SLIT2_MOUSE
ID SLIT2_MOUSE Reviewed; 1521 AA.
AC Q9R1B9; E9QKB4; Q9Z166;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Slit homolog 2 protein;
DE Short=Slit-2;
DE Contains:
DE RecName: Full=Slit homolog 2 protein N-product;
DE Contains:
DE RecName: Full=Slit homolog 2 protein C-product;
DE Flags: Precursor;
GN Name=Slit2;
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], AND DEVELOPMENTAL 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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 497-1521.
RX PubMed=10349621; DOI=10.1016/s0925-4773(98)00174-9;
RA Holmes G.P., Negus K., Burridge L., Raman S., Algar E., Yamada T.,
RA Little M.H.;
RT "Distinct but overlapping expression patterns of two vertebrate slit
RT homologs implies functional roles in CNS development and organogenesis.";
RL Mech. Dev. 79:57-72(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 577-1521.
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 [5]
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 [6]
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 [7]
RP TISSUE SPECIFICITY.
RX PubMed=10864954; DOI=10.1523/jneurosci.20-13-04962.2000;
RA Niclou S.P., Jia L., Raper J.A.;
RT "Slit2 is a repellent for retinal ganglion cell axons.";
RL J. Neurosci. 20:4962-4974(2000).
RN [8]
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. SLIT1 and SLIT2 seem to be
CC essential for midline guidance in the forebrain by acting as repulsive
CC signal preventing inappropriate midline crossing by axons projecting
CC from the olfactory bulb. In spinal cord development, may play a role in
CC guiding commissural axons once they reached the floor plate by
CC modulating the response to netrin. In vitro, silences the attractive
CC effect of NTN1 but not its growth-stimulatory effect and silencing
CC requires the formation of a ROBO1-DCC complex. May be implicated in
CC spinal cord midline post-crossing axon repulsion. In vitro, only
CC commissural axons that crossed the midline responded to SLIT2. In the
CC developing visual system, appears to function as repellent for retinal
CC ganglion axons by providing a repulsion that directs these axons along
CC their appropriate paths prior to, and after passage through, the optic
CC chiasm. In vitro, collapses and repels retinal ganglion cell growth
CC cones. Seems to play a role in branching and arborization of CNS
CC sensory axons, and in neuronal cell migration. In vitro, Slit homolog 2
CC protein N-product, but not Slit homolog 2 protein C-product, repels
CC olfactory bulb (OB) but not dorsal root ganglia (DRG) axons, induces OB
CC growth cones collapse and induces branching of DRG axons. Seems to be
CC involved in regulating leukocyte migration (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:11804571,
CC ECO:0000269|PubMed:12097499}.
CC -!- SUBUNIT: Homodimer. Interacts with GREM1 (By similarity). Binds ROBO1
CC and ROBO2 with high affinity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=The C-terminal
CC cleavage protein is more diffusible than the larger N-terminal protein
CC that is more tightly cell associated. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in developing eye, in the optic stalk,
CC and in the ventral diencephalon. {ECO:0000269|PubMed:10864954}.
CC -!- DEVELOPMENTAL STAGE: According to PubMed:10864955 is expressed during
CC retinal development by 14.5 dpc throughout the RGC layer, and is
CC clearly restricted to the inner nuclear layer at 17.5 dpc. In the
CC developing optic chiasm is strongly expressed at 12.5 dpc at the
CC ventral midline of the diencephalon in the region in which the RGC
CC axons enter the brain and turn to grow ventrally, the region expression
CC includes the position of the glial knot. At 14.5 dpc expression is
CC maintained at the ventral midline of the diencephalon, in a region
CC directly dorsal to the site of axon divergence. Outside the developing
CC brain. According to PubMed:10433822 prominently expressed in neural and
CC mesodermally derived tissues. From 8.5 dpc to 9.5 dpc expressed
CC strongly in the roof plate, floor plate, and notochord. Beginning at
CC 10.5 dpc intense expression is also observed in the motor columns. By
CC 13.5 dpc the expression decreased in the roof plate but is still
CC retained in the floor plate and motor columns. In the rostral CNS
CC between 8.5 dpc and 9.5 dpc expressed intensely in the dorsal
CC neuroepithelium overlying the hindbrain, in the dorsal midline of the
CC midbrain and forebrain, and in the ventral midbrain region. By 10.5 dpc
CC to 11.5 dpc, additional intense expression is observed in the rhombic
CC lip and the rostral midline. From 13.5 dpc to 17.5 dpc, the expression
CC decreased dorsally and continued to be detected in the ventral
CC mesencephalon and diencephalon. Outside neuronal development expressed
CC between 8.5 dpc and 9.5 dpc in the clefts between the first, the
CC second, and the third branchial arches. From 10.5 dpc to 11.5 dpc,
CC expression is detected in the nasal pit, the developing eye, the otic
CC vesicle, and the visceral grooves. From 13.5 dpc to 17.5 dpc expressed
CC in the developing cochlea (in a pattern consistent with expression in
CC the organ of Corti), in the olfactory epithelium and in the inner
CC neuronal layer of the retina and in the optic nerve. At this stage also
CC expressed in the tongue, in the tooth primordium, and in the outer root
CC sheath of the whisker follicle in the layer surrounding the bulb. At
CC 11.5 dpc is intensely expressed in the rostral lateral ridge flanking
CC the forelimb buds and in lateral ridge tissue between the fore- and the
CC hindlimb buds. Weak expression is observed in a segmented pattern in
CC the posterior part of the sclerotome. Expression is notably absent in
CC the base of the limb buds and weak expression is observed in the
CC interdigital regions of the distal limb bud beginning at 11.5 dpc. By
CC 13.5 dpc intensely expressed in interdigital mesenchyme.
CC {ECO:0000269|PubMed:10433822, ECO:0000269|PubMed:10864955}.
CC -!- DOMAIN: The leucine-rich repeat domain is sufficient for guiding both
CC axon projection and neuronal migration, in vitro.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF144628; AAD44759.1; -; mRNA.
DR EMBL; AC101004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC157351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF074960; AAD04345.1; -; mRNA.
DR EMBL; BC059267; AAH59267.1; -; mRNA.
DR CCDS; CCDS19280.1; -.
DR PIR; T42626; T42626.
DR RefSeq; NP_848919.3; NM_178804.5.
DR AlphaFoldDB; Q9R1B9; -.
DR BioGRID; 203328; 6.
DR DIP; DIP-61876N; -.
DR IntAct; Q9R1B9; 3.
DR MINT; Q9R1B9; -.
DR STRING; 10090.ENSMUSP00000127615; -.
DR GlyGen; Q9R1B9; 12 sites.
DR iPTMnet; Q9R1B9; -.
DR PhosphoSitePlus; Q9R1B9; -.
DR MaxQB; Q9R1B9; -.
DR PaxDb; Q9R1B9; -.
DR PRIDE; Q9R1B9; -.
DR ProteomicsDB; 261192; -.
DR Antibodypedia; 3487; 324 antibodies from 40 providers.
DR DNASU; 20563; -.
DR Ensembl; ENSMUST00000173107; ENSMUSP00000133840; ENSMUSG00000031558.
DR GeneID; 20563; -.
DR KEGG; mmu:20563; -.
DR UCSC; uc008xjo.3; mouse.
DR CTD; 9353; -.
DR MGI; MGI:1315205; Slit2.
DR VEuPathDB; HostDB:ENSMUSG00000031558; -.
DR eggNOG; KOG4237; Eukaryota.
DR GeneTree; ENSGT00940000158402; -.
DR InParanoid; Q9R1B9; -.
DR TreeFam; TF332887; -.
DR Reactome; R-MMU-376176; Signaling by ROBO receptors.
DR Reactome; R-MMU-428890; Role of ABL in ROBO-SLIT signaling.
DR Reactome; R-MMU-8985586; SLIT2:ROBO1 increases RHOA activity.
DR Reactome; R-MMU-9010553; Regulation of expression of SLITs and ROBOs.
DR BioGRID-ORCS; 20563; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Slit2; mouse.
DR PRO; PR:Q9R1B9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9R1B9; protein.
DR Bgee; ENSMUSG00000031558; Expressed in metanephric ureteric bud and 309 other tissues.
DR ExpressionAtlas; Q9R1B9; baseline and differential.
DR Genevisible; Q9R1B9; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0045499; F:chemorepellent activity; IMP:MGI.
DR GO; GO:0005095; F:GTPase inhibitor activity; ISO:MGI.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0043237; F:laminin-1 binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0043394; F:proteoglycan binding; ISO:MGI.
DR GO; GO:0048495; F:Roundabout binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; TAS:MGI.
DR GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
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:0048754; P:branching morphogenesis of an epithelial tube; ISO:MGI.
DR GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISO:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI.
DR GO; GO:0071504; P:cellular response to heparin; ISO:MGI.
DR GO; GO:0021836; P:chemorepulsion involved in postnatal olfactory bulb interneuron migration; ISO:MGI.
DR GO; GO:0021972; P:corticospinal neuron axon guidance through spinal cord; ISO:MGI.
DR GO; GO:0033563; P:dorsal/ventral axon guidance; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0050929; P:induction of negative chemotaxis; ISO:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0060763; P:mammary duct terminal end bud growth; IMP:MGI.
DR GO; GO:0060603; P:mammary gland duct morphogenesis; IMP:MGI.
DR GO; GO:0001656; P:metanephros development; IMP:MGI.
DR GO; GO:0008045; P:motor neuron axon guidance; ISO:MGI.
DR GO; GO:0050919; P:negative chemotaxis; IMP:MGI.
DR GO; GO:0030837; P:negative regulation of actin filament polymerization; ISO:MGI.
DR GO; GO:0030517; P:negative regulation of axon extension; IDA:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0090288; P:negative regulation of cellular response to growth factor stimulus; ISO:MGI.
DR GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IGI:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:MGI.
DR GO; GO:0010593; P:negative regulation of lamellipodium assembly; ISO:MGI.
DR GO; GO:0002689; P:negative regulation of leukocyte chemotaxis; ISO:MGI.
DR GO; GO:0090027; P:negative regulation of monocyte chemotaxis; ISO:MGI.
DR GO; GO:0071676; P:negative regulation of mononuclear cell migration; ISO:MGI.
DR GO; GO:0090024; P:negative regulation of neutrophil chemotaxis; ISO:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0090260; P:negative regulation of retinal ganglion cell axon guidance; ISO:MGI.
DR GO; GO:0051058; P:negative regulation of small GTPase mediated signal transduction; ISO:MGI.
DR GO; GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; ISO:MGI.
DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0043116; P:negative regulation of vascular permeability; ISO:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:MGI.
DR GO; GO:0021772; P:olfactory bulb development; IGI:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0003184; P:pulmonary valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:MGI.
DR GO; GO:0035385; P:Roundabout signaling pathway; ISO:MGI.
DR GO; GO:0022029; P:telencephalon cell migration; IGI:MGI.
DR GO; GO:0001657; P:ureteric bud development; ISO:MGI.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
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; 5.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF00054; Laminin_G_1; 1.
DR Pfam; PF13855; LRR_8; 7.
DR Pfam; PF01463; LRRCT; 4.
DR Pfam; PF01462; LRRNT; 3.
DR SMART; SM00041; CT; 1.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 6.
DR SMART; SM00274; FOLN; 3.
DR SMART; SM00282; LamG; 1.
DR SMART; SM00369; LRR_TYP; 17.
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; 7.
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 2: Evidence at transcript level;
KW Chemotaxis; Developmental protein; Differentiation; Disulfide bond;
KW EGF-like domain; Glycoprotein; Heparin-binding; Leucine-rich repeat;
KW Neurogenesis; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1521
FT /note="Slit homolog 2 protein"
FT /id="PRO_0000007728"
FT CHAIN 26..1113
FT /note="Slit homolog 2 protein N-product"
FT /evidence="ECO:0000250"
FT /id="PRO_0000007729"
FT CHAIN 1114..1521
FT /note="Slit homolog 2 protein C-product"
FT /evidence="ECO:0000250"
FT /id="PRO_0000007730"
FT DOMAIN 26..55
FT /note="LRRNT"
FT REPEAT 56..77
FT /note="LRR 1"
FT REPEAT 80..101
FT /note="LRR 2"
FT REPEAT 104..125
FT /note="LRR 3"
FT REPEAT 128..149
FT /note="LRR 4"
FT REPEAT 152..173
FT /note="LRR 5"
FT REPEAT 176..197
FT /note="LRR 6"
FT DOMAIN 209..259
FT /note="LRRCT 1"
FT DOMAIN 264..300
FT /note="LRRNT 2"
FT REPEAT 301..322
FT /note="LRR 7"
FT REPEAT 325..346
FT /note="LRR 8"
FT REPEAT 349..370
FT /note="LRR 9"
FT REPEAT 373..394
FT /note="LRR 10"
FT REPEAT 397..418
FT /note="LRR 11"
FT DOMAIN 430..480
FT /note="LRRCT 2"
FT DOMAIN 489..525
FT /note="LRRNT 3"
FT REPEAT 526..547
FT /note="LRR 12"
FT REPEAT 551..572
FT /note="LRR 13"
FT REPEAT 575..596
FT /note="LRR 14"
FT REPEAT 599..620
FT /note="LRR 15"
FT REPEAT 623..644
FT /note="LRR 16"
FT DOMAIN 656..706
FT /note="LRRCT 3"
FT DOMAIN 710..746
FT /note="LRRNT 4"
FT REPEAT 747..769
FT /note="LRR 17"
FT REPEAT 770..791
FT /note="LRR 18"
FT REPEAT 794..815
FT /note="LRR 19"
FT REPEAT 818..839
FT /note="LRR 20"
FT DOMAIN 851..901
FT /note="LRRCT 4"
FT DOMAIN 912..947
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 949..988
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 990..1026
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1028..1066
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1068..1104
FT /note="EGF-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1113..1149
FT /note="EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1152..1325
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1329..1360
FT /note="EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1363..1399
FT /note="EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1404..1440
FT /note="EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1445..1520
FT /note="CTCK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039"
FT SITE 1113..1114
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 786
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1001
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1002
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1011
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 277..286
FT /evidence="ECO:0000250"
FT DISULFID 434..457
FT /evidence="ECO:0000250"
FT DISULFID 436..478
FT /evidence="ECO:0000250"
FT DISULFID 498..504
FT /evidence="ECO:0000250"
FT DISULFID 502..511
FT /evidence="ECO:0000250"
FT DISULFID 660..683
FT /evidence="ECO:0000250"
FT DISULFID 662..704
FT /evidence="ECO:0000250"
FT DISULFID 719..725
FT /evidence="ECO:0000250"
FT DISULFID 723..732
FT /evidence="ECO:0000250"
FT DISULFID 855..878
FT /evidence="ECO:0000250"
FT DISULFID 857..899
FT /evidence="ECO:0000250"
FT DISULFID 914..925
FT /evidence="ECO:0000250"
FT DISULFID 919..935
FT /evidence="ECO:0000250"
FT DISULFID 937..946
FT /evidence="ECO:0000250"
FT DISULFID 953..964
FT /evidence="ECO:0000250"
FT DISULFID 958..976
FT /evidence="ECO:0000250"
FT DISULFID 978..987
FT /evidence="ECO:0000250"
FT DISULFID 994..1005
FT /evidence="ECO:0000250"
FT DISULFID 999..1014
FT /evidence="ECO:0000250"
FT DISULFID 1016..1025
FT /evidence="ECO:0000250"
FT DISULFID 1032..1045
FT /evidence="ECO:0000250"
FT DISULFID 1039..1054
FT /evidence="ECO:0000250"
FT DISULFID 1056..1065
FT /evidence="ECO:0000250"
FT DISULFID 1072..1083
FT /evidence="ECO:0000250"
FT DISULFID 1077..1092
FT /evidence="ECO:0000250"
FT DISULFID 1094..1103
FT /evidence="ECO:0000250"
FT DISULFID 1117..1128
FT /evidence="ECO:0000250"
FT DISULFID 1122..1137
FT /evidence="ECO:0000250"
FT DISULFID 1139..1148
FT /evidence="ECO:0000250"
FT DISULFID 1299..1325
FT /evidence="ECO:0000250"
FT DISULFID 1333..1338
FT /evidence="ECO:0000250"
FT DISULFID 1350..1359
FT /evidence="ECO:0000250"
FT DISULFID 1367..1377
FT /evidence="ECO:0000250"
FT DISULFID 1372..1387
FT /evidence="ECO:0000250"
FT DISULFID 1389..1398
FT /evidence="ECO:0000250"
FT DISULFID 1408..1418
FT /evidence="ECO:0000250"
FT DISULFID 1413..1428
FT /evidence="ECO:0000250"
FT DISULFID 1430..1439
FT /evidence="ECO:0000250"
FT DISULFID 1445..1484
FT /evidence="ECO:0000250"
FT DISULFID 1463..1498
FT /evidence="ECO:0000250"
FT DISULFID 1474..1514
FT /evidence="ECO:0000250"
FT DISULFID 1478..1516
FT /evidence="ECO:0000250"
FT CONFLICT 73
FT /note="I -> T (in Ref. 1; AAD44759)"
FT /evidence="ECO:0000305"
FT CONFLICT 903
FT /note="V -> M (in Ref. 3; AAD04345)"
FT /evidence="ECO:0000305"
FT CONFLICT 1277
FT /note="P -> S (in Ref. 4; AAH59267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1521 AA; 168783 MW; 0DC3626D46FDB711 CRC64;
MSGIGWQTLS LSLGLVLSIL NKVAPQACPA QCSCSGSTVD CHGLALRSVP RNIPRNTERL
DLNGNNITRI TKIDFAGLRH LRVLQLMENR ISTIERGAFQ DLKELERLRL NRNNLQLFPE
LLFLGTAKLY RLDLSENQIQ AIPRKAFRGA VDIKNLQLDY NQISCIEDGA FRALRDLEVL
TLNNNNITRL SVASFNHMPK LRTFRLHSNN LYCDCHLAWL SDWLRQRPRV GLYTQCMGPS
HLRGHNVAEV QKREFVCSGH QSFMAPSCSV LHCPAACTCS NNIVDCRGKG LTEIPTNLPE
TITEIRLEQN SIRVIPPGAF SPYKKLRRLD LSNNQISELA PDAFQGLRSL NSLVLYGNKI
TELPKSLFEG LFSLQLLLLN ANKINCLRVD AFQDLHNLNL LSLYDNKLQT VAKGTFSALR
AIQTMHLAQN PFICDCHLKW LADYLHTNPI ETSGARCTSP RRLANKRIGQ IKSKKFRCSG
TEDYRSKLSG DCFADLACPE KCRCEGTTVD CSNQRLNKIP DHIPQYTAEL RLNNNEFTVL
EATGIFKKLP QLRKINFSNN KITDIEEGAF EGASGVNEIL LTSNRLENVQ HKMFKGLESL
KTLMLRSNRI SCVGNDSFIG LGSVRLLSLY DNQITTVAPG AFDSLHSLST LNLLANPFNC
NCHLAWLGEW LRRKRIVTGN PRCQKPYFLK EIPIQDVAIQ DFTCDDGNDD NSCSPLSRCP
SECTCLDTVV RCSNKGLKVL PKGIPKDVTE LYLDGNQFTL VPKELSNYKH LTLIDLSNNR
ISTLSNQSFS NMTQLLTLIL SYNRLRCIPP RTFDGLKSLR LLSLHGNDIS VVPEGAFNDL
SALSHLAIGA NPLYCDCNMQ WLSDWVKSEY KEPGIARCAG PGEMADKLLL TTPSKKFTCQ
GPVDITIQAK CNPCLSNPCK NDGTCNNDPV DFYRCTCPYG FKGQDCDVPI HACISNPCKH
GGTCHLKEGE NAGFWCTCAD GFEGENCEVN IDDCEDNDCE NNSTCVDGIN NYTCLCPPEY
TGELCEEKLD FCAQDLNPCQ HDSKCILTPK GFKCDCTPGY IGEHCDIDFD DCQDNKCKNG
AHCTDAVNGY TCVCPEGYSG LFCEFSPPMV LPRTSPCDNF DCQNGAQCII RINEPICQCL
PGYLGEKCEK LVSVNFVNKE SYLQIPSAKV RPQTNITLQI ATDEDSGILL YKGDKDHIAV
ELYRGRVRAS YDTGSHPASA IYSVETINDG NFHIVELLTL DSSLSLSVDG GSPKVITNLS
KQSTLNFDSP LYVGGMPGKN NVASLRQAPG QNGTSFHGCI RNLYINSELQ DFRKMPMQTG
ILPGCEPCHK KVCAHGMCQP SSQSGFTCEC EEGWMGPLCD QRTNDPCLGN KCVHGTCLPI
NAFSYSCKCL EGHGGVLCDE EEDLFNPCQM IKCKHGKCRL SGVGQPYCEC NSGFTGDSCD
REISCRGERI RDYYQKQQGY AACQTTKKVS RLECRGGCAG GQCCGPLRSK RRKYSFECTD
GSSFVDEVEK VVKCGCARCA S
