SLIT1_RAT
ID SLIT1_RAT Reviewed; 1531 AA.
AC O88279; Q8CJG8; Q8CJG9; Q8CJH0; Q9QWL1; Q9WUG5;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 160.
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=Megf4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; 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-like
RT motifs by motif-trap screening.";
RL Genomics 51:27-34(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10102268; DOI=10.1016/s0092-8674(00)80590-5;
RA Brose K., Bland K.S., Wang K.H., Arnott D., Henzel W., Goodman C.S.,
RA Tessier-Lavigne M., Kidd T.;
RT "Slit proteins bind Robo receptors and have an evolutionarily conserved
RT role in repulsive axon guidance.";
RL Cell 96:795-806(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Tanno T.;
RT "Alternative splicing for slit-1 in rat brain.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1209-1404 (ISOFORMS 1/2/3/4), AND TISSUE
RP 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 slit
RT suggest possible roles for Slit in the formation and maintenance of the
RT nervous system.";
RL Brain Res. Mol. Brain Res. 62:175-186(1998).
RN [5]
RP FUNCTION.
RX PubMed=10864956; DOI=10.1523/jneurosci.20-13-04983.2000;
RA Ringstedt T., Braisted J.E., Brose K., Kidd T., Goodman C.,
RA Tessier-Lavigne M., O'Leary D.D.;
RT "Slit inhibition of retinal axon growth and its role in retinal axon
RT pathfinding and innervation patterns in the diencephalon.";
RL J. Neurosci. 20:4983-4991(2000).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=11754167; DOI=10.1002/cne.10068;
RA Marillat V., Cases O., Nguyen-Ba-Charvet K.T., Tessier-Lavigne M.,
RA Sotelo C., Chedotal A.;
RT "Spatiotemporal expression patterns of slit and robo genes in the rat
RT brain.";
RL J. Comp. Neurol. 442:130-155(2002).
RN [7]
RP INTERACTION WITH GREM1.
RX PubMed=15528323; DOI=10.4049/jimmunol.173.10.5914;
RA Chen B., Blair D.G., Plisov S., Vasiliev G., Perantoni A.O., Chen Q.,
RA Athanasiou M., Wu J.Y., Oppenheim J.J., Yang D.;
RT "Bone morphogenetic protein antagonists Drm/Gremlin and Dan interact with
RT Slits and act as negative regulators of monocyte chemotaxis.";
RL J. Immunol. 173:5914-5917(2004).
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. SLIT1 and SLIT2 together seem
CC to be essential for midline guidance in the forebrain by acting as
CC repulsive signal preventing inappropriate midline crossing by axons
CC projecting from the olfactory bulb (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10864956}.
CC -!- SUBUNIT: Interacts with ROBO1 (By similarity) and GREM1. {ECO:0000250,
CC ECO:0000269|PubMed:15528323}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O88279-1; Sequence=Displayed;
CC Name=2; Synonyms=Sb;
CC IsoId=O88279-2; Sequence=VSP_009710, VSP_009711;
CC Name=3; Synonyms=La;
CC IsoId=O88279-3; Sequence=VSP_009712, VSP_009713;
CC Name=4; Synonyms=Sa;
CC IsoId=O88279-4; Sequence=VSP_009709;
CC -!- TISSUE SPECIFICITY: In adult brains expressed in the hippocampus,
CC cerebral cortex, and olfactory bulb but not in the cerebellum. In
CC embryo expressed in cerebral cortex. {ECO:0000269|PubMed:9813312}.
CC -!- DEVELOPMENTAL STAGE: Detected between E15 and E20, between P0 and P10,
CC and in adult in different regions of the telencephalon and
CC diencephalon. {ECO:0000269|PubMed:11754167}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC21664.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB011530; BAA32460.1; -; mRNA.
DR EMBL; AF133730; AAD25540.1; -; mRNA.
DR EMBL; AB073213; BAC21664.1; ALT_INIT; mRNA.
DR EMBL; AB073214; BAC21665.1; -; mRNA.
DR EMBL; AB073215; BAC21666.1; -; mRNA.
DR EMBL; AB017170; BAA35187.1; -; mRNA.
DR PIR; T42218; T42218.
DR RefSeq; NP_075242.1; NM_022953.2. [O88279-1]
DR AlphaFoldDB; O88279; -.
DR STRING; 10116.ENSRNOP00000035315; -.
DR GlyGen; O88279; 13 sites.
DR iPTMnet; O88279; -.
DR PhosphoSitePlus; O88279; -.
DR PaxDb; O88279; -.
DR Ensembl; ENSRNOT00000034758; ENSRNOP00000035315; ENSRNOG00000026065. [O88279-1]
DR Ensembl; ENSRNOT00000035415; ENSRNOP00000035180; ENSRNOG00000026065. [O88279-4]
DR Ensembl; ENSRNOT00000111197; ENSRNOP00000079283; ENSRNOG00000026065. [O88279-3]
DR GeneID; 65047; -.
DR KEGG; rno:65047; -.
DR UCSC; RGD:69307; rat. [O88279-1]
DR CTD; 6585; -.
DR RGD; 69307; Slit1.
DR eggNOG; KOG4237; Eukaryota.
DR GeneTree; ENSGT00940000157322; -.
DR InParanoid; O88279; -.
DR OrthoDB; 28488at2759; -.
DR PhylomeDB; O88279; -.
DR PRO; PR:O88279; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:RGD.
DR GO; GO:0008201; F:heparin binding; IBA:GO_Central.
DR GO; GO:0048495; F:Roundabout binding; ISO:RGD.
DR GO; GO:0048846; P:axon extension involved in axon guidance; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0007409; P:axonogenesis; ISO:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0033563; P:dorsal/ventral axon guidance; ISO:RGD.
DR GO; GO:0008045; P:motor neuron axon guidance; ISO:RGD.
DR GO; GO:0050919; P:negative chemotaxis; ISO:RGD.
DR GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IDA:RGD.
DR GO; GO:0051964; P:negative regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:RGD.
DR GO; GO:0007097; P:nuclear migration; ISO:RGD.
DR GO; GO:0021772; P:olfactory bulb development; ISO:RGD.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISO:RGD.
DR GO; GO:0021510; P:spinal cord development; IEP:RGD.
DR GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; ISO:RGD.
DR GO; GO:0022029; P:telencephalon cell migration; ISO:RGD.
DR CDD; cd00110; LamG; 1.
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; 4.
DR Pfam; PF12661; hEGF; 3.
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; 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; 20.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Differentiation;
KW Disulfide bond; EGF-like domain; Glycoprotein; Leucine-rich repeat;
KW Neurogenesis; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..1531
FT /note="Slit homolog 1 protein"
FT /id="PRO_0000007724"
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 2"
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 VAR_SEQ 113..136
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_009709"
FT VAR_SEQ 1412..1474
FT /note="VGAVAEPCGGLQCLHGHCQASATRGAHCVCSPGFSGELCEQESECRGDPVRD
FT FHRVQRGYAIC -> SPSAGGTLSGTFTGSRGAMPSARPRAHCHGWNAGARARARAAAR
FT AAAEAEEAHLRVQRWDLVC (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_009710"
FT VAR_SEQ 1453..1458
FT /note="ESECRG -> GQGAPS (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_009712"
FT VAR_SEQ 1459..1531
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_009713"
FT VAR_SEQ 1475..1531
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_009711"
FT CONFLICT 75
FT /note="R -> W (in Ref. 2; AAD25540)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="Q -> P (in Ref. 2; AAD25540)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="V -> A (in Ref. 3; BAC21666)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="R -> P (in Ref. 2; AAD25540)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="M -> V (in Ref. 3; BAC21665)"
FT /evidence="ECO:0000305"
FT CONFLICT 113..115
FT /note="RLR -> PFQ (in Ref. 2; AAD25540)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="V -> M (in Ref. 2; AAD25540)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="C -> R (in Ref. 3; BAC21664)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="S -> T (in Ref. 3; BAC21665)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="S -> P (in Ref. 3; BAC21665)"
FT /evidence="ECO:0000305"
FT CONFLICT 442..443
FT /note="IC -> TW (in Ref. 3; BAC21665)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="S -> T (in Ref. 3; BAC21666)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="V -> A (in Ref. 3; BAC21666)"
FT /evidence="ECO:0000305"
FT CONFLICT 616..617
FT /note="RT -> WS (in Ref. 2; AAD25540)"
FT /evidence="ECO:0000305"
FT CONFLICT 652
FT /note="I -> T (in Ref. 3; BAC21665)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="Q -> H (in Ref. 3; BAC21666)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="F -> L (in Ref. 3; BAC21665)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="A -> T (in Ref. 3; BAC21665/BAC21666)"
FT /evidence="ECO:0000305"
FT CONFLICT 754..756
FT /note="ALP -> LL (in Ref. 2; AAD25540)"
FT /evidence="ECO:0000305"
FT CONFLICT 921
FT /note="A -> T (in Ref. 3; BAC21666)"
FT /evidence="ECO:0000305"
FT CONFLICT 932
FT /note="S -> N (in Ref. 2; AAD25540)"
FT /evidence="ECO:0000305"
FT CONFLICT 1008
FT /note="D -> N (in Ref. 3; BAC21665)"
FT /evidence="ECO:0000305"
FT CONFLICT 1078
FT /note="D -> A (in Ref. 3; BAC21666)"
FT /evidence="ECO:0000305"
FT CONFLICT 1094
FT /note="N -> T (in Ref. 3; BAC21666)"
FT /evidence="ECO:0000305"
FT CONFLICT 1159
FT /note="C -> R (in Ref. 3; BAC21665)"
FT /evidence="ECO:0000305"
FT CONFLICT 1247
FT /note="E -> K (in Ref. 2; AAD25540)"
FT /evidence="ECO:0000305"
FT CONFLICT 1256
FT /note="N -> D (in Ref. 3; BAC21665)"
FT /evidence="ECO:0000305"
FT CONFLICT 1258
FT /note="S -> F (in Ref. 2; AAD25540)"
FT /evidence="ECO:0000305"
FT CONFLICT 1280..1283
FT /note="APLY -> GPPS (in Ref. 2; AAD25540)"
FT /evidence="ECO:0000305"
FT CONFLICT 1433
FT /note="A -> V (in Ref. 2; AAD25540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1531 AA; 167499 MW; DFC4B60CCBC5529A CRC64;
MALTPQRGSS SGLSRPELWL LLWAAAWRLG ATACPALCTC TGTTVDCHGT GLQAIPKNIP
RNTERLELNG NNITRIHKND FAGLKQLRVL QLMENQIGAV ERGAFDDMKE LERLRLNRNQ
LQVLPELLFQ NNQALSRLDL SENSLQAVPR KAFRGATDLK NLQLDKNQIS CIEEGAFRAL
RGLEVLTLNN NNITTIPVSS FNHMPKLRTF RLHSNHLFCD CHLAWLSQWL RQRPTIGLFT
QCSGPASLRG LNVAEVQKSE FSCSGQGEAA QVPACTLSSG SCPAMCSCSN GIVDCRGKGL
TAIPANLPET MTEIRLELNG IKSIPPGAFS PYRKLRRIDL SNNQIAEIAP DAFQGLRSLN
SLVLYGNKIT DLPRGVFGGL YTLQLLLLNA NKINCIRPDA FQDLQNLSLL SLYDNKIQSL
AKGTFTSLRA IQTLHLAQNP FICDCNLKWL ADFLRTNPIE TTGARCASPR RLANKRIGQI
KSKKFRCSAK EQYFIPGTED YHLNSECTSD VACPHKCRCE ASVVECSGLK LSKIPERIPQ
STTELRLNNN EISILEATGL FKKLSHLKKI NLSNNKVSEI EDGTFEGATS VSELHLTANQ
LESVRSGMFR GLDGLRTLML RNNRISCIHN DSFTGLRNVR LLSLYDNHIT TISPGAFDTL
QALSTLNLLA NPFNCNCQLA WLGDWLRKRK IVTGNPRCQN PDFLRQIPLQ DVAFPDFRCE
EGQEEVGCLP RPQCPQECAC LDTVVRCSNK HLQALPKGIP KNVTELYLDG NQFTLVPGQL
STFKYLQLVD LSNNKISSLS NSSFTNMSQL TTLILSYNAL QCIPPLAFQG LRSLRLLSLH
GNDVSTLQEG IFADVTSLSH LAIGANPLYC DCHLRWLSSW VKTGYKEPGI ARCAGPPEME
GKLLLTTPAK KFECQGPPSL AVQAKCDPCL SSPCQNQGTC HNDPLEVYRC TCPSGYKGRN
CEVSLDSCSS NPCGNGGTCH AQEGEDAGFT CSCPSGFEGL TCGMNTDDCV KHDCVNGGVC
VDGIGNYTCQ CPLQYTGRAC EQLVDFCSPD LNPCQHEAQC VGTPEGPRCE CVPGYTGDNC
SKNQDDCKDH QCQNGAQCVD EINSYACLCA EGYSGQLCEI PPAPRNSCEG 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 ASATRGAHCV
CSPGFSGELC EQESECRGDP VRDFHRVQRG YAICQTTRPL SWVECRGACP GQGCCQGLRL
KRRKLTFECS DGTSFAEEVE KPTKCGCAPC A
