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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}.
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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
 
 
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