CEPU1_CHICK
ID CEPU1_CHICK Reviewed; 353 AA.
AC Q90773;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Protein CEPU-1;
DE Flags: Precursor;
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).
RC TISSUE=Brain;
RX PubMed=8774445; DOI=10.1523/jneurosci.16-05-01770.1996;
RA Spaltmann F., Bruemmendorf T.;
RT "CEPU-1, a novel immunoglobulin superfamily molecule, is expressed by
RT developing cerebellar Purkinje cells.";
RL J. Neurosci. 16:1770-1779(1996).
RN [2]
RP INTERACTION WITH NEGR1.
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: It may be a cellular address molecule specific to Purkinje
CC cells. It may represent a receptor or a subunit of a receptor complex.
CC -!- SUBUNIT: Interacts with NEGR1. {ECO:0000269|PubMed:10330412}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Minor;
CC IsoId=Q90773-1; Sequence=Displayed;
CC Name=2; Synonyms=Major;
CC IsoId=Q90773-2; Sequence=VSP_002607;
CC -!- TISSUE SPECIFICITY: Found on the dendrites, somata and axons of
CC developing Purkinje cells. Undetectable on other neurons like Golgi or
CC granule cells.
CC -!- DEVELOPMENTAL STAGE: Expressed by developing cerebellar Purkinje cells.
CC Expression coincides with the growth of the dendritic tree, after
CC Purkinje cells have finished their migration from the ventricular zone
CC (from E15 until E21). Expressed in the adult.
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; Z72497; CAA96578.1; -; mRNA.
DR RefSeq; NP_990042.1; NM_204711.1. [Q90773-1]
DR AlphaFoldDB; Q90773; -.
DR SMR; Q90773; -.
DR STRING; 9031.ENSGALP00000002185; -.
DR PaxDb; Q90773; -.
DR GeneID; 395450; -.
DR KEGG; gga:395450; -.
DR CTD; 50863; -.
DR VEuPathDB; HostDB:geneid_395450; -.
DR eggNOG; KOG3510; Eukaryota.
DR PhylomeDB; Q90773; -.
DR PRO; PR:Q90773; -.
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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..330
FT /note="Protein CEPU-1"
FT /id="PRO_0000015061"
FT PROPEP 331..353
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000015062"
FT DOMAIN 37..124
FT /note="Ig-like C2-type 1"
FT DOMAIN 134..216
FT /note="Ig-like C2-type 2"
FT DOMAIN 220..314
FT /note="Ig-like C2-type 3"
FT LIPID 330
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 55..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 155..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 241..293
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 310..320
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8774445"
FT /id="VSP_002607"
SQ SEQUENCE 353 AA; 38736 MW; 2550C48591EBBBA6 CRC64;
MAQAKMQHPV SWVIFAGMAA LLLFQGVPVR SGDATFPKAM DNVTVRQGES ATLRCSVDNR
VTRVAWLNRS SILYAGNDKW CLDPRVVLLA NTKTQYSIQI HDVDVYDEGP YTCSVQTDNH
PKTSRVHLIV QVSPKITETS SDISINEGGN VSLTCIATGR PDPTITWRHI SPKAVGFISE
DEYLEITGIT REQSGEYECS ASNDVAAPVV QRVKVTVNYP PYISDAKSTG VPVGQKGILM
CEASAVPSAD FQWYKDDKRL AEGQKGLKVE NKAFFSRLTF FNVSEQDYGN YTCVASNQLG
NTNASMILYE ETTTALTPWK GPGAVHDGNS GAWRRGSCAW LLALPLAQLA RQF
