NEGR1_CHICK
ID NEGR1_CHICK Reviewed; 352 AA.
AC Q9W6V2; Q9W6V1;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Neuronal growth regulator 1;
DE AltName: Full=Neurotractin;
DE Flags: Precursor;
GN Name=NEGR1; Synonyms=NTRA;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, GLYCOSYLATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH CEPU-1 AND LAMP.
RC TISSUE=Embryonic brain;
RX PubMed=10330412; DOI=10.1083/jcb.145.4.865;
RA Marg A., Sirim P., Spaltmann F., Plagge A., Kauselmann G., Buck F.,
RA Rathjen F.G., Bruemmendorf T.;
RT "Neurotractin, a novel neurite outgrowth-promoting Ig-like protein that
RT interacts with CEPU-1 and LAMP.";
RL J. Cell Biol. 145:865-876(1999).
CC -!- FUNCTION: May be involved in cell-adhesion. May participate in the
CC regulation of neurite outgrowth in the developing brain.
CC {ECO:0000269|PubMed:10330412}.
CC -!- SUBUNIT: Interacts with CEPU-1 and LAMP. {ECO:0000269|PubMed:10330412}.
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; Synonyms=Neurotractin-L, NTRA-L;
CC IsoId=Q9W6V2-1; Sequence=Displayed;
CC Name=2; Synonyms=Neurotractin-S, NTRA-S;
CC IsoId=Q9W6V2-2; Sequence=VSP_017295;
CC -!- TISSUE SPECIFICITY: Expressed in embryonic retina, telencephalon,
CC tectum, cerebellum and diencephalon (at protein level).
CC {ECO:0000269|PubMed:10330412}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:10330412}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON family.
CC {ECO:0000305}.
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DR EMBL; AJ132998; CAB44445.1; -; mRNA.
DR EMBL; AJ132999; CAB44446.1; -; mRNA.
DR RefSeq; NP_990187.1; NM_204856.1. [Q9W6V2-1]
DR AlphaFoldDB; Q9W6V2; -.
DR SMR; Q9W6V2; -.
DR STRING; 9031.ENSGALP00000018497; -.
DR PaxDb; Q9W6V2; -.
DR GeneID; 395662; -.
DR KEGG; gga:395662; -.
DR CTD; 257194; -.
DR VEuPathDB; HostDB:geneid_395662; -.
DR eggNOG; KOG3510; Eukaryota.
DR HOGENOM; CLU_027228_2_2_1; -.
DR InParanoid; Q9W6V2; -.
DR OrthoDB; 583722at2759; -.
DR PhylomeDB; Q9W6V2; -.
DR PRO; PR:Q9W6V2; -.
DR Proteomes; UP000000539; 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 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000250"
FT CHAIN 36..322
FT /note="Neuronal growth regulator 1"
FT /id="PRO_0000223873"
FT PROPEP 323..352
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000223874"
FT DOMAIN 36..132
FT /note="Ig-like C2-type 1"
FT DOMAIN 137..219
FT /note="Ig-like C2-type 2"
FT DOMAIN 223..311
FT /note="Ig-like C2-type 3"
FT LIPID 322
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
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 DISULFID 58..116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 158..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 243..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 221..311
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10330412"
FT /id="VSP_017295"
FT CONFLICT 190
FT /note="G -> V (in Ref. 1; CAB44445)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="P -> S (in Ref. 1; CAB44445)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 37944 MW; B0FA99F295FD8FA0 CRC64;
MVPLVRGAGG SHQWLAAVLL GLCCLLPAGR LAAPGGDFPG AAADSLVVRK GDTAVLRCYL
EDGASKGAWL NRSSIIFAGS DKWSVDPRVS IATANRREYS LQIQDVDVTD DGPYTCSVQT
QHTPRTMQVH LTVQVSPKIF RISSDIVVNE GSNVTLVCLA TGKPEPSISW RHISPSAKPF
ESGQYLDIYG ITRDQAGEYE CSAENDVSVP DVKKVKVTVN FAPTIQELKS SGVMLGGNGL
IRCEGAGVPA PVFEWYRGER KLISGQQGIT IKNYSTRSLL TVTNVTEEHF GNYTCVAANK
LGMTNASLPL NPPSTAQYGI TGDAEVLFSC WYLVLTLSSL TSIFYLKNII LH
