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 01-MAY-2013, entry version 126.
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.
CC -!- SUBUNIT: Interacts with ROBO1 and GREM1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Secreted (By similarity).
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 -!- SIMILARITY: Contains 1 CTCK (C-terminal cystine knot-like) domain.
CC -!- SIMILARITY: Contains 9 EGF-like domains.
CC -!- SIMILARITY: Contains 1 laminin G-like domain.
CC -!- SIMILARITY: Contains 20 LRR (leucine-rich) repeats.
CC -!- SIMILARITY: Contains 4 LRRCT domains.
CC -!- SIMILARITY: Contains 4 LRRNT domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32465.3; Type=Erroneous initiation;
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DR EMBL; AB017167; BAA35184.1; -; mRNA.
DR EMBL; AB011537; BAA32465.3; ALT_INIT; mRNA.
DR EMBL; AL442123; CAH70918.1; -; Genomic_DNA.
DR EMBL; AL512424; CAH70918.1; JOINED; Genomic_DNA.
DR EMBL; AL512424; CAI14258.1; -; Genomic_DNA.
DR EMBL; AL442123; CAI14258.1; JOINED; Genomic_DNA.
DR EMBL; CH471066; EAW49958.1; -; Genomic_DNA.
DR EMBL; BC146851; AAI46852.1; -; mRNA.
DR EMBL; AY029183; AAK31796.1; -; mRNA.
DR IPI; IPI00296434; -.
DR IPI; IPI00871419; -.
DR RefSeq; NP_003052.2; NM_003061.2.
DR UniGene; Hs.632082; -.
DR ProteinModelPortal; O75093; -.
DR IntAct; O75093; 1.
DR MINT; MINT-2797238; -.
DR STRING; 9606.ENSP00000266058; -.
DR PhosphoSite; O75093; -.
DR PaxDb; O75093; -.
DR PRIDE; O75093; -.
DR Ensembl; ENST00000266058; ENSP00000266058; ENSG00000187122.
DR GeneID; 6585; -.
DR KEGG; hsa:6585; -.
DR UCSC; uc001kmw.2; human.
DR CTD; 6585; -.
DR GeneCards; GC10M098747; -.
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 PharmGKB; PA35938; -.
DR eggNOG; COG4886; -.
DR HOGENOM; HOG000116120; -.
DR HOVERGEN; HBG057959; -.
DR InParanoid; O75093; -.
DR KO; K06838; -.
DR OrthoDB; EOG4VDPXM; -.
DR PhylomeDB; O75093; -.
DR Reactome; REACT_111045; Developmental Biology.
DR ChiTaRS; SLIT1; human.
DR GenomeRNAi; 6585; -.
DR NextBio; 25625; -.
DR ArrayExpress; O75093; -.
DR Bgee; O75093; -.
DR CleanEx; HS_SLIT1; -.
DR Genevestigator; O75093; -.
DR GermOnline; ENSG00000187122; Homo sapiens.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005615; C:extracellular space; NAS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0048846; P:axon extension involved in axon guidance; IDA:UniProtKB.
DR GO; GO:0033563; P:dorsal/ventral axon guidance; IEA:Compara.
DR GO; GO:0040023; P:establishment of nucleus localization; IEA:Compara.
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:0048843; P:negative regulation of axon extension involved in axon guidance; IEA:Compara.
DR GO; GO:0051964; P:negative regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Compara.
DR GO; GO:0021510; P:spinal cord development; IEA:Compara.
DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEA:Compara.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013320; ConA-like_subgrp.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR006207; Cys_knot_C.
DR InterPro; IPR000742; EG-like_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd.
DR InterPro; IPR013032; EGF-like_CS.
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; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR000372; LRR-contain_N.
DR Pfam; PF00008; EGF; 3.
DR Pfam; PF12661; hEGF; 2.
DR Pfam; PF02210; Laminin_G_2; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF01463; LRRCT; 4.
DR Pfam; PF01462; LRRNT; 4.
DR SMART; SM00041; CT; 1.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00274; FOLN; 4.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00369; LRR_TYP; 10.
DR SMART; SM00082; LRRCT; 4.
DR SMART; SM00013; LRRNT; 4.
DR SUPFAM; SSF49899; ConA_like_lec_gl; 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 Potential.
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.
FT DOMAIN 964 1003 EGF-like 2.
FT DOMAIN 1005 1041 EGF-like 3.
FT DOMAIN 1043 1081 EGF-like 4.
FT DOMAIN 1083 1119 EGF-like 5.
FT DOMAIN 1127 1163 EGF-like 6.
FT DOMAIN 1166 1339 Laminin G-like.
FT DOMAIN 1340 1374 EGF-like 7.
FT DOMAIN 1377 1413 EGF-like 8.
FT DOMAIN 1418 1454 EGF-like 9.
FT DOMAIN 1459 1534 CTCK.
FT CARBOHYD 72 72 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 192 192 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 406 406 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 571 571 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 630 630 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 762 762 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 801 801 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 806 806 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1026 1026 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1079 1079 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1189 1189 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1259 1259 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1306 1306 N-linked (GlcNAc...) (Potential).
FT DISULFID 286 295 By similarity.
FT DISULFID 443 466 By similarity.
FT DISULFID 445 487 By similarity.
FT DISULFID 513 519 By similarity.
FT DISULFID 517 526 By similarity.
FT DISULFID 675 698 By similarity.
FT DISULFID 677 719 By similarity.
FT DISULFID 929 940 By similarity.
FT DISULFID 934 950 By similarity.
FT DISULFID 952 961 By similarity.
FT DISULFID 968 979 By similarity.
FT DISULFID 973 991 By similarity.
FT DISULFID 993 1002 By similarity.
FT DISULFID 1009 1020 By similarity.
FT DISULFID 1014 1029 By similarity.
FT DISULFID 1031 1040 By similarity.
FT DISULFID 1047 1060 By similarity.
FT DISULFID 1054 1069 By similarity.
FT DISULFID 1071 1080 By similarity.
FT DISULFID 1087 1098 By similarity.
FT DISULFID 1092 1107 By similarity.
FT DISULFID 1109 1118 By similarity.
FT DISULFID 1131 1142 By similarity.
FT DISULFID 1136 1151 By similarity.
FT DISULFID 1153 1162 By similarity.
FT DISULFID 1313 1339 By similarity.
FT DISULFID 1342 1352 By similarity.
FT DISULFID 1347 1362 By similarity.
FT DISULFID 1364 1373 By similarity.
FT DISULFID 1381 1391 By similarity.
FT DISULFID 1386 1401 By similarity.
FT DISULFID 1403 1412 By similarity.
FT DISULFID 1422 1432 By similarity.
FT DISULFID 1427 1442 By similarity.
FT DISULFID 1444 1453 By similarity.
FT DISULFID 1459 1498 By similarity.
FT DISULFID 1477 1512 By similarity.
FT DISULFID 1488 1528 By similarity.
FT DISULFID 1492 1530 By similarity.
FT VAR_SEQ 338 338 I -> IRPLSFCSPCR (in isoform 2).
FT /FTId=VSP_009706.
FT VAR_SEQ 790 813 Missing (in isoform 2).
FT /FTId=VSP_009707.
FT VAR_SEQ 830 1534 Missing (in isoform 2).
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 CONFLICT 163 163 Q -> R (in Ref. 1; BAA35184).
FT CONFLICT 829 829 Q -> P (in Ref. 8; AAK31796).
FT CONFLICT 966 966 D -> N (in Ref. 1; BAA35184).
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
//
