LSAMP_CHICK
ID LSAMP_CHICK Reviewed; 338 AA.
AC Q98919;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Limbic system-associated membrane protein;
DE AltName: Full=CHLAMP G19-isoform;
DE AltName: Full=E19S;
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].
RC TISSUE=Brain;
RX PubMed=9004047; DOI=10.1242/jcs.109.13.3129;
RA Wilson D.J.A., Kim D.-S., Clarke G.A., Marshall-Clarke S., Moss D.J.;
RT "A family of glycoproteins (GP55), which inhibit neurite outgrowth, are
RT members of the Ig superfamily and are related to OBCAM, neurotrimin, LAMP
RT and CEPU-1.";
RL J. Cell Sci. 109:3129-3138(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9215692; DOI=10.1111/j.1460-9568.1997.tb01463.x;
RA Brummendorf T., Spaltmann F., Treubert U.;
RT "Cloning and characterization of a neural cell recognition molecule on
RT axons of the retinotectal system and spinal cord.";
RL Eur. J. Neurosci. 9:1105-1116(1997).
CC -!- FUNCTION: Mediates selective neuronal growth and axon targeting.
CC Probably serves as a recognition molecule for the formation of limbic
CC connections (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}.
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; Y08171; CAA69357.1; -; mRNA.
DR EMBL; Z94720; CAB08115.1; -; mRNA.
DR RefSeq; NP_990205.1; NM_204874.1.
DR AlphaFoldDB; Q98919; -.
DR SMR; Q98919; -.
DR STRING; 9031.ENSGALP00000024292; -.
DR PaxDb; Q98919; -.
DR Ensembl; ENSGALT00000070123; ENSGALP00000058018; ENSGALG00000040620.
DR GeneID; 395687; -.
DR KEGG; gga:395687; -.
DR CTD; 4045; -.
DR VEuPathDB; HostDB:geneid_395687; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000158516; -.
DR HOGENOM; CLU_027228_2_3_1; -.
DR InParanoid; Q98919; -.
DR OMA; QCEAVAV; -.
DR OrthoDB; 583722at2759; -.
DR Reactome; R-GGA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:Q98919; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000040620; Expressed in cerebellum and 8 other tissues.
DR ExpressionAtlas; Q98919; baseline and differential.
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; Reference proteome; Repeat;
KW Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..315
FT /note="Limbic system-associated membrane protein"
FT /id="PRO_0000015100"
FT PROPEP 316..338
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000015101"
FT DOMAIN 29..122
FT /note="Ig-like C2-type 1"
FT DOMAIN 132..214
FT /note="Ig-like C2-type 2"
FT DOMAIN 219..306
FT /note="Ig-like C2-type 3"
FT LIPID 315
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 153..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 239..290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 338 AA; 37395 MW; 8FA4A60AD98426B4 CRC64;
MVARAQPDRK QLPLVLLRLL CLLPTGLPVR SVDFTRGTDN ITVRQGDTAI LRCFVEDRSS
KVAWLNRSGI IFAGEDKWSL DPRVELEKRS PLEYSLRIQK VDVYDEGSYT CSVQTQHHPK
TSQVYLIVQV PPKISNISSD ITVNEGSNVT LVCMANGRPE PVITWRHLTP TGKEFEGEEE
YLEILGITRE QSGKYECKAA NEVASADVKQ VRVTVNYPPT ITESKSNEAA TGRQALLRCE
ASAVPTPDFE WYRDDTRINS ANGLEIKSTG SQSLLMVANV TEEHYGNYTC VAANKLGVTN
ASLYLYRPGT GRVDNGSVSL AVPLWLLAAS LLCLLSKC
