ID SLIT1_MOUSE Reviewed; 1531 AA.
AC Q80TR4; Q9WVB5;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 27-MAR-2024, entry version 184.
DE RecName: Full=Slit homolog 1 protein;
DE Short=Slit-1;
DE Flags: Precursor;
GN Name=Slit1; Synonyms=Kiaa0813;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ROBO1, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=ICR X Swiss Webster;
RX PubMed=10433822; DOI=10.1006/dbio.1999.9371;
RA Yuan W., Zhou L., Chen J.H., Wu J.Y., Rao Y., Ornitz D.M.;
RT "The mouse SLIT family: secreted ligands for ROBO expressed in patterns
RT that suggest a role in morphogenesis and axon guidance.";
RL Dev. Biol. 212:290-306(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12097499; DOI=10.1523/jneurosci.22-13-05473.2002;
RA Nguyen-Ba-Charvet K.T., Plump A.S., Tessier-Lavigne M., Chedotal A.;
RT "Slit1 and slit2 proteins control the development of the lateral olfactory
RT tract.";
RL J. Neurosci. 22:5473-5480(2002).
RN [5]
RP FUNCTION.
RX PubMed=11804571; DOI=10.1016/s0896-6273(02)00561-5;
RA Bagri A., Marin O., Plump A.S., Mak J., Pleasure S.J., Rubenstein J.L.,
RA Tessier-Lavigne M.;
RT "Slit proteins prevent midline crossing and determine the dorsoventral
RT position of major axonal pathways in the mammalian forebrain.";
RL Neuron 33:233-248(2002).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=10864955; DOI=10.1523/jneurosci.20-13-04975.2000;
RA Erskine L., Williams S.E., Brose K., Kidd T., Rachel R.A., Goodman C.S.,
RA Tessier-Lavigne M., Mason C.A.;
RT "Retinal ganglion cell axon guidance in the mouse optic chiasm: expression
RT and function of robos and slits.";
RL J. Neurosci. 20:4975-4982(2000).
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 in
CC axonal navigation at the ventral midline of the neural tube and
CC projection of axons to different regions (By similarity). SLIT1 and
CC SLIT2 together seem to be essential for midline guidance in the
CC forebrain by acting as repulsive signal preventing inappropriate
CC midline crossing by axons projecting from the olfactory bulb.
CC {ECO:0000250, ECO:0000269|PubMed:11804571,
CC ECO:0000269|PubMed:12097499}.
CC -!- SUBUNIT: Interacts with GREM1 (By similarity) and ROBO1. {ECO:0000250,
CC ECO:0000269|PubMed:10433822}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: During retinal development, is expressed at 12.5
CC dpc in the dorsocentral region of the retina, and at 17.5 dpc is only
CC very weakly expressed. In the developing optic chiasm is expressed at
CC 12.5 dpc around the junction of the optic nerve and the brain, with
CC strongest expression dorsal to the site at which the optic stalk joins
CC the diencephalon, and also weakly in a subset of the CD44/SSEA neurons.
CC In the more dorsal region of the developing optic chiasm, is expressed
CC in some distance posterior to the axons. However, more ventrally, is
CC expressed in a region directly adjacent to the path taken by the RGC
CC axons. By 17.5 dpc is not longer be detected at the junction of the
CC brain and optic nerve and is only weakly expressed by the CD44/SSEA
CC neurons. Outside the developing brain detected at between 8.5 dpc and
CC 9.5 dpc in the primordiun of the branchial arches, between 9.5 dpc and
CC 10.5 dpc in the posterior dermamyotome. By 11.5 dpc the expression
CC pattern along somite boundaries was most prominent caudally. Weak
CC expression was also observed in the nasal pit at 11.5 dpc. From 13.5
CC dpc to 17.5 dpc expression was observed in the trigeminal ganglion, in
CC the olfactory epithelium, and in the neural layer of the retina in the
CC developing eye (with strongest expression in the inner nuclear layer).
CC {ECO:0000269|PubMed:10433822, ECO:0000269|PubMed:10864955}.
CC -!- DISRUPTION PHENOTYPE: Mice show significant axon guidance errors in a
CC variety of pathways, including corticofugal, callosal and
CC thalamocortical tracts. Mice double-deficient in SLIT1 and SLIT2 show
CC retinal axon guidance defects and a disorganized lateral olfactory
CC tract (LOT). {ECO:0000269|PubMed:12097499}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65658.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF144627; AAD44758.1; -; mRNA.
DR EMBL; AK122376; BAC65658.1; ALT_INIT; mRNA.
DR EMBL; BC057131; AAH57131.1; -; mRNA.
DR EMBL; BC062091; AAH62091.1; -; mRNA.
DR CCDS; CCDS29812.1; -.
DR RefSeq; NP_056563.2; NM_015748.3.
DR RefSeq; XP_011245502.1; XM_011247200.2.
DR AlphaFoldDB; Q80TR4; -.
DR BioGRID; 203327; 3.
DR IntAct; Q80TR4; 1.
DR MINT; Q80TR4; -.
DR STRING; 10090.ENSMUSP00000025993; -.
DR GlyCosmos; Q80TR4; 13 sites, No reported glycans.
DR GlyGen; Q80TR4; 13 sites.
DR iPTMnet; Q80TR4; -.
DR PhosphoSitePlus; Q80TR4; -.
DR MaxQB; Q80TR4; -.
DR PaxDb; 10090-ENSMUSP00000025993; -.
DR ProteomicsDB; 257198; -.
DR Antibodypedia; 1515; 221 antibodies from 27 providers.
DR DNASU; 20562; -.
DR Ensembl; ENSMUST00000025993.10; ENSMUSP00000025993.4; ENSMUSG00000025020.12.
DR GeneID; 20562; -.
DR KEGG; mmu:20562; -.
DR UCSC; uc008hmf.2; mouse.
DR AGR; MGI:1315203; -.
DR CTD; 6585; -.
DR MGI; MGI:1315203; Slit1.
DR VEuPathDB; HostDB:ENSMUSG00000025020; -.
DR eggNOG; KOG4237; Eukaryota.
DR GeneTree; ENSGT00940000157322; -.
DR InParanoid; Q80TR4; -.
DR OMA; ETKCQNN; -.
DR OrthoDB; 5475408at2759; -.
DR PhylomeDB; Q80TR4; -.
DR TreeFam; TF332887; -.
DR BioGRID-ORCS; 20562; 0 hits in 78 CRISPR screens.
DR ChiTaRS; Slit1; mouse.
DR PRO; PR:Q80TR4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q80TR4; Protein.
DR Bgee; ENSMUSG00000025020; Expressed in dentate gyrus of hippocampal formation granule cell and 89 other cell types or tissues.
DR ExpressionAtlas; Q80TR4; baseline and differential.
DR Genevisible; Q80TR4; MM.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0048495; F:Roundabout binding; IPI:MGI.
DR GO; GO:0005102; F:signaling receptor binding; TAS:MGI.
DR GO; GO:0048846; P:axon extension involved in axon guidance; ISO:MGI.
DR GO; GO:0007411; P:axon guidance; IDA:MGI.
DR GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR GO; GO:0033563; P:dorsal/ventral axon guidance; IGI:MGI.
DR GO; GO:0008045; P:motor neuron axon guidance; ISO:MGI.
DR GO; GO:0050919; P:negative chemotaxis; IMP:MGI.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; ISO:MGI.
DR GO; GO:0051964; P:negative regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; IGI:MGI.
DR GO; GO:0007097; P:nuclear migration; IDA:MGI.
DR GO; GO:0021772; P:olfactory bulb development; IGI:MGI.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:MGI.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IMP:MGI.
DR GO; GO:0022029; P:telencephalon cell migration; IGI:MGI.
DR CDD; cd00054; EGF_CA; 6.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.10.25.10; Laminin; 8.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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; 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 PANTHER; PTHR45836:SF23; LRRCT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45836; SLIT HOMOLOG; 1.
DR Pfam; PF00008; EGF; 4.
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; 3.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00364; LRR_BAC; 6.
DR SMART; SM00365; LRR_SD22; 8.
DR SMART; SM00369; LRR_TYP; 18.
DR SMART; SM00082; LRRCT; 4.
DR SMART; SM00013; LRRNT; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 5.
DR SUPFAM; SSF52058; L domain-like; 2.
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 1: Evidence at protein level;
KW Developmental protein; Differentiation; Disulfide bond; EGF-like domain;
KW Glycoprotein; Leucine-rich repeat; Neurogenesis; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1531
FT /note="Slit homolog 1 protein"
FT /id="PRO_0000007723"
FT DOMAIN 34..61
FT /note="LRRNT"
FT REPEAT 62..83
FT /note="LRR 1"
FT REPEAT 86..107
FT /note="LRR 2"
FT REPEAT 110..131
FT /note="LRR 3"
FT REPEAT 134..155
FT /note="LRR 4"
FT REPEAT 158..179
FT /note="LRR 5"
FT REPEAT 182..203
FT /note="LRR 6"
FT DOMAIN 215..265
FT /note="LRRCT 1"
FT DOMAIN 273..309
FT /note="LRRNT 23"
FT REPEAT 310..331
FT /note="LRR 7"
FT REPEAT 334..355
FT /note="LRR 8"
FT REPEAT 358..379
FT /note="LRR 9"
FT REPEAT 382..403
FT /note="LRR 10"
FT REPEAT 406..427
FT /note="LRR 11"
FT DOMAIN 439..489
FT /note="LRRCT 2"
FT DOMAIN 504..540
FT /note="LRRNT 3"
FT REPEAT 541..562
FT /note="LRR 12"
FT REPEAT 566..587
FT /note="LRR 13"
FT REPEAT 590..611
FT /note="LRR 14"
FT REPEAT 614..635
FT /note="LRR 15"
FT REPEAT 638..659
FT /note="LRR 16"
FT DOMAIN 671..721
FT /note="LRRCT 3"
FT DOMAIN 725..761
FT /note="LRRNT 4"
FT REPEAT 762..783
FT /note="LRR 17"
FT REPEAT 785..806
FT /note="LRR 18"
FT REPEAT 809..830
FT /note="LRR 19"
FT REPEAT 833..854
FT /note="LRR 20"
FT DOMAIN 866..916
FT /note="LRRCT 4"
FT DOMAIN 927..962
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 964..1003
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1005..1041
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1043..1081
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1083..1119
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1124..1160
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1163..1336
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1337..1371
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1374..1410
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1415..1451
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1456..1531
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 762
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 806
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1026
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1079
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 286..295
FT /evidence="ECO:0000250"
FT DISULFID 443..466
FT /evidence="ECO:0000250"
FT DISULFID 445..487
FT /evidence="ECO:0000250"
FT DISULFID 513..519
FT /evidence="ECO:0000250"
FT DISULFID 517..526
FT /evidence="ECO:0000250"
FT DISULFID 675..698
FT /evidence="ECO:0000250"
FT DISULFID 677..719
FT /evidence="ECO:0000250"
FT DISULFID 929..940
FT /evidence="ECO:0000250"
FT DISULFID 934..950
FT /evidence="ECO:0000250"
FT DISULFID 952..961
FT /evidence="ECO:0000250"
FT DISULFID 968..979
FT /evidence="ECO:0000250"
FT DISULFID 973..991
FT /evidence="ECO:0000250"
FT DISULFID 993..1002
FT /evidence="ECO:0000250"
FT DISULFID 1009..1020
FT /evidence="ECO:0000250"
FT DISULFID 1014..1029
FT /evidence="ECO:0000250"
FT DISULFID 1031..1040
FT /evidence="ECO:0000250"
FT DISULFID 1047..1060
FT /evidence="ECO:0000250"
FT DISULFID 1054..1069
FT /evidence="ECO:0000250"
FT DISULFID 1071..1080
FT /evidence="ECO:0000250"
FT DISULFID 1087..1098
FT /evidence="ECO:0000250"
FT DISULFID 1092..1107
FT /evidence="ECO:0000250"
FT DISULFID 1109..1118
FT /evidence="ECO:0000250"
FT DISULFID 1128..1139
FT /evidence="ECO:0000250"
FT DISULFID 1133..1148
FT /evidence="ECO:0000250"
FT DISULFID 1150..1159
FT /evidence="ECO:0000250"
FT DISULFID 1310..1336
FT /evidence="ECO:0000250"
FT DISULFID 1339..1349
FT /evidence="ECO:0000250"
FT DISULFID 1344..1359
FT /evidence="ECO:0000250"
FT DISULFID 1361..1370
FT /evidence="ECO:0000250"
FT DISULFID 1378..1388
FT /evidence="ECO:0000250"
FT DISULFID 1383..1398
FT /evidence="ECO:0000250"
FT DISULFID 1400..1409
FT /evidence="ECO:0000250"
FT DISULFID 1419..1429
FT /evidence="ECO:0000250"
FT DISULFID 1424..1439
FT /evidence="ECO:0000250"
FT DISULFID 1441..1450
FT /evidence="ECO:0000250"
FT DISULFID 1456..1495
FT /evidence="ECO:0000250"
FT DISULFID 1474..1509
FT /evidence="ECO:0000250"
FT DISULFID 1485..1525
FT /evidence="ECO:0000250"
FT DISULFID 1489..1527
FT /evidence="ECO:0000250"
FT CONFLICT 44
FT /note="Missing (in Ref. 3; AAH57131/AAH62091)"
FT /evidence="ECO:0000305"
FT CONFLICT 830
FT /note="G -> R (in Ref. 1; AAD44758)"
FT /evidence="ECO:0000305"
FT CONFLICT 1531
FT /note="A -> V (in Ref. 1; AAD44758 and 2; BAC65658)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1531 AA; 167420 MW; C0F1C5A4E3DF6108 CRC64;
MALTPQRGSS SGLSRPELWL LLWAAAWRLG ATACPALCTC TGTTVDCHGT GLQAIPKNIP
RNTERLELNG NNITRIHKND FAGLKQLRVL QLMENQIGAV ERGAFDDMKE LERLRLNRNQ
LQVLPELLFQ NNQALSRLDL SENFLQAVPR KAFRGATDLK NLQLDKNRIS CIEEGAFRAL
RGLEVLTLNN NNITTIPVSS FNHMPKLRTF RLHSNHLFCD CHLAWLSQWL RQRPTIGLFT
QCSGPASLRG LNVAEVQKGE FSCSGQGEAA GAPACTLSSG SCPAMCSCSS GIVDCRGKGL
TAIPANLPET MTEIRLELNG IKSIPPGAFS PYRKLRRIDL SNNQIAEIAP DAFQGLRSLN
SLVLYGNKIT DLPRGVFGGL YTLQLLLLNA NKINCIRPDA FQDLQNLSLL SLYDNKIQSL
AKGTFTSLRA IQTLHLAQNP FICDCNLKWL ADFLRTNPIE TTGARCASPR RLANKRIGQI
KSKKFRCSAK EQYFIPGTED YHLNSECTSD VACPHKCRCE ASVVECSSLK LSKIPERIPQ
STTELRLNNN EISILEATGL FKKLSHLKKI NLSNNKVSEI EDGTFEGAAS VSELHLTANQ
LESIRSGMFR GLDGLRTLML RNNRISCIHN DSFTGLRNVR LLSLYDNHIT TISPGAFDTL
QALSTLNLLA NPFNCNCHLS WLGDWLRKRK IVTGNPRCQN PDFLRQIPLQ DVAFPDFRCE
EGQEEVGCLP RPQCPQECAC LDTVVRCSNK HLQALPKGIP KNVTELYLDG NQFTLVPGQL
STFKYLQLVD LSNNKISSLS NSSFTNMSQL TTLILSYNAL QCIPPLAFQG LRSLRLLSLH
GNDVSTLQEG IFADVTSLSH LAIGANPLYC DCRLRWLSSW VKTGYKEPGI ARCAGPPEME
GKLLLTTPAK KFECQGPPSL AVQAKCDPCL SSPCQNQGTC HNDPLEVYRC TCPSGYKGRH
CEVSLDGCSS NPCGNGGTCH AQEGEDAGFT CSCPSGFEGP TCGVDTDDCV KHACVNGGVC
VDGVGNYTCQ CPLQYTGRAC EQLVDFCSPD MNPCQHEAQC VGTPDGPRCE CMLGYTGDNC
SENQDDCKDH KCQNGAQCVD EVNSYACLCV EGYSGQLCEI PPAPRSSCEG TECQNGANCV
DQGSRPVCQC LPGFGGPECE KLLSVNFVDR DTYLQFTDLQ NWPRANITLQ VSTAEDNGIL
LYNGDNDHIA VELYQGHVRV SYDPGSYPSS AIYSAETIND GQFHTVELVT FDQMVNLSID
GGSPMTMDNF GKHYTLNSEA PLYVGGMPVD VNSAAFRLWQ ILNGTSFHGC IRNLYINNEL
QDFTKTQMKP GVVPGCEPCR KLYCLHGICQ PNATPGPVCH CEAGWGGLHC DQPVDGPCHG
HKCVHGKCVP LDALAYSCQC QDGYSGALCN QVGAVAEPCG GLQCLHGHCQ ASATKGAHCV
CSPGFSGELC EQESECRGDP VRDFHRVQRG YAICQTTRPL SWVECRGACP GQGCCQGLRL
KRRKLTFECS DGTSFAEEVE KPTKCGCAQC A
//
