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Database: UniProt
Entry: SLIT1_HUMAN
LinkDB: SLIT1_HUMAN
Original site: SLIT1_HUMAN 
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   29-OCT-2014, entry version 140.
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   -!- SIMILARITY: Contains 1 CTCK (C-terminal cystine knot-like) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00039}.
CC   -!- SIMILARITY: Contains 9 EGF-like domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00076}.
CC   -!- SIMILARITY: Contains 1 laminin G-like domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00122}.
CC   -!- SIMILARITY: Contains 20 LRR (leucine-rich) repeats. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 4 LRRCT domains. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 4 LRRNT domains. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA32465.3; Type=Erroneous initiation; Evidence={ECO:0000305};
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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   CCDS; CCDS7453.1; -. [O75093-1]
DR   RefSeq; NP_003052.2; NM_003061.2. [O75093-1]
DR   UniGene; Hs.632082; -.
DR   ProteinModelPortal; O75093; -.
DR   SMR; O75093; 30-1521.
DR   BioGrid; 112472; 1.
DR   IntAct; O75093; 2.
DR   MINT; MINT-2797238; -.
DR   STRING; 9606.ENSP00000266058; -.
DR   PhosphoSite; O75093; -.
DR   MaxQB; O75093; -.
DR   PaxDb; O75093; -.
DR   PRIDE; O75093; -.
DR   Ensembl; ENST00000266058; ENSP00000266058; ENSG00000187122. [O75093-1]
DR   GeneID; 6585; -.
DR   KEGG; hsa:6585; -.
DR   UCSC; uc001kmw.2; human. [O75093-1]
DR   UCSC; uc009xvh.1; human. [O75093-2]
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   GeneTree; ENSGT00760000118811; -.
DR   HOGENOM; HOG000116120; -.
DR   HOVERGEN; HBG057959; -.
DR   InParanoid; O75093; -.
DR   KO; K06838; -.
DR   OrthoDB; EOG78WKQW; -.
DR   PhylomeDB; O75093; -.
DR   TreeFam; TF332887; -.
DR   Reactome; REACT_22237; Netrin-1 signaling.
DR   ChiTaRS; SLIT1; human.
DR   GeneWiki; SLIT1; -.
DR   GenomeRNAi; 6585; -.
DR   NextBio; 25625; -.
DR   PRO; PR:O75093; -.
DR   Bgee; O75093; -.
DR   CleanEx; HS_SLIT1; -.
DR   ExpressionAtlas; O75093; baseline.
DR   Genevestigator; O75093; -.
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:0040023; P:establishment of nucleus localization; 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:0048843; P:negative regulation of axon extension involved in axon guidance; IEA:Ensembl.
DR   GO; GO:0051964; P:negative regulation of synapse assembly; ISS:UniProtKB.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
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; IEA:Ensembl.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom.
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_dom.
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; IPR009030; Growth_fac_rcpt_N_dom.
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; PF12799; LRR_4; 1.
DR   Pfam; PF13855; LRR_8; 5.
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; 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...). {ECO:0000255}.
FT   CARBOHYD    192    192       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    406    406       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    571    571       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    630    630       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    762    762       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    801    801       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    806    806       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1026   1026       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1079   1079       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1189   1189       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1259   1259       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1306   1306       N-linked (GlcNAc...). {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
//
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