ID SLIT1_HUMAN Reviewed; 1534 AA. AC O75093; Q5T0V1; Q8WWZ2; Q9UIL7; DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 4. DT 13-FEB-2019, entry version 178. DE RecName: Full=Slit homolog 1 protein; DE Short=Slit-1; DE AltName: Full=Multiple epidermal growth factor-like domains protein 4; DE Short=Multiple EGF-like domains protein 4; DE Flags: Precursor; GN Name=SLIT1; Synonyms=KIAA0813, MEGF4, SLIL1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=9813312; DOI=10.1016/S0169-328X(98)00224-1; RA Itoh A., Miyabayashi T., Ohno M., Sakano S.; RT "Cloning and expressions of three mammalian homologues of Drosophila RT slit suggest possible roles for Slit in the formation and maintenance RT of the nervous system."; RL Brain Res. Mol. Brain Res. 62:175-186(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9693030; DOI=10.1006/geno.1998.5341; RA Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.; RT "Identification of high-molecular-weight proteins with multiple EGF- RT like motifs by motif-trap screening."; RL Genomics 51:27-34(1998). RN [3] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [4] RP SEQUENCE REVISION. RA Nakayama M., Nakajima D., Ohara O.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-1534 (ISOFORM 2). RX PubMed=12141424; RA Little M., Rumballe B., Georgas K., Yamada T., Teasdale R.D.; RT "Conserved modularity and potential for alternate splicing in mouse RT and human Slit genes."; RL Int. J. Dev. Biol. 46:385-391(2002). RN [9] RP REVIEW. RX PubMed=12200164; DOI=10.1016/S0959-437X(02)00343-X; RA Wong K., Park H.T., Wu J.Y., Rao Y.; RT "Slit proteins: molecular guidance cues for cells ranging from neurons RT to leukocytes."; RL Curr. Opin. Genet. Dev. 12:583-591(2002). CC -!- FUNCTION: Thought to act as molecular guidance cue in cellular CC migration, and function appears to be mediated by interaction with CC roundabout homolog receptors. During neural development involved CC in axonal navigation at the ventral midline of the neural tube and CC projection of axons to different regions (By similarity). SLIT1 CC and SLIT2 together seem to be essential for midline guidance in CC the forebrain by acting as repulsive signal preventing CC inappropriate midline crossing by axons projecting from the CC olfactory bulb. {ECO:0000250}. CC -!- SUBUNIT: Interacts with ROBO1 and GREM1. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O75093-1; Sequence=Displayed; CC Name=2; Synonyms=B; CC IsoId=O75093-2; Sequence=VSP_009706, VSP_009707, VSP_009708; CC -!- TISSUE SPECIFICITY: Predominantly expressed in adult forebrain. CC Expressed in fetal brain, lung and kidney. CC {ECO:0000269|PubMed:9813312}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA32465.3; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AB017167; BAA35184.1; -; mRNA. DR EMBL; AB011537; BAA32465.3; ALT_INIT; mRNA. DR EMBL; AL442123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL512424; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW49958.1; -; Genomic_DNA. DR EMBL; BC146851; AAI46852.1; -; mRNA. DR EMBL; AY029183; AAK31796.1; -; mRNA. DR CCDS; CCDS7453.1; -. [O75093-1] DR RefSeq; NP_003052.2; NM_003061.2. [O75093-1] DR UniGene; Hs.632082; -. DR ProteinModelPortal; O75093; -. DR BioGrid; 112472; 2. DR IntAct; O75093; 16. DR STRING; 9606.ENSP00000266058; -. DR CarbonylDB; O75093; -. DR iPTMnet; O75093; -. DR PhosphoSitePlus; O75093; -. DR BioMuta; SLIT1; -. DR EPD; O75093; -. DR jPOST; O75093; -. DR PaxDb; O75093; -. DR PeptideAtlas; O75093; -. DR PRIDE; O75093; -. DR ProteomicsDB; 49753; -. DR ProteomicsDB; 49754; -. [O75093-2] DR Ensembl; ENST00000266058; ENSP00000266058; ENSG00000187122. [O75093-1] DR GeneID; 6585; -. DR KEGG; hsa:6585; -. DR UCSC; uc001kmw.3; human. [O75093-1] DR CTD; 6585; -. DR DisGeNET; 6585; -. DR EuPathDB; HostDB:ENSG00000187122.16; -. DR GeneCards; SLIT1; -. DR H-InvDB; HIX0079168; -. DR H-InvDB; HIX0170440; -. DR HGNC; HGNC:11085; SLIT1. DR HPA; HPA006879; -. DR MIM; 603742; gene. DR neXtProt; NX_O75093; -. DR OpenTargets; ENSG00000187122; -. DR PharmGKB; PA35938; -. DR eggNOG; KOG4237; Eukaryota. DR eggNOG; COG4886; LUCA. DR GeneTree; ENSGT00940000157322; -. DR HOGENOM; HOG000116120; -. DR HOVERGEN; HBG057959; -. DR InParanoid; O75093; -. DR KO; K06838; -. DR OrthoDB; 28488at2759; -. DR PhylomeDB; O75093; -. DR TreeFam; TF332887; -. DR Reactome; R-HSA-373752; Netrin-1 signaling. DR Reactome; R-HSA-376176; Signaling by ROBO receptors. DR Reactome; R-HSA-428542; Regulation of commissural axon pathfinding by SLIT and ROBO. DR Reactome; R-HSA-8985801; Regulation of cortical dendrite branching. DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs. DR SIGNOR; O75093; -. DR ChiTaRS; SLIT1; human. DR GeneWiki; SLIT1; -. DR GenomeRNAi; 6585; -. DR PRO; PR:O75093; -. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; ENSG00000187122; Expressed in 122 organ(s), highest expression level in Brodmann (1909) area 23. DR ExpressionAtlas; O75093; baseline and differential. DR Genevisible; O75093; HS. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0005615; C:extracellular space; NAS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB. DR GO; GO:0048495; F:Roundabout binding; IPI:UniProtKB. DR GO; GO:0048846; P:axon extension involved in axon guidance; IDA:UniProtKB. DR GO; GO:0007411; P:axon guidance; IDA:UniProtKB. DR GO; GO:0033563; P:dorsal/ventral axon guidance; IEA:Ensembl. DR GO; GO:0048853; P:forebrain morphogenesis; NAS:UniProtKB. DR GO; GO:0008045; P:motor neuron axon guidance; IMP:UniProtKB. DR GO; GO:0050919; P:negative chemotaxis; IDA:UniProtKB. DR GO; GO:0051964; P:negative regulation of synapse assembly; ISS:UniProtKB. DR GO; GO:0007097; P:nuclear migration; IEA:Ensembl. DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl. DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEA:Ensembl. DR Gene3D; 3.80.10.10; -; 5. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR000483; Cys-rich_flank_reg_C. DR InterPro; IPR006207; Cys_knot_C. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR013032; EGF-like_CS. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR003645; Fol_N. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR001791; Laminin_G. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp. DR InterPro; IPR032675; LRR_dom_sf. DR InterPro; IPR000372; LRRNT. DR Pfam; PF00008; EGF; 5. DR Pfam; PF12661; hEGF; 2. DR Pfam; PF02210; Laminin_G_2; 1. DR Pfam; PF13855; LRR_8; 6. DR Pfam; PF01463; LRRCT; 4. DR Pfam; PF01462; LRRNT; 4. DR SMART; SM00041; CT; 1. DR SMART; SM00181; EGF; 9. DR SMART; SM00179; EGF_CA; 7. DR SMART; SM00274; FOLN; 4. DR SMART; SM00282; LamG; 1. DR SMART; SM00369; LRR_TYP; 18. DR SMART; SM00082; LRRCT; 4. DR SMART; SM00013; LRRNT; 4. DR SUPFAM; SSF49899; SSF49899; 1. DR SUPFAM; SSF57184; SSF57184; 1. DR PROSITE; PS01185; CTCK_1; 1. DR PROSITE; PS01225; CTCK_2; 1. DR PROSITE; PS00022; EGF_1; 9. DR PROSITE; PS01186; EGF_2; 8. DR PROSITE; PS50026; EGF_3; 9. DR PROSITE; PS01187; EGF_CA; 2. DR PROSITE; PS50025; LAM_G_DOMAIN; 1. DR PROSITE; PS51450; LRR; 21. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Developmental protein; KW Differentiation; Disulfide bond; EGF-like domain; Glycoprotein; KW Leucine-rich repeat; Neurogenesis; Polymorphism; Reference proteome; KW Repeat; Secreted; Signal. FT SIGNAL 1 33 {ECO:0000255}. FT CHAIN 34 1534 Slit homolog 1 protein. FT /FTId=PRO_0000007722. FT DOMAIN 34 61 LRRNT. FT REPEAT 62 83 LRR 1. FT REPEAT 86 107 LRR 2. FT REPEAT 110 131 LRR 3. FT REPEAT 134 155 LRR 4. FT REPEAT 158 179 LRR 5. FT REPEAT 182 203 LRR 6. FT DOMAIN 215 265 LRRCT 1. FT DOMAIN 273 309 LRRNT 2. FT REPEAT 310 331 LRR 7. FT REPEAT 334 355 LRR 8. FT REPEAT 358 379 LRR 9. FT REPEAT 382 403 LRR 10. FT REPEAT 406 427 LRR 11. FT DOMAIN 439 489 LRRCT 2. FT DOMAIN 504 540 LRRNT 3. FT REPEAT 541 562 LRR 12. FT REPEAT 566 587 LRR 13. FT REPEAT 590 611 LRR 14. FT REPEAT 614 635 LRR 15. FT REPEAT 638 659 LRR 16. FT DOMAIN 671 721 LRRCT 3. FT DOMAIN 725 761 LRRNT 4. FT REPEAT 762 783 LRR 17. FT REPEAT 785 806 LRR 18. FT REPEAT 809 830 LRR 19. FT REPEAT 833 854 LRR 20. FT DOMAIN 866 916 LRRCT 4. FT DOMAIN 927 962 EGF-like 1. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 964 1003 EGF-like 2. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1005 1041 EGF-like 3. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1043 1081 EGF-like 4. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1083 1119 EGF-like 5. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1127 1163 EGF-like 6. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1166 1339 Laminin G-like. {ECO:0000255|PROSITE- FT ProRule:PRU00122}. FT DOMAIN 1340 1374 EGF-like 7. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1377 1413 EGF-like 8. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1418 1454 EGF-like 9. {ECO:0000255|PROSITE- FT ProRule:PRU00076}. FT DOMAIN 1459 1534 CTCK. {ECO:0000255|PROSITE- FT ProRule:PRU00039}. FT CARBOHYD 72 72 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 192 192 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 406 406 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 571 571 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 630 630 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 762 762 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 801 801 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 806 806 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1026 1026 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1079 1079 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1189 1189 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1259 1259 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 1306 1306 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 286 295 {ECO:0000250}. FT DISULFID 443 466 {ECO:0000250}. FT DISULFID 445 487 {ECO:0000250}. FT DISULFID 513 519 {ECO:0000250}. FT DISULFID 517 526 {ECO:0000250}. FT DISULFID 675 698 {ECO:0000250}. FT DISULFID 677 719 {ECO:0000250}. FT DISULFID 929 940 {ECO:0000250}. FT DISULFID 934 950 {ECO:0000250}. FT DISULFID 952 961 {ECO:0000250}. FT DISULFID 968 979 {ECO:0000250}. FT DISULFID 973 991 {ECO:0000250}. FT DISULFID 993 1002 {ECO:0000250}. FT DISULFID 1009 1020 {ECO:0000250}. FT DISULFID 1014 1029 {ECO:0000250}. FT DISULFID 1031 1040 {ECO:0000250}. FT DISULFID 1047 1060 {ECO:0000250}. FT DISULFID 1054 1069 {ECO:0000250}. FT DISULFID 1071 1080 {ECO:0000250}. FT DISULFID 1087 1098 {ECO:0000250}. FT DISULFID 1092 1107 {ECO:0000250}. FT DISULFID 1109 1118 {ECO:0000250}. FT DISULFID 1131 1142 {ECO:0000250}. FT DISULFID 1136 1151 {ECO:0000250}. FT DISULFID 1153 1162 {ECO:0000250}. FT DISULFID 1313 1339 {ECO:0000250}. FT DISULFID 1342 1352 {ECO:0000250}. FT DISULFID 1347 1362 {ECO:0000250}. FT DISULFID 1364 1373 {ECO:0000250}. FT DISULFID 1381 1391 {ECO:0000250}. FT DISULFID 1386 1401 {ECO:0000250}. FT DISULFID 1403 1412 {ECO:0000250}. FT DISULFID 1422 1432 {ECO:0000250}. FT DISULFID 1427 1442 {ECO:0000250}. FT DISULFID 1444 1453 {ECO:0000250}. FT DISULFID 1459 1498 {ECO:0000250}. FT DISULFID 1477 1512 {ECO:0000250}. FT DISULFID 1488 1528 {ECO:0000250}. FT DISULFID 1492 1530 {ECO:0000250}. FT VAR_SEQ 338 338 I -> IRPLSFCSPCR (in isoform 2). FT {ECO:0000303|PubMed:12141424}. FT /FTId=VSP_009706. FT VAR_SEQ 790 813 Missing (in isoform 2). FT {ECO:0000303|PubMed:12141424}. FT /FTId=VSP_009707. FT VAR_SEQ 830 1534 Missing (in isoform 2). FT {ECO:0000303|PubMed:12141424}. FT /FTId=VSP_009708. FT VARIANT 824 824 P -> L (in dbSNP:rs2817673). FT /FTId=VAR_049003. FT CONFLICT 99 99 A -> V (in Ref. 2; BAA32465). FT {ECO:0000305}. FT CONFLICT 163 163 Q -> R (in Ref. 1; BAA35184). FT {ECO:0000305}. FT CONFLICT 829 829 Q -> P (in Ref. 8; AAK31796). FT {ECO:0000305}. FT CONFLICT 966 966 D -> N (in Ref. 1; BAA35184). FT {ECO:0000305}. SQ SEQUENCE 1534 AA; 167926 MW; 47B11CE6704A3E1D CRC64; MALTPGWGSS AGPVRPELWL LLWAAAWRLG ASACPALCTC TGTTVDCHGT GLQAIPKNIP RNTERLELNG NNITRIHKND FAGLKQLRVL QLMENQIGAV ERGAFDDMKE LERLRLNRNQ LHMLPELLFQ NNQALSRLDL SENAIQAIPR KAFRGATDLK NLQLDKNQIS CIEEGAFRAL RGLEVLTLNN NNITTIPVSS FNHMPKLRTF RLHSNHLFCD CHLAWLSQWL RQRPTIGLFT QCSGPASLRG LNVAEVQKSE FSCSGQGEAG RVPTCTLSSG SCPAMCTCSN GIVDCRGKGL TAIPANLPET MTEIRLELNG IKSIPPGAFS PYRKLRRIDL SNNQIAEIAP DAFQGLRSLN SLVLYGNKIT DLPRGVFGGL YTLQLLLLNA NKINCIRPDA FQDLQNLSLL SLYDNKIQSL AKGTFTSLRA IQTLHLAQNP FICDCNLKWL ADFLRTNPIE TSGARCASPR RLANKRIGQI KSKKFRCSAK EQYFIPGTED YQLNSECNSD VVCPHKCRCE ANVVECSSLK LTKIPERIPQ STAELRLNNN EISILEATGM FKKLTHLKKI NLSNNKVSEI EDGAFEGAAS VSELHLTANQ LESIRSGMFR GLDGLRTLML RNNRISCIHN DSFTGLRNVR LLSLYDNQIT TVSPGAFDTL QSLSTLNLLA NPFNCNCQLA WLGGWLRKRK IVTGNPRCQN PDFLRQIPLQ DVAFPDFRCE EGQEEGGCLP RPQCPQECAC LDTVVRCSNK HLRALPKGIP KNVTELYLDG NQFTLVPGQL STFKYLQLVD LSNNKISSLS NSSFTNMSQL TTLILSYNAL QCIPPLAFQG LRSLRLLSLH GNDISTLQEG IFADVTSLSH LAIGANPLYC DCHLRWLSSW VKTGYKEPGI ARCAGPQDME GKLLLTTPAK KFECQGPPTL AVQAKCDLCL SSPCQNQGTC HNDPLEVYRC ACPSGYKGRD CEVSLDSCSS GPCENGGTCH AQEGEDAPFT CSCPTGFEGP TCGVNTDDCV DHACANGGVC VDGVGNYTCQ CPLQYEGKAC EQLVDLCSPD LNPCQHEAQC VGTPDGPRCE CMPGYAGDNC SENQDDCRDH RCQNGAQCMD EVNSYSCLCA EGYSGQLCEI PPHLPAPKSP CEGTECQNGA NCVDQGNRPV CQCLPGFGGP ECEKLLSVNF VDRDTYLQFT DLQNWPRANI TLQVSTAEDN GILLYNGDND HIAVELYQGH VRVSYDPGSY PSSAIYSAET INDGQFHTVE LVAFDQMVNL SIDGGSPMTM DNFGKHYTLN SEAPLYVGGM PVDVNSAAFR LWQILNGTGF HGCIRNLYIN NELQDFTKTQ MKPGVVPGCE PCRKLYCLHG ICQPNATPGP MCHCEAGWVG LHCDQPADGP CHGHKCVHGQ CVPLDALSYS CQCQDGYSGA LCNQAGALAE PCRGLQCLHG HCQASGTKGA HCVCDPGFSG ELCEQESECR GDPVRDFHQV QRGYAICQTT RPLSWVECRG SCPGQGCCQG LRLKRRKFTF ECSDGTSFAE EVEKPTKCGC ALCA //