SLIK2_MOUSE
ID SLIK2_MOUSE Reviewed; 846 AA.
AC Q810C0; Q8BXL6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=SLIT and NTRK-like protein 2;
DE Flags: Precursor;
GN Name=Slitrk2;
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 {ECO:0000312|EMBL:BAC67205.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=14550773; DOI=10.1016/s1044-7431(03)00129-5;
RA Aruga J., Mikoshiba K.;
RT "Identification and characterization of Slitrk, a novel neuronal
RT transmembrane protein family controlling neurite outgrowth.";
RL Mol. Cell. Neurosci. 24:117-129(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-724.
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-757, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [4] {ECO:0007744|PDB:4Y61}
RP X-RAY CRYSTALLOGRAPHY (3.36 ANGSTROMS) OF 1-266 IN COMPLEX WITH PTPRD,
RP INTERACTION WITH PTPRD, MUTAGENESIS OF ARG-114; ASP-167; ASP-187; GLU-215
RP AND 247-PHE--HIS-250, FUNCTION, REGION, DISULFIDE BONDS, AND GLYCOSYLATION
RP AT ASN-84 AND ASN-219.
RX PubMed=25989451; DOI=10.1038/srep09686;
RA Yamagata A., Sato Y., Goto-Ito S., Uemura T., Maeda A., Shiroshima T.,
RA Yoshida T., Fukai S.;
RT "Structure of Slitrk2-PTPdelta complex reveals mechanisms for splicing-
RT dependent trans-synaptic adhesion.";
RL Sci. Rep. 5:9686-9686(2015).
CC -!- FUNCTION: It is involved in synaptogenesis (PubMed:25989451). Promotes
CC excitatory synapse differentiation (By similarity). Suppresses neurite
CC outgrowth (PubMed:14550773). {ECO:0000250|UniProtKB:Q9H156,
CC ECO:0000269|PubMed:14550773, ECO:0000269|PubMed:25989451}.
CC -!- SUBUNIT: Interacts with PTPRD; this interaction is PTPRD splicing-
CC dependent and may induce pre-synaptic differentiation.
CC {ECO:0000269|PubMed:25989451}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9H156}.
CC -!- TISSUE SPECIFICITY: In the adult, significant expression is detected
CC only in the brain. Broadly expressed in embryonic brain with highest
CC expression in ventricular layer, subventricular zone, cortical plate,
CC pyramidal layer of hippocampus, subicular neuroepithelium, thalamus,
CC hypothalumus and spinal cord. {ECO:0000269|PubMed:14550773}.
CC -!- DEVELOPMENTAL STAGE: In the embryo, expressed from day 9-12 and
CC continues through later gestational development and into adulthood.
CC {ECO:0000269|PubMed:14550773}.
CC -!- SIMILARITY: Belongs to the SLITRK family. {ECO:0000305}.
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DR EMBL; AB097571; BAC67205.1; -; Genomic_DNA.
DR EMBL; AK044761; BAC32071.2; -; mRNA.
DR CCDS; CCDS30169.1; -.
DR RefSeq; NP_001154903.1; NM_001161431.1.
DR RefSeq; NP_942563.2; NM_198863.2.
DR RefSeq; XP_006528077.1; XM_006528014.1.
DR RefSeq; XP_006528079.1; XM_006528016.1.
DR PDB; 4Y61; X-ray; 3.36 A; B=1-266.
DR PDBsum; 4Y61; -.
DR AlphaFoldDB; Q810C0; -.
DR SMR; Q810C0; -.
DR BioGRID; 232772; 2.
DR STRING; 10090.ENSMUSP00000130057; -.
DR GlyGen; Q810C0; 3 sites.
DR iPTMnet; Q810C0; -.
DR PhosphoSitePlus; Q810C0; -.
DR MaxQB; Q810C0; -.
DR PaxDb; Q810C0; -.
DR PRIDE; Q810C0; -.
DR ProteomicsDB; 261080; -.
DR Antibodypedia; 30574; 148 antibodies from 28 providers.
DR DNASU; 245450; -.
DR Ensembl; ENSMUST00000036043; ENSMUSP00000044094; ENSMUSG00000036790.
DR Ensembl; ENSMUST00000166241; ENSMUSP00000130057; ENSMUSG00000036790.
DR GeneID; 245450; -.
DR KEGG; mmu:245450; -.
DR UCSC; uc009tir.2; mouse.
DR CTD; 84631; -.
DR MGI; MGI:2679449; Slitrk2.
DR VEuPathDB; HostDB:ENSMUSG00000036790; -.
DR eggNOG; ENOG502QR6C; Eukaryota.
DR GeneTree; ENSGT00940000161248; -.
DR HOGENOM; CLU_012706_1_0_1; -.
DR InParanoid; Q810C0; -.
DR OMA; GEQVAYY; -.
DR OrthoDB; 217854at2759; -.
DR PhylomeDB; Q810C0; -.
DR TreeFam; TF351826; -.
DR Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases.
DR BioGRID-ORCS; 245450; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Slitrk2; mouse.
DR PRO; PR:Q810C0; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q810C0; protein.
DR Bgee; ENSMUSG00000036790; Expressed in trigeminal ganglion and 120 other tissues.
DR ExpressionAtlas; Q810C0; baseline and differential.
DR Genevisible; Q810C0; MM.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:UniProtKB.
DR GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
DR GO; GO:0050807; P:regulation of synapse organization; ISO:MGI.
DR GO; GO:0099560; P:synaptic membrane adhesion; ISO:MGI.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
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 InterPro; IPR043326; Slitrk.
DR PANTHER; PTHR45773; PTHR45773; 1.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 10.
DR SMART; SM00082; LRRCT; 2.
DR SMART; SM00013; LRRNT; 2.
DR PROSITE; PS51450; LRR; 12.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein;
KW Leucine-rich repeat; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..846
FT /note="SLIT and NTRK-like protein 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000032676"
FT TOPO_DOM 22..622
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..846
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 63..84
FT /note="LRR 1"
FT REPEAT 87..108
FT /note="LRR 2"
FT REPEAT 111..132
FT /note="LRR 3"
FT REPEAT 135..156
FT /note="LRR 4"
FT REPEAT 159..180
FT /note="LRR 5"
FT REPEAT 182..203
FT /note="LRR 6"
FT DOMAIN 216..265
FT /note="LRRCT 1"
FT DOMAIN 332..374
FT /note="LRRNT"
FT REPEAT 377..398
FT /note="LRR 7"
FT REPEAT 401..422
FT /note="LRR 8"
FT REPEAT 425..446
FT /note="LRR 9"
FT REPEAT 449..470
FT /note="LRR 10"
FT REPEAT 473..494
FT /note="LRR 11"
FT REPEAT 496..517
FT /note="LRR 12"
FT DOMAIN 530..581
FT /note="LRRCT 2"
FT REGION 167..215
FT /note="Required for interaction with PTPRD"
FT /evidence="ECO:0000269|PubMed:25989451"
FT REGION 261..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 757
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:25989451,
FT ECO:0007744|PDB:4Y61"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25989451,
FT ECO:0007744|PDB:4Y61"
FT CARBOHYD 422
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..35
FT /evidence="ECO:0000269|PubMed:25989451,
FT ECO:0007744|PDB:4Y61"
FT DISULFID 33..46
FT /evidence="ECO:0000269|PubMed:25989451,
FT ECO:0007744|PDB:4Y61"
FT DISULFID 220..243
FT /evidence="ECO:0000269|PubMed:25989451,
FT ECO:0007744|PDB:4Y61"
FT DISULFID 222..263
FT /evidence="ECO:0000269|PubMed:25989451,
FT ECO:0007744|PDB:4Y61"
FT MUTAGEN 114
FT /note="R->A: No effect on interaction with PTPRD. No effect
FT on synapse assembly."
FT /evidence="ECO:0000269|PubMed:25989451"
FT MUTAGEN 167
FT /note="D->A: Abolishes interaction with PTPRD. Abolishes
FT synapse assembly."
FT /evidence="ECO:0000269|PubMed:25989451"
FT MUTAGEN 187
FT /note="D->A: Abolishes interaction with PTPRD. Abolishes
FT synapse assembly."
FT /evidence="ECO:0000269|PubMed:25989451"
FT MUTAGEN 215
FT /note="E->A: Abolishes interaction with PTPRD.
FT Significantly reduces synapse assembly."
FT /evidence="ECO:0000269|PubMed:25989451"
FT MUTAGEN 247..250
FT /note="FRLH->ARLA: No effect on interaction with PTPRD. No
FT effect on synapse assembly."
FT /evidence="ECO:0000269|PubMed:25989451"
FT CONFLICT 526
FT /note="D -> H (in Ref. 2; BAC32071)"
FT /evidence="ECO:0000305"
FT STRAND 31..37
FT /evidence="ECO:0007829|PDB:4Y61"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:4Y61"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:4Y61"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4Y61"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:4Y61"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4Y61"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:4Y61"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:4Y61"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:4Y61"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:4Y61"
FT HELIX 151..154
FT /evidence="ECO:0007829|PDB:4Y61"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:4Y61"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:4Y61"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:4Y61"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:4Y61"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:4Y61"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:4Y61"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:4Y61"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:4Y61"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:4Y61"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:4Y61"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:4Y61"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:4Y61"
SQ SEQUENCE 846 AA; 95436 MW; 4DF3E94C445840A6 CRC64;
MLSGVWFLSV LTVAGILQTE SRKTAKDICK IRCLCEEKEN VLNINCENKG FTTVSLLQPP
QYRIYQLFLN GNLLTRLYPN EFVNYSNAVT LHLGNNGLQE IRPGAFSGLK TLKRLHLNNN
KLEVLREDTF LGLESLEYLQ ADYNYISTIE AGAFSKLNKL KVLILNDNLL LSLPSNVFRF
VLLTHLDLRG NRLKVMPFAG VLEHIGGIME IQLEENPWNC TCDLLPLKAW LDTITVFVGE
IVCETPFRLH GKDVTQLTRQ DLCPRKSASG DSSQRSSHSD THVQRLTPTT NPALNPTRAP
KASRPPKMRN RPTPRVTVSK DRQSFGPIMV YQTKSPVALT CPSSCVCTSQ SSDNGLNVNC
QERKFTNISD LQPKPTSPKK LYLTGNYLQT VYKNDLLEYS SLDLLHLGNN RIAVIQEGAF
TNLTSLRRLY LNGNYLEVLY PSMFDGLQSL QYLYLEYNVI KEIKPLTFDA LINLQLLFLN
NNLLRSLPDN IFGGTALTRL NLRNNHFSHL PVKGVLDQLP AFIQIDLQEN PWDCTCDIMG
LKDWTEHANS PVIINEVTCE SPAKHAGEIL KFLGREAICP ENPNLSDGTI LSMNHNTDTP
RSLSVSPSSY PELHTEVPLS VLILGLLVVF ILSVCFGAGL FVFVLKRRKG VPNVPRNATN
LDVSSFQLQY GSYNTETNDK ADGHVYNYIP PPVGQMCQNP IYMQKEGDPV AYYRNLQDFS
YGNLEEKKEE PATLAYTISA TELLEKQATP REPELLYQNI AERVKELPSA GLVHYNFCTL
PKRQFAPSYE SRRQNQDRIN KTVLYGTPRK CFVGQSKPDH PLLQAKPQSE PDYLEVLEKQ
TAISQL
