NTRI_RAT
ID NTRI_RAT Reviewed; 344 AA.
AC Q62718;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Neurotrimin;
DE AltName: Full=GP65;
DE Flags: Precursor;
GN Name=Ntm; Synonyms=Hnt, Nt;
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], AND PROTEIN SEQUENCE OF 217-229.
RC STRAIN=Sprague-Dawley;
RX PubMed=7891157; DOI=10.1523/jneurosci.15-03-02141.1995;
RA Struyk A.F., Canoll P.D., Wolfgang M.J., Rosen C.L., D'Eustachio P.,
RA Salzer J.L.;
RT "Cloning of neurotrimin defines a new subfamily of differentially expressed
RT neural cell adhesion molecules.";
RL J. Neurosci. 15:2141-2156(1995).
RN [2]
RP PROTEIN SEQUENCE OF 33-56; 72-87; 176-193; 230-257; 271-279 AND 301-326,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
CC -!- FUNCTION: Neural cell adhesion molecule.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- TISSUE SPECIFICITY: Central nervous system.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in several developing
CC projection systems: in neurons of the thalamus, subplate, and lower
CC cortical laminae in the forebrain and in the pontine nucleus,
CC cerebellar granule cells, and Purkinje cells in the hindbrain.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON family.
CC {ECO:0000305}.
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; U16845; AAA67445.1; -; mRNA.
DR PIR; I56551; I56551.
DR RefSeq; NP_059050.1; NM_017354.1.
DR AlphaFoldDB; Q62718; -.
DR SMR; Q62718; -.
DR BioGRID; 248433; 2.
DR IntAct; Q62718; 1.
DR MINT; Q62718; -.
DR STRING; 10116.ENSRNOP00000037037; -.
DR GlyGen; Q62718; 8 sites, 6 N-linked glycans (5 sites).
DR iPTMnet; Q62718; -.
DR PhosphoSitePlus; Q62718; -.
DR SwissPalm; Q62718; -.
DR PaxDb; Q62718; -.
DR PRIDE; Q62718; -.
DR GeneID; 50864; -.
DR KEGG; rno:50864; -.
DR UCSC; RGD:620958; rat.
DR CTD; 50863; -.
DR RGD; 620958; Ntm.
DR eggNOG; KOG3510; Eukaryota.
DR InParanoid; Q62718; -.
DR OrthoDB; 583722at2759; -.
DR PhylomeDB; Q62718; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:Q62718; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0060076; C:excitatory synapse; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0021549; P:cerebellum development; IEP:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..32
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 33..321
FT /note="Neurotrimin"
FT /id="PRO_0000015114"
FT PROPEP 322..344
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000015115"
FT DOMAIN 39..126
FT /note="Ig-like C2-type 1"
FT DOMAIN 136..218
FT /note="Ig-like C2-type 2"
FT DOMAIN 222..309
FT /note="Ig-like C2-type 3"
FT LIPID 321
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 157..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 243..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 344 AA; 37998 MW; CBB39BE53B33B224 CRC64;
MGVCGYLFLP WKCLVVVSLR LLFLVPTGVP VRSGDATFPK AMDNVTVRQG ESATLRCTID
NRVTRVAWLN RSTILYAGND KWCLDPRVVL LSNTQTQYSI EIQNVDVYDE GPYTCSVQTD
NHPKTSRVHL IVQVSPKIVE ISSDISINEG NNISLTCIAT GRPEPTVTWR HISPKAVGFV
SEDEYLEIQG ITREQSGEYE CSASNDVAAP VVRRVNVTVN YPPYISEAKG TGVPVGQKGT
LQCEASAVPS AEFQWFKDDK RLVEGKKGVK VENRPFLSRL TFFNVSEHDY GNYTCVASNK
LGHTNASIML FGPGAVSEVN NGTSRRAGCI WLLPLLVLHL LLKF
