SLIK1_PONAB
ID SLIK1_PONAB Reviewed; 696 AA.
AC Q5RAC4;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=SLIT and NTRK-like protein 1;
DE Flags: Precursor;
GN Name=SLITRK1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: It is involved in synaptogenesis and promotes excitatory
CC synapse differentiation. Enhances neuronal dendrite outgrowth.
CC {ECO:0000250|UniProtKB:Q96PX8}.
CC -!- SUBUNIT: Can form homodimers; homodimerization requires repeat LRR 2.
CC Interacts with YWHAB, YWHAE, YWHAG, YWHAH, SFN, YWHAQ and YWHAZ.
CC {ECO:0000250|UniProtKB:Q96PX8}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q96PX8}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:Q96PX8}. Secreted
CC {ECO:0000250|UniProtKB:Q96PX8}. Synapse {ECO:0000250|UniProtKB:Q810C1}.
CC -!- PTM: Undergoes proteolytic cleavage that results in shedding of the
CC ectodomain and cleavage of the C-terminal cytoplasmic tail.
CC Glycosylated. Phosphorylation at Ser-695 is necessary for proper
CC function in promoting neurite outgrowth.
CC {ECO:0000250|UniProtKB:Q96PX8}.
CC -!- SIMILARITY: Belongs to the SLITRK family. {ECO:0000305}.
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DR EMBL; CR859094; CAH91286.1; -; mRNA.
DR RefSeq; NP_001125761.1; NM_001132289.1.
DR AlphaFoldDB; Q5RAC4; -.
DR SMR; Q5RAC4; -.
DR STRING; 9601.ENSPPYP00000006192; -.
DR GeneID; 100172686; -.
DR KEGG; pon:100172686; -.
DR CTD; 114798; -.
DR eggNOG; ENOG502QTHH; Eukaryota.
DR InParanoid; Q5RAC4; -.
DR OrthoDB; 217854at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; IEA:InterPro.
DR GO; GO:0050772; P:positive regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:1905606; P:regulation of presynapse assembly; IEA:InterPro.
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; IPR043326; Slitrk.
DR PANTHER; PTHR45773; PTHR45773; 1.
DR Pfam; PF13855; LRR_8; 2.
DR SMART; SM00369; LRR_TYP; 11.
DR SMART; SM00082; LRRCT; 2.
DR PROSITE; PS51450; LRR; 12.
PE 2: Evidence at transcript level;
KW Glycoprotein; Leucine-rich repeat; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..696
FT /note="SLIT and NTRK-like protein 1"
FT /id="PRO_0000045829"
FT TOPO_DOM 18..622
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..696
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..57
FT /note="LRRNT 1"
FT REPEAT 59..80
FT /note="LRR 1"
FT REPEAT 83..104
FT /note="LRR 2"
FT REPEAT 106..128
FT /note="LRR 3"
FT REPEAT 131..152
FT /note="LRR 4"
FT REPEAT 155..176
FT /note="LRR 5"
FT REPEAT 178..199
FT /note="LRR 6"
FT DOMAIN 212..263
FT /note="LRRCT 1"
FT DOMAIN 332..373
FT /note="LRRNT 2"
FT REPEAT 376..397
FT /note="LRR 7"
FT REPEAT 400..421
FT /note="LRR 8"
FT REPEAT 424..445
FT /note="LRR 9"
FT REPEAT 448..469
FT /note="LRR 10"
FT REPEAT 472..493
FT /note="LRR 11"
FT REPEAT 495..516
FT /note="LRR 12"
FT DOMAIN 529..580
FT /note="LRRCT 2"
FT REGION 265..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PX8"
SQ SEQUENCE 696 AA; 77699 MW; 7AF48D3844D97CBC CRC64;
MLLWILLLET SLCFAAGNVT GDVCKEKICS CNEIEGDLHV DCEKKGFTSL QRFTAPTSQF
YHLFLHGNSL TRLFPNEFAN FYNAVSLHME NNGLHEIVPG AFLGLQLVKR LHINNNKIKS
FRKQTFLGLD DLEYLQADFN LLRDIDPGAF QDLNKLEVLI LNDNLISTLP ANVFQYVPIT
HLDLRGNRLK TLPYEEVLEQ IPGIAEILLE DNPWDCTCDL LSLKEWLENI PKNALIGRVV
CEAPTRLQGK DLNETTEQDL CPLKNRVDSS LPAPPAQEET FAPGPLPTPF KTNGQEDHAT
PGSAPNGGTK IPGNWQIKIR PTAAIATGSA RNKPLANSLP CPGGCSCDHI PGSGLKMNCN
NRNVSSLADL KPKLSNVQEL FLRDNKIHSI RKSHFVDYKN LILLDLGNNN IATVENNTFK
NLLDLRWLYM DSNYLDTLSR EKFAGLQNLE YLNVEYNAIQ LILPGTFNAM PKLRILILNN
NLLRSLPVDV FAGVSLSKLS LHNNYFMYLP VAGVLDQLTS IIQIDLHGNP WEYSCTIVPF
KQWAERLGSE VLMSDLKCET PVNFFRKDFM LLSNDEICPQ LYARISPTLT SHSKNSTGLA
ETGTHSNSYL DTSRVSISVL VPGLLLVFVT SAFTVVGMLV FILRNGKRSK RRDANSSASE
INSLQTVCDS SYWRNGPYNA DGAHRVYDCG SHSLSD
