17974005; DOI=10.1186/1471-2164-8-399;
 Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
 Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
 Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
 Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
 "The full-ORF clone resource of the German cDNA consortium.";
 BMC Genomics 8:399-399(2007).
 [8]
 NUCLEOTIDE SEQUENCE [MRNA] OF 574-1523 (ISOFORM 2).
 PubMed=10349621; DOI=10.1016/S0925-4773(98)00174-9;
 Holmes G.P., Negus K., Burridge L., Raman S., Algar E., Yamada T.,
 Little M.H.;
 "Distinct but overlapping expression patterns of two vertebrate slit
 homologs implies functional roles in CNS development and
 organogenesis.";
 Mech. Dev. 79:57-72(1998).
 -!- FUNCTION: May act as molecular guidance cue in cellular migration,
     and function may be mediated by interaction with roundabout
     homolog receptors.
 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=4;
     Name=1;
       IsoId=O75094-1; Sequence=Displayed;
     Name=2;
       IsoId=O75094-2; Sequence=VSP_009714;
     Name=3;
       IsoId=O75094-3; Sequence=VSP_009715;
     Name=4;
       IsoId=O75094-4; Sequence=VSP_054798;
       Note=No experimental confirmation available.;
 -!- TISSUE SPECIFICITY: Predominantly expressed in thyroid.
     {ECO:0000269|PubMed:9813312}.
 -!- SEQUENCE CAUTION:
     Sequence=BAA32466.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
     Sequence=CAB59249.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
 -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
     and Haematology;
     URL="http://atlasgeneticsoncology.org/Genes/SLIT3ID50515ch5q34.html";
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 EMBL; AB017169; BAA35186.1; -; mRNA.
 EMBL; AB011538; BAA32466.2; ALT_INIT; mRNA.
 EMBL; AY358884; AAQ89243.1; -; mRNA.
 EMBL; AC008409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AC008479; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AC011365; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AC011389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AC027311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AC094081; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AC112165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; BC146759; AAI46760.1; -; mRNA.
 EMBL; AL122074; CAB59249.1; ALT_SEQ; mRNA.
 EMBL; AF075240; AAD19336.1; -; mRNA.
 CCDS; CCDS4369.1; -. [O75094-1]
 CCDS; CCDS64311.1; -. [O75094-4]
 PIR; T34555; T34555.
 RefSeq; NP_001258875.1; NM_001271946.1.
 RefSeq; NP_003053.1; NM_003062.3.
 UniGene; Hs.552087; -.
 ProteinModelPortal; O75094; -.
 BioGrid; 112473; 2.
 IntAct; O75094; 4.
 STRING; 9606.ENSP00000430333; -.
 iPTMnet; O75094; -.
 PhosphoSitePlus; O75094; -.
 MaxQB; O75094; -.
 PaxDb; O75094; -.
 PeptideAtlas; O75094; -.
 PRIDE; O75094; -.
 ProteomicsDB; 49755; -.
 ProteomicsDB; 49756; -. [O75094-2]
 ProteomicsDB; 49757; -. [O75094-3]
 Ensembl; ENST00000332966; ENSP00000332164; ENSG00000184347. [O75094-4]
 Ensembl; ENST00000519560; ENSP00000430333; ENSG00000184347. [O75094-1]
 GeneID; 6586; -.
 KEGG; hsa:6586; -.
 UCSC; uc003mab.5; human. [O75094-1]
 CTD; 6586; -.
 DisGeNET; 6586; -.
 EuPathDB; HostDB:ENSG00000184347.14; -.
 GeneCards; SLIT3; -.
 H-InvDB; HIX0005394; -.
 HGNC; HGNC:11087; SLIT3.
 HPA; HPA051630; -.
 MIM; 603745; gene.
 neXtProt; NX_O75094; -.
 OpenTargets; ENSG00000184347; -.
 PharmGKB; PA35940; -.
 eggNOG; KOG4237; Eukaryota.
 eggNOG; COG4886; LUCA.
 GeneTree; ENSGT00910000144018; -.
 HOGENOM; HOG000116120; -.
 HOVERGEN; HBG057959; -.
 InParanoid; O75094; -.
 KO; K06850; -.
 OMA; CPGPHSE; -.
 OrthoDB; EOG091G0MHP; -.
 PhylomeDB; O75094; -.
 TreeFam; TF332887; -.
 Reactome; R-HSA-373752; Netrin-1 signaling.
 Reactome; R-HSA-376176; Signaling by ROBO receptors.
 Reactome; R-HSA-428542; Regulation of commissural axon pathfinding by SLIT and ROBO.
 ChiTaRS; SLIT3; human.
 GeneWiki; SLIT3; -.
 GenomeRNAi; 6586; -.
 PRO; PR:O75094; -.
 Proteomes; UP000005640; Chromosome 5.
 Bgee; ENSG00000184347; Expressed in 221 organ(s), highest expression level in popliteal artery.
 CleanEx; HS_SLIT3; -.
 ExpressionAtlas; O75094; baseline and differential.
 Genevisible; O75094; HS.
 GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO; GO:0005739; C:mitochondrion; NAS:UniProtKB.
 GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
 GO; GO:0048495; F:Roundabout binding; IPI:UniProtKB.
 GO; GO:0003180; P:aortic valve morphogenesis; ISS:BHF-UCL.
 GO; GO:0061364; P:apoptotic process involved in luteolysis; IEP:UniProtKB.
 GO; GO:0003181; P:atrioventricular valve morphogenesis; ISS:BHF-UCL.
 GO; GO:0048846; P:axon extension involved in axon guidance; IDA:UniProtKB.
 GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
 GO; GO:0032870; P:cellular response to hormone stimulus; IEP:UniProtKB.
 GO; GO:0050919; P:negative chemotaxis; IDA:UniProtKB.
 GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
 GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
 GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; IMP:BHF-UCL.
 GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
 GO; GO:0051414; P:response to cortisol; IEP:UniProtKB.
 GO; GO:0035385; P:Roundabout signaling pathway; IMP:BHF-UCL.
 GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL.
 Gene3D; 3.80.10.10; -; 5.
 InterPro; IPR013320; ConA-like_dom_sf.
 InterPro; IPR000483; Cys-rich_flank_reg_C.
 InterPro; IPR006207; Cys_knot_C.
 InterPro; IPR001881; EGF-like_Ca-bd_dom.
 InterPro; IPR013032; EGF-like_CS.
 InterPro; IPR000742; EGF-like_dom.
 InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
 InterPro; IPR018097; EGF_Ca-bd_CS.
 InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
 InterPro; IPR001791; Laminin_G.
 InterPro; IPR001611; Leu-rich_rpt.
 InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
 InterPro; IPR032675; LRR_dom_sf.
 InterPro; IPR000372; LRRNT.
 Pfam; PF00008; EGF; 6.
 Pfam; PF02210; Laminin_G_2; 1.
 Pfam; PF13855; LRR_8; 5.
 Pfam; PF01463; LRRCT; 4.
 Pfam; PF01462; LRRNT; 3.
 SMART; SM00041; CT; 1.
 SMART; SM00181; EGF; 9.
 SMART; SM00179; EGF_CA; 9.
 SMART; SM00282; LamG; 1.
 SMART; SM00369; LRR_TYP; 18.
 SMART; SM00082; LRRCT; 4.
 SMART; SM00013; LRRNT; 4.
 SUPFAM; SSF49899; SSF49899; 1.
 SUPFAM; SSF57184; SSF57184; 1.
 PROSITE; PS01185; CTCK_1; 1.
 PROSITE; PS01225; CTCK_2; 1.
 PROSITE; PS00022; EGF_1; 9.
 PROSITE; PS01186; EGF_2; 7.
 PROSITE; PS50026; EGF_3; 9.
 PROSITE; PS01187; EGF_CA; 2.
 PROSITE; PS50025; LAM_G_DOMAIN; 1.
 PROSITE; PS51450; LRR; 20.
 2: Evidence at transcript level;
 Alternative splicing; Complete proteome; Developmental protein;
 Differentiation; Disulfide bond; EGF-like domain; Glycoprotein;
 Leucine-rich repeat; Neurogenesis; Polymorphism; Reference proteome;
 Repeat; Secreted; Signal.
 SIGNAL        1     33       {ECO:0000255}.
 CHAIN        34   1523       Slit homolog 3 protein.
                              /FTId=PRO_0000007732.
 DOMAIN       34     61       LRRNT.
 REPEAT       62     83       LRR 1.
 REPEAT       86    107       LRR 2.
 REPEAT      110    131       LRR 3.
 REPEAT      134    155       LRR 4.
 REPEAT      158    179       LRR 5.
 REPEAT      182    203       LRR 6.
 DOMAIN      215    265       LRRCT 1.
 DOMAIN      271    307       LRRNT 2.
 REPEAT      308    329       LRR 7.
 REPEAT      332    353       LRR 8.
 REPEAT      356    377       LRR 9.
 REPEAT      380    401       LRR 10.
 REPEAT      404    425       LRR 11.
 DOMAIN      437    487       LRRCT 2.
 DOMAIN      496    532       LRRNT 3.
 REPEAT      533    554       LRR 12.
 REPEAT      558    579       LRR 13.
 REPEAT      582    603       LRR 14.
 REPEAT      606    627       LRR 15.
 REPEAT      630    651       LRR 16.
 DOMAIN      663    713       LRRCT 3.
 DOMAIN      716    752       LRRNT 4.
 REPEAT      753    775       LRR 17.
 REPEAT      776    797       LRR 18.
 REPEAT      800    821       LRR 19.
 REPEAT      824    845       LRR 20.
 DOMAIN      857    907       LRRCT 4.
 DOMAIN      918    953       EGF-like 1. {ECO:0000255|PROSITE-
                              ProRule:PRU00076}.
 DOMAIN      955    994       EGF-like 2. {ECO:0000255|PROSITE-
                              ProRule:PRU00076}.
 DOMAIN      996   1032       EGF-like 3. {ECO:0000255|PROSITE-
                              ProRule:PRU00076}.
 DOMAIN     1034   1072       EGF-like 4. {ECO:0000255|PROSITE-
                              ProRule:PRU00076}.
 DOMAIN     1074   1110       EGF-like 5. {ECO:0000255|PROSITE-
                              ProRule:PRU00076}.
 DOMAIN     1119   1155       EGF-like 6. {ECO:0000255|PROSITE-
                              ProRule:PRU00076}.
 DOMAIN     1158   1332       Laminin G-like. {ECO:0000255|PROSITE-
                              ProRule:PRU00122}.
 DOMAIN     1340   1365       EGF-like 7. {ECO:0000255|PROSITE-
                              ProRule:PRU00076}.
 DOMAIN     1368   1403       EGF-like 8. {ECO:0000255|PROSITE-
                              ProRule:PRU00076}.
 DOMAIN     1408   1444       EGF-like 9. {ECO:0000255|PROSITE-
                              ProRule:PRU00076}.
 DOMAIN     1449   1523       CTCK. {ECO:0000255|PROSITE-
                              ProRule:PRU00039}.
 CARBOHYD     72     72       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    192    192       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    563    563       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    622    622       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    784    784       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    792    792       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    797    797       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD    928    928       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1008   1008       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1025   1025       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1181   1181       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1247   1247       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 CARBOHYD   1406   1406       N-linked (GlcNAc...) asparagine.
                              {ECO:0000255}.
 DISULFID    284    293       {ECO:0000250}.
 DISULFID    441    464       {ECO:0000250}.
 DISULFID    443    485       {ECO:0000250}.
 DISULFID    505    511       {ECO:0000250}.
 DISULFID    509    518       {ECO:0000250}.
 DISULFID    667    690       {ECO:0000250}.
 DISULFID    669    711       {ECO:0000250}.
 DISULFID    920    931       {ECO:0000250}.
 DISULFID    925    941       {ECO:0000250}.
 DISULFID    943    952       {ECO:0000250}.
 DISULFID    959    970       {ECO:0000250}.
 DISULFID    964    982       {ECO:0000250}.
 DISULFID    984    993       {ECO:0000250}.
 DISULFID   1000   1011       {ECO:0000250}.
 DISULFID   1005   1020       {ECO:0000250}.
 DISULFID   1022   1031       {ECO:0000250}.
 DISULFID   1038   1051       {ECO:0000250}.
 DISULFID   1045   1060       {ECO:0000250}.
 DISULFID   1062   1071       {ECO:0000250}.
 DISULFID   1078   1089       {ECO:0000250}.
 DISULFID   1083   1098       {ECO:0000250}.
 DISULFID   1100   1109       {ECO:0000250}.
 DISULFID   1123   1134       {ECO:0000250}.
 DISULFID   1128   1143       {ECO:0000250}.
 DISULFID   1145   1154       {ECO:0000250}.
 DISULFID   1305   1332       {ECO:0000250}.
 DISULFID   1355   1364       {ECO:0000250}.
 DISULFID   1372   1382       {ECO:0000250}.
 DISULFID   1377   1391       {ECO:0000250}.
 DISULFID   1393   1402       {ECO:0000250}.
 DISULFID   1412   1422       {ECO:0000250}.
 DISULFID   1417   1432       {ECO:0000250}.
 DISULFID   1434   1443       {ECO:0000250}.
 DISULFID   1449   1487       {ECO:0000250}.
 DISULFID   1467   1501       {ECO:0000250}.
 DISULFID   1478   1517       {ECO:0000250}.
 DISULFID   1482   1519       {ECO:0000250}.
 VAR_SEQ     906    906       K -> KVLWFCCP (in isoform 4).
                              {ECO:0000305}.
                              /FTId=VSP_054798.
 VAR_SEQ    1117   1216       Missing (in isoform 2).
                              {ECO:0000303|PubMed:10349621,
                              ECO:0000303|PubMed:9813312}.
                              /FTId=VSP_009714.
 VAR_SEQ    1446   1523       ENPCLGQVVREVIRRQKGYASCATASKVPIMECRGGCGPQC
                              CQPTRSKRRKYVFQCTDGSSFVEEVERHLECGCLACS ->
                              VFRAQVFQSSLPGNCSWSCWPPRPPMP (in isoform
                              3). {ECO:0000303|PubMed:9813312}.
                              /FTId=VSP_009715.
 VARIANT     371    371       V -> A (in dbSNP:rs891921).
                              {ECO:0000269|PubMed:12975309,
                              ECO:0000269|PubMed:15489334,
                              ECO:0000269|PubMed:17974005,
                              ECO:0000269|PubMed:9693030,
                              ECO:0000269|PubMed:9813312}.
                              /FTId=VAR_049004.
 VARIANT     395    395       R -> Q (in dbSNP:rs2288792).
                              /FTId=VAR_021905.
 VARIANT     618    618       G -> S (in dbSNP:rs10036727).
                              {ECO:0000269|PubMed:12975309}.
                              /FTId=VAR_024265.
 VARIANT     810    810       R -> Q (in dbSNP:rs36052924).
                              /FTId=VAR_049005.
 VARIANT     994    994       E -> G (in dbSNP:rs2305993).
                              /FTId=VAR_020168.
 VARIANT    1064   1064       P -> A (in dbSNP:rs10072243).
                              /FTId=VAR_049006.
 SEQUENCE   1523 AA;  167713 MW;  CEB00887F6908554 CRC64;
 MAPGWAGVGA AVRARLALAL ALASVLSGPP AVACPTKCTC SAASVDCHGL GLRAVPRGIP
 RNAERLDLDR NNITRITKMD FAGLKNLRVL HLEDNQVSVI ERGAFQDLKQ LERLRLNKNK
 LQVLPELLFQ STPKLTRLDL SENQIQGIPR KAFRGITDVK NLQLDNNHIS CIEDGAFRAL
 RDLEILTLNN NNISRILVTS FNHMPKIRTL RLHSNHLYCD CHLAWLSDWL RQRRTVGQFT
 LCMAPVHLRG FNVADVQKKE YVCPAPHSEP PSCNANSISC PSPCTCSNNI VDCRGKGLME
 IPANLPEGIV EIRLEQNSIK AIPAGAFTQY KKLKRIDISK NQISDIAPDA FQGLKSLTSL
 VLYGNKITEI VKGLFDGLVS LQLLLLNANK INCLRVNTFQ DLQNLNLLSL YDNKLQTISK
 GLFAPLQSIQ TLHLAQNPFV CDCHLKWLAD YLQDNPIETS GARCSSPRRL ANKRISQIKS
 KKFRCSGSED YRSRFSSECF MDLVCPEKCR CEGTIVDCSN QKLVRIPSHL PEYVTDLRLN
 DNEVSVLEAT GIFKKLPNLR KINLSNNKIK EVREGAFDGA ASVQELMLTG NQLETVHGRV
 FRGLSGLKTL MLRSNLIGCV SNDTFAGLSS VRLLSLYDNR ITTITPGAFT TLVSLSTINL
 LSNPFNCNCH LAWLGKWLRK RRIVSGNPRC QKPFFLKEIP IQDVAIQDFT CDGNEESSCQ
 LSPRCPEQCT CMETVVRCSN KGLRALPRGM PKDVTELYLE GNHLTAVPRE LSALRHLTLI
 DLSNNSISML TNYTFSNMSH LSTLILSYNR LRCIPVHAFN GLRSLRVLTL HGNDISSVPE
 GSFNDLTSLS HLALGTNPLH CDCSLRWLSE WVKAGYKEPG IARCSSPEPM ADRLLLTTPT
 HRFQCKGPVD INIVAKCNAC LSSPCKNNGT CTQDPVELYR CACPYSYKGK DCTVPINTCI
 QNPCQHGGTC HLSDSHKDGF SCSCPLGFEG QRCEINPDDC EDNDCENNAT CVDGINNYVC
 ICPPNYTGEL CDEVIDHCVP ELNLCQHEAK CIPLDKGFSC ECVPGYSGKL CETDNDDCVA
 HKCRHGAQCV DTINGYTCTC PQGFSGPFCE HPPPMVLLQT SPCDQYECQN GAQCIVVQQE
 PTCRCPPGFA GPRCEKLITV NFVGKDSYVE LASAKVRPQA NISLQVATDK DNGILLYKGD
 NDPLALELYQ GHVRLVYDSL SSPPTTVYSV ETVNDGQFHS VELVTLNQTL NLVVDKGTPK
 SLGKLQKQPA VGINSPLYLG GIPTSTGLSA LRQGTDRPLG GFHGCIHEVR INNELQDFKA
 LPPQSLGVSP GCKSCTVCKH GLCRSVEKDS VVCECRPGWT GPLCDQEARD PCLGHRCHHG
 KCVATGTSYM CKCAEGYGGD LCDNKNDSAN ACSAFKCHHG QCHISDQGEP YCLCQPGFSG
 EHCQQENPCL GQVVREVIRR QKGYASCATA SKVPIMECRG GCGPQCCQPT RSKRRKYVFQ
 CTDGSSFVEE VERHLECGCL ACS

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