NETO2_RAT
ID NETO2_RAT Reviewed; 525 AA.
AC C6K2K4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Neuropilin and tolloid-like protein 2;
DE AltName: Full=Brain-specific transmembrane protein containing 2 CUB and 1 LDL-receptor class A domains protein 2;
DE Flags: Precursor;
GN Name=Neto2; Synonyms=Btcl2;
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], FUNCTION, INTERACTION WITH GRIK2 AND GRIK3,
RP TISSUE SPECIFICITY, AND GLYCOSYLATION.
RC STRAIN=Sprague-Dawley; TISSUE=Cerebellum;
RX PubMed=19217376; DOI=10.1016/j.neuron.2008.12.014;
RA Zhang W., St-Gelais F., Grabner C.P., Trinidad J.C., Sumioka A.,
RA Morimoto-Tomita M., Kim K.S., Straub C., Burlingame A.L., Howe J.R.,
RA Tomita S.;
RT "A transmembrane accessory subunit that modulates kainate-type glutamate
RT receptors.";
RL Neuron 61:385-396(2009).
CC -!- FUNCTION: Accessory subunit of neuronal kainate-sensitive glutamate
CC receptors, GRIK2 and GRIK3. Increases kainate-receptor channel
CC activity, slowing the decay kinetics of the receptors, without
CC affecting their expression at the cell surface, and increasing the open
CC probability of the receptor channels. Modulates the agonist sensitivity
CC of kainate receptors. Slows the decay of kainate receptor-mediated
CC excitatory postsynaptic currents (EPSCs), thus directly influencing
CC synaptic transmission. {ECO:0000269|PubMed:19217376}.
CC -!- SUBUNIT: Interacts with GRIK2 and GRIK3, but neither with AMPA-nor with
CC NMDA-sensitive glutamate receptors. {ECO:0000269|PubMed:19217376}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Brain (at protein level).
CC {ECO:0000269|PubMed:19217376}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19217376}.
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DR EMBL; GQ149762; ACS44815.1; -; mRNA.
DR RefSeq; NP_001100887.2; NM_001107417.2.
DR PDB; 7F56; EM; 4.10 A; E=1-525.
DR PDB; 7F57; EM; 3.80 A; E=1-525.
DR PDB; 7F59; EM; 4.20 A; E=1-525.
DR PDB; 7F5A; EM; 6.40 A; E/F=1-525.
DR PDB; 7F5B; EM; 3.90 A; E=1-525.
DR PDBsum; 7F56; -.
DR PDBsum; 7F57; -.
DR PDBsum; 7F59; -.
DR PDBsum; 7F5A; -.
DR PDBsum; 7F5B; -.
DR AlphaFoldDB; C6K2K4; -.
DR SMR; C6K2K4; -.
DR STRING; 10116.ENSRNOP00000021739; -.
DR GlyGen; C6K2K4; 1 site.
DR iPTMnet; C6K2K4; -.
DR PhosphoSitePlus; C6K2K4; -.
DR PaxDb; C6K2K4; -.
DR PRIDE; C6K2K4; -.
DR Ensembl; ENSRNOT00000021739; ENSRNOP00000021739; ENSRNOG00000016245.
DR GeneID; 307757; -.
DR KEGG; rno:307757; -.
DR CTD; 81831; -.
DR RGD; 1305310; Neto2.
DR eggNOG; ENOG502QW0Z; Eukaryota.
DR InParanoid; C6K2K4; -.
DR OrthoDB; 477476at2759; -.
DR PhylomeDB; C6K2K4; -.
DR PRO; PR:C6K2K4; -.
DR Proteomes; UP000002494; Chromosome 19.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:RGD.
DR GO; GO:2000312; P:regulation of kainate selective glutamate receptor activity; IEA:InterPro.
DR CDD; cd00041; CUB; 2.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.60.120.290; -; 2.
DR Gene3D; 4.10.400.10; -; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR028868; NETO2.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR45645:SF22; PTHR45645:SF22; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF57424; SSF57424; 1.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..525
FT /note="Neuropilin and tolloid-like protein 2"
FT /id="PRO_0000385453"
FT TOPO_DOM 23..347
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..525
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 45..159
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 177..292
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 296..332
FT /note="LDL-receptor class A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BNJ6"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..72
FT /evidence="ECO:0000250"
FT DISULFID 100..122
FT /evidence="ECO:0000250"
FT DISULFID 177..207
FT /evidence="ECO:0000250"
FT DISULFID 234..256
FT /evidence="ECO:0000250"
FT DISULFID 297..309
FT /evidence="ECO:0000250"
FT DISULFID 304..322
FT /evidence="ECO:0000250"
FT DISULFID 316..331
FT /evidence="ECO:0000250"
SQ SEQUENCE 525 AA; 59342 MW; D8D17910224F3256 CRC64;
MALEQLCAVL KVLLITVLVV EGIAVAQKTQ DGQNIGIKHV PATQCGIWVR TSNGGHFASP
NYPDSYPPNK ECIYILEAAP RQRIELTFDE RYYIEPSFEC RFDHLEVRDG PFGFSPLIDR
YCGMKSPALI RSTGRFMWIK FSSDEELEGL GFRAKYSFIP DPDFTYLGGI LNPIPDCQFE
LSGADGIVRS SQVEQEEKTK PGQAVDCIWT IKATPKAKIY LRFLDYQMEH SNECKRNFVA
VYDGSSAIEN LKAKFCSTVA NDVMLKTGVG VIRMWADEGS RLSRFRMLFT SFVEPPCTSS
TFFCHSNMCI NNSLVCNGVQ NCAYPWDENH CKEKKKAGLF EQITKTHGTI IGVTSGIVLV
LLIISILVQV KQPRKKVMAC KTAFNKTGFQ EVFDPPHYEL FSLREKEISA DLADLSEELD
NYQKLRRSST ASRCIHDHHC GSQASSVKQS RTNLSSMELP FRNDFAQPQP MKTFNSTFKK
SSYTFKQTHD CPEQALEDRV MEEIPCEIYV RGRDDSAQAS ISIDF
