ID   NEGR1_PONAB             Reviewed;         354 AA.
AC   Q5R412; Q5R645;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Neuronal growth regulator 1;
DE   Flags: Precursor;
GN   Name=NEGR1;
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: 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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON family.
CC       {ECO:0000305}.
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DR   EMBL; CR860651; CAH92771.1; -; mRNA.
DR   EMBL; CR861448; CAH93504.1; -; mRNA.
DR   RefSeq; NP_001127049.1; NM_001133577.1.
DR   AlphaFoldDB; Q5R412; -.
DR   SMR; Q5R412; -.
DR   STRING; 9601.ENSPPYP00000001443; -.
DR   GeneID; 100174077; -.
DR   KEGG; pon:100174077; -.
DR   CTD; 257194; -.
DR   eggNOG; KOG3510; Eukaryota.
DR   InParanoid; Q5R412; -.
DR   OrthoDB; 583722at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Immunoglobulin domain; Lipoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000255"
FT   CHAIN           38..324
FT                   /note="Neuronal growth regulator 1"
FT                   /id="PRO_0000223871"
FT   PROPEP          325..354
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000223872"
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:0000250|UniProtKB:Q7Z3B1"
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   CONFLICT        205
FT                   /note="A -> T (in Ref. 1; CAH92771)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        242
FT                   /note="L -> V (in Ref. 1; CAH92771)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        282
FT                   /note="L -> F (in Ref. 1; CAH92771)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   354 AA;  38738 MW;  1F1C20E16583A9BD CRC64;
     MDMMLLVQGA CCSNQWLAAV LLSLCCLLPS CLPAGQSVDF PWAAVDNMMV RKGDTAVLRC
     YLEDGASKGA WLNRSSIIFA GGDKWSVDPR VSISTLNKRD YSLQIQNVDV TDDGPYTCSV
     QTQHTPRTMQ VHLTVQVPPK IYDISSDMTI NEGTNVTLTC LATGKPEPSI SWRHISPSAK
     PFENGQYLDI YGITRDQAGE YECSAENDVS FPDVRKVKVV VNFAPTIQEI KSGTMTPGRS
     GLIRCEGAGV PPPAFEWYKG EKKLFNGQQG IIIQNFSTRS ILTVTNVTQE HFGNYTCVAA
     NKLGTTNASL PLNPPSTAQY GITGSADVLF SCWYLVLTLS SFTSIFYLKN AILQ