NEGR1_HUMAN
ID NEGR1_HUMAN Reviewed; 354 AA.
AC Q7Z3B1; Q5VT21; Q6UY06; Q8N440; Q8NAQ3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Neuronal growth regulator 1;
DE AltName: Full=IgLON family member 4;
DE Flags: Precursor;
GN Name=NEGR1; Synonyms=IGLON4; ORFNames=UNQ2433/PRO4993;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17566972; DOI=10.1002/pmic.200700068;
RA Omaetxebarria M.J., Elortza F., Rodriguez-Suarez E., Aloria K.,
RA Arizmendi J.M., Jensen O.N., Matthiesen R.;
RT "Computational approach for identification and characterization of GPI-
RT anchored peptides in proteomics experiments.";
RL Proteomics 7:1951-1960(2007).
CC -!- FUNCTION: May be involved in cell-adhesion. May function as a trans-
CC neural growth-promoting factor in regenerative axon sprouting in the
CC mammalian brain (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q7Z3B1; Q13449: LSAMP; NbExp=2; IntAct=EBI-4314838, EBI-4314821;
CC Q7Z3B1; P61916: NPC2; NbExp=9; IntAct=EBI-4314838, EBI-2368946;
CC Q7Z3B1; Q9P121: NTM; NbExp=2; IntAct=EBI-4314838, EBI-4315078;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC anchor {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7Z3B1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z3B1-2; Sequence=VSP_056313;
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ88499.1; Type=Erroneous initiation; Evidence={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; BX538014; CAD97961.1; -; mRNA.
DR EMBL; AY358132; AAQ88499.1; ALT_INIT; mRNA.
DR EMBL; AK092307; BAC03858.1; -; mRNA.
DR EMBL; AL359821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL354949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356600; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL391239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036771; AAH36771.1; -; mRNA.
DR CCDS; CCDS661.1; -. [Q7Z3B1-1]
DR RefSeq; NP_776169.2; NM_173808.2. [Q7Z3B1-1]
DR PDB; 6DLD; X-ray; 3.30 A; B/D=38-324.
DR PDB; 6U6T; X-ray; 3.01 A; A/B=38-313.
DR PDBsum; 6DLD; -.
DR PDBsum; 6U6T; -.
DR AlphaFoldDB; Q7Z3B1; -.
DR SMR; Q7Z3B1; -.
DR BioGRID; 129205; 8.
DR IntAct; Q7Z3B1; 4.
DR STRING; 9606.ENSP00000350364; -.
DR GlyGen; Q7Z3B1; 6 sites.
DR iPTMnet; Q7Z3B1; -.
DR PhosphoSitePlus; Q7Z3B1; -.
DR BioMuta; NEGR1; -.
DR DMDM; 88984537; -.
DR EPD; Q7Z3B1; -.
DR jPOST; Q7Z3B1; -.
DR MassIVE; Q7Z3B1; -.
DR MaxQB; Q7Z3B1; -.
DR PaxDb; Q7Z3B1; -.
DR PeptideAtlas; Q7Z3B1; -.
DR PRIDE; Q7Z3B1; -.
DR ProteomicsDB; 69021; -. [Q7Z3B1-1]
DR ProteomicsDB; 71878; -.
DR Antibodypedia; 2206; 203 antibodies from 29 providers.
DR DNASU; 257194; -.
DR Ensembl; ENST00000306821.3; ENSP00000305938.3; ENSG00000172260.15. [Q7Z3B1-2]
DR Ensembl; ENST00000357731.10; ENSP00000350364.4; ENSG00000172260.15. [Q7Z3B1-1]
DR GeneID; 257194; -.
DR KEGG; hsa:257194; -.
DR MANE-Select; ENST00000357731.10; ENSP00000350364.4; NM_173808.3; NP_776169.2.
DR UCSC; uc001dfv.4; human. [Q7Z3B1-1]
DR CTD; 257194; -.
DR DisGeNET; 257194; -.
DR GeneCards; NEGR1; -.
DR HGNC; HGNC:17302; NEGR1.
DR HPA; ENSG00000172260; Tissue enhanced (retina).
DR MIM; 613173; gene.
DR neXtProt; NX_Q7Z3B1; -.
DR OpenTargets; ENSG00000172260; -.
DR PharmGKB; PA134862452; -.
DR VEuPathDB; HostDB:ENSG00000172260; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000159289; -.
DR HOGENOM; CLU_027228_2_3_1; -.
DR InParanoid; Q7Z3B1; -.
DR OMA; CLAISME; -.
DR OrthoDB; 583722at2759; -.
DR PhylomeDB; Q7Z3B1; -.
DR TreeFam; TF351104; -.
DR PathwayCommons; Q7Z3B1; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; Q7Z3B1; -.
DR BioGRID-ORCS; 257194; 13 hits in 1063 CRISPR screens.
DR ChiTaRS; NEGR1; human.
DR GeneWiki; NEGR1; -.
DR GenomeRNAi; 257194; -.
DR Pharos; Q7Z3B1; Tbio.
DR PRO; PR:Q7Z3B1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q7Z3B1; protein.
DR Bgee; ENSG00000172260; Expressed in Brodmann (1909) area 46 and 174 other tissues.
DR Genevisible; Q7Z3B1; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0007631; P:feeding behavior; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0051963; P:regulation of synapse assembly; IEA:Ensembl.
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 Disulfide bond; Glycoprotein; GPI-anchor; Immunoglobulin domain;
KW Lipoprotein; Membrane; Phosphoprotein; Reference proteome; Repeat; Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000250"
FT CHAIN 38..324
FT /note="Neuronal growth regulator 1"
FT /id="PRO_0000015037"
FT PROPEP 325..354
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000015038"
FT DOMAIN 38..134
FT /note="Ig-like C2-type 1"
FT DOMAIN 139..221
FT /note="Ig-like C2-type 2"
FT DOMAIN 225..313
FT /note="Ig-like C2-type 3"
FT MOD_RES 187
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80Z24"
FT LIPID 324
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 60..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 160..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 245..297
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..128
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056313"
FT CONFLICT 169
FT /note="S -> F (in Ref. 3; BAC03858)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="D -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:6U6T"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 156..166
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 169..178
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 184..192
FT /evidence="ECO:0007829|PDB:6U6T"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 213..232
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 241..251
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 254..259
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6DLD"
FT STRAND 271..275
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 277..286
FT /evidence="ECO:0007829|PDB:6U6T"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:6U6T"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:6U6T"
SQ SEQUENCE 354 AA; 38719 MW; 41B05D00224CF34A CRC64;
MDMMLLVQGA CCSNQWLAAV LLSLCCLLPS CLPAGQSVDF PWAAVDNMMV RKGDTAVLRC
YLEDGASKGA WLNRSSIIFA GGDKWSVDPR VSISTLNKRD YSLQIQNVDV TDDGPYTCSV
QTQHTPRTMQ VHLTVQVPPK IYDISNDMTV NEGTNVTLTC LATGKPEPSI SWRHISPSAK
PFENGQYLDI YGITRDQAGE YECSAENDVS FPDVRKVKVV VNFAPTIQEI KSGTVTPGRS
GLIRCEGAGV PPPAFEWYKG EKKLFNGQQG IIIQNFSTRS ILTVTNVTQE HFGNYTCVAA
NKLGTTNASL PLNPPSTAQY GITGSADVLF SCWYLVLTLS SFTSIFYLKN AILQ