NTRI_HUMAN
ID NTRI_HUMAN Reviewed; 344 AA.
AC Q9P121; A0MTT2; Q6UXJ3; Q86VJ9;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Neurotrimin;
DE Short=hNT;
DE AltName: Full=IgLON family member 2;
DE Flags: Precursor;
GN Name=NTM; Synonyms=IGLON2, NT; ORFNames=UNQ297/PRO337;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Li G., Jin J., Tan X., Hu S., Yuan J., Qiang B.;
RT "Cloning and identification of human neurotrimin full length cDNA.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Wang Y., Tao Q.;
RT "Deregulation of neurotrimin (HNT) in tumors.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Skin;
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 PROTEIN SEQUENCE OF 34-48.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
CC -!- FUNCTION: Neural cell adhesion molecule.
CC -!- INTERACTION:
CC Q9P121; Q8N9M1: C19orf47; NbExp=3; IntAct=EBI-4315078, EBI-2835503;
CC Q9P121; P32239: CCKBR; NbExp=3; IntAct=EBI-4315078, EBI-1753137;
CC Q9P121; Q9BYR7: KRTAP3-2; NbExp=4; IntAct=EBI-4315078, EBI-751260;
CC Q9P121; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-4315078, EBI-3958099;
CC Q9P121; Q13449: LSAMP; NbExp=2; IntAct=EBI-4315078, EBI-4314821;
CC Q9P121; Q7Z3B1: NEGR1; NbExp=2; IntAct=EBI-4315078, EBI-4314838;
CC Q9P121-3; O95967: EFEMP2; NbExp=3; IntAct=EBI-12027160, EBI-743414;
CC Q9P121-3; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-12027160, EBI-11959885;
CC Q9P121-3; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-12027160, EBI-1043191;
CC Q9P121-3; P01229: LHB; NbExp=3; IntAct=EBI-12027160, EBI-11659791;
CC Q9P121-3; Q96FE5: LINGO1; NbExp=3; IntAct=EBI-12027160, EBI-719955;
CC Q9P121-3; P52815: MRPL12; NbExp=3; IntAct=EBI-12027160, EBI-358272;
CC Q9P121-3; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-12027160, EBI-22310682;
CC Q9P121-3; P32242: OTX1; NbExp=3; IntAct=EBI-12027160, EBI-740446;
CC Q9P121-3; P07237: P4HB; NbExp=3; IntAct=EBI-12027160, EBI-395883;
CC Q9P121-3; Q3KNR5: PAX4; NbExp=3; IntAct=EBI-12027160, EBI-10240813;
CC Q9P121-3; Q96P65: QRFPR; NbExp=3; IntAct=EBI-12027160, EBI-12820497;
CC Q9P121-3; O43609: SPRY1; NbExp=3; IntAct=EBI-12027160, EBI-3866665;
CC Q9P121-3; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-12027160, EBI-11957238;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9P121-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P121-2; Sequence=VSP_010939;
CC Name=3;
CC IsoId=Q9P121-3; Sequence=VSP_010940, VSP_010941;
CC Name=4;
CC IsoId=Q9P121-4; Sequence=VSP_041165;
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON family.
CC {ECO:0000305}.
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DR EMBL; AF126426; AAF37591.1; -; mRNA.
DR EMBL; EF043567; ABK34282.1; -; mRNA.
DR EMBL; AY358331; AAQ88697.1; -; mRNA.
DR EMBL; BC050716; AAH50716.1; -; mRNA.
DR CCDS; CCDS41733.1; -. [Q9P121-2]
DR CCDS; CCDS44777.1; -. [Q9P121-4]
DR CCDS; CCDS44778.1; -. [Q9P121-3]
DR CCDS; CCDS8491.1; -. [Q9P121-1]
DR RefSeq; NP_001041674.1; NM_001048209.1. [Q9P121-2]
DR RefSeq; NP_001137530.1; NM_001144058.1. [Q9P121-4]
DR RefSeq; NP_001137531.1; NM_001144059.1. [Q9P121-3]
DR RefSeq; NP_057606.1; NM_016522.2. [Q9P121-1]
DR PDB; 6DLF; X-ray; 3.45 A; A/B=34-322.
DR PDBsum; 6DLF; -.
DR AlphaFoldDB; Q9P121; -.
DR SMR; Q9P121; -.
DR BioGRID; 119163; 33.
DR IntAct; Q9P121; 28.
DR MINT; Q9P121; -.
DR STRING; 9606.ENSP00000396722; -.
DR GlyGen; Q9P121; 7 sites.
DR iPTMnet; Q9P121; -.
DR PhosphoSitePlus; Q9P121; -.
DR BioMuta; NTM; -.
DR DMDM; 27151645; -.
DR EPD; Q9P121; -.
DR jPOST; Q9P121; -.
DR MassIVE; Q9P121; -.
DR MaxQB; Q9P121; -.
DR PaxDb; Q9P121; -.
DR PeptideAtlas; Q9P121; -.
DR PRIDE; Q9P121; -.
DR ProteomicsDB; 83631; -. [Q9P121-1]
DR ProteomicsDB; 83632; -. [Q9P121-2]
DR ProteomicsDB; 83633; -. [Q9P121-3]
DR ProteomicsDB; 83634; -. [Q9P121-4]
DR Antibodypedia; 33124; 218 antibodies from 31 providers.
DR DNASU; 50863; -.
DR Ensembl; ENST00000374784.5; ENSP00000363916.1; ENSG00000182667.15. [Q9P121-3]
DR Ensembl; ENST00000374786.5; ENSP00000363918.1; ENSG00000182667.15. [Q9P121-1]
DR Ensembl; ENST00000374791.7; ENSP00000363923.3; ENSG00000182667.15. [Q9P121-2]
DR Ensembl; ENST00000425719.6; ENSP00000396722.2; ENSG00000182667.15. [Q9P121-4]
DR GeneID; 50863; -.
DR KEGG; hsa:50863; -.
DR UCSC; uc001qgm.4; human. [Q9P121-1]
DR CTD; 50863; -.
DR DisGeNET; 50863; -.
DR GeneCards; NTM; -.
DR HGNC; HGNC:17941; NTM.
DR HPA; ENSG00000182667; Tissue enhanced (brain, choroid plexus, retina).
DR MIM; 607938; gene.
DR neXtProt; NX_Q9P121; -.
DR OpenTargets; ENSG00000182667; -.
DR PharmGKB; PA164724212; -.
DR VEuPathDB; HostDB:ENSG00000182667; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000158679; -.
DR HOGENOM; CLU_027228_2_2_1; -.
DR InParanoid; Q9P121; -.
DR OMA; RPDFEWY; -.
DR OrthoDB; 583722at2759; -.
DR PhylomeDB; Q9P121; -.
DR TreeFam; TF325565; -.
DR PathwayCommons; Q9P121; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; Q9P121; -.
DR BioGRID-ORCS; 50863; 15 hits in 1064 CRISPR screens.
DR ChiTaRS; NTM; human.
DR GeneWiki; HNT; -.
DR GenomeRNAi; 50863; -.
DR Pharos; Q9P121; Tbio.
DR PRO; PR:Q9P121; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9P121; protein.
DR Bgee; ENSG00000182667; Expressed in right hemisphere of cerebellum and 160 other tissues.
DR ExpressionAtlas; Q9P121; baseline and differential.
DR Genevisible; Q9P121; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0007155; P:cell adhesion; NAS:ProtInc.
DR GO; GO:0008038; P:neuron recognition; TAS:ProtInc.
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 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 34..321
FT /note="Neurotrimin"
FT /id="PRO_0000015110"
FT PROPEP 322..344
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000015111"
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 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"
FT VAR_SEQ 1..27
FT /note="MGVCGYLFLPWKCLVVVSLRLLFLVPT -> MKTIQPKMHNSISWAIFTGLA
FT ALCLFQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_010939"
FT VAR_SEQ 311
FT /note="F -> FEVKTTALTPWK (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_041165"
FT VAR_SEQ 313..316
FT /note="PGAV -> ETVL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_010940"
FT VAR_SEQ 317..344
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_010941"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:6DLF"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 111..117
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 125..141
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:6DLF"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 211..225
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 252..256
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:6DLF"
FT STRAND 303..309
FT /evidence="ECO:0007829|PDB:6DLF"
SQ SEQUENCE 344 AA; 37971 MW; DA4D12C295ABBE3A CRC64;
MGVCGYLFLP WKCLVVVSLR LLFLVPTGVP VRSGDATFPK AMDNVTVRQG ESATLRCTID
NRVTRVAWLN RSTILYAGND KWCLDPRVVL LSNTQTQYSI EIQNVDVYDE GPYTCSVQTD
NHPKTSRVHL IVQVSPKIVE ISSDISINEG NNISLTCIAT GRPEPTVTWR HISPKAVGFV
SEDEYLEIQG ITREQSGDYE CSASNDVAAP VVRRVKVTVN YPPYISEAKG TGVPVGQKGT
LQCEASAVPS AEFQWYKDDK RLIEGKKGVK VENRPFLSKL IFFNVSEHDY GNYTCVASNK
LGHTNASIML FGPGAVSEVS NGTSRRAGCV WLLPLLVLHL LLKF
