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   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.
DR   Genevisible; Q80TR4; MM.
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
//