LSAMP_RAT
ID LSAMP_RAT Reviewed; 338 AA.
AC Q62813; Q6VUH9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Limbic system-associated membrane protein;
DE Short=LSAMP;
DE Flags: Precursor;
GN Name=Lsamp; Synonyms=Lamp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 29-49.
RC TISSUE=Hippocampus;
RX PubMed=7646886; DOI=10.1016/0896-6273(95)90034-9;
RA Pimenta A.F., Zhukareva V., Barbe M.F., Reinoso B.S., Grimley C.,
RA Henzel W., Fischer I., Levitt P.;
RT "The limbic system-associated membrane protein is an Ig superfamily member
RT that mediates selective neuronal growth and axon targeting.";
RL Neuron 15:287-297(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=Sprague-Dawley;
RX PubMed=15081109; DOI=10.1016/j.ygeno.2003.11.013;
RA Pimenta A.F., Levitt P.;
RT "Characterization of the genomic structure of the mouse limbic system-
RT associated membrane protein (Lsamp) gene.";
RL Genomics 83:790-801(2004).
RN [3]
RP PROTEIN SEQUENCE OF 78-83; 90-97; 167-189; 199-209 AND 213-225, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
CC -!- FUNCTION: Mediates selective neuronal growth and axon targeting.
CC Contributes to the guidance of developing axons and remodeling of
CC mature circuits in the limbic system. Essential for normal growth of
CC the hippocampal mossy fiber projection.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62813-1; Sequence=Displayed;
CC Name=2; Synonyms=6C;
CC IsoId=Q62813-2; Sequence=VSP_011601;
CC -!- TISSUE SPECIFICITY: Expressed mostly by neurons comprising limbic-
CC associated cortical and subcortical regions that function in cognition,
CC emotion, memory, and learning.
CC -!- DEVELOPMENTAL STAGE: First detected at E15-16, at stage E20 it is
CC detected in presumptive cortex, medial limbic areas of the thalamus and
CC hypothalamus. In the adult, it is found in hypothalamus, perirhinal
CC cortex, amygdala and medial thalamic region.
CC -!- MISCELLANEOUS: [Isoform 1]: GPI-anchored form.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON family.
CC {ECO:0000305}.
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DR EMBL; U31554; AAA86120.1; -; mRNA.
DR EMBL; AY326256; AAQ91613.1; -; mRNA.
DR RefSeq; NP_058938.1; NM_017242.1. [Q62813-1]
DR RefSeq; XP_006248401.1; XM_006248339.3. [Q62813-2]
DR AlphaFoldDB; Q62813; -.
DR SMR; Q62813; -.
DR BioGRID; 248195; 1.
DR IntAct; Q62813; 1.
DR MINT; Q62813; -.
DR STRING; 10116.ENSRNOP00000040165; -.
DR GlyGen; Q62813; 8 sites, 4 N-linked glycans (5 sites).
DR iPTMnet; Q62813; -.
DR PhosphoSitePlus; Q62813; -.
DR PRIDE; Q62813; -.
DR Ensembl; ENSRNOT00000047907; ENSRNOP00000040165; ENSRNOG00000031852. [Q62813-2]
DR Ensembl; ENSRNOT00000100246; ENSRNOP00000085583; ENSRNOG00000031852. [Q62813-1]
DR GeneID; 29561; -.
DR KEGG; rno:29561; -.
DR UCSC; RGD:71102; rat. [Q62813-1]
DR CTD; 4045; -.
DR RGD; 71102; Lsamp.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000158516; -.
DR HOGENOM; CLU_027228_2_1_1; -.
DR InParanoid; Q62813; -.
DR TreeFam; TF325565; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:Q62813; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Genevisible; Q62813; RN.
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 GO; GO:0035641; P:locomotory exploration behavior; ISO:RGD.
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;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW Immunoglobulin domain; Lipoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:7646886"
FT CHAIN 29..315
FT /note="Limbic system-associated membrane protein"
FT /id="PRO_0000015106"
FT PROPEP 316..338
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000015107"
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..304
FT /note="Ig-like C2-type 3"
FT MOD_RES 94
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BLK3"
FT LIPID 315
FT /note="GPI-anchor amidated asparagine; alternate"
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; alternate"
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"
FT VAR_SEQ 307
FT /note="R -> KRVLPTVPHPIQEIGTTVHFKQKG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15081109"
FT /id="VSP_011601"
SQ SEQUENCE 338 AA; 37324 MW; 0B76AFDD68A39BB6 CRC64;
MVGRVQPDRK QLPLVLLRLL CLLPTGLPVR SVDFNRGTDN ITVRQGDTAI LRCVVEDKNS
KVAWLNRSGI IFAGHDKWSL DPRVELEKRH ALEYSLRIQK VDVYDEGSYT CSVQTQHEPK
TSQVYLIVQV PPKISNISSD VTVNEGSNVT LVCMANGRPE PVITWRHLTP LGREFEGEEE
YLEILGITRE QSGKYECKAA NEVSSADVKQ VKVTVNYPPT ITESKSNEAT TGRQASLKCE
ASAVPAPDFE WYRDDTRINS ANGLEIKSTE GQSSLTVTNV TEEHYGNYTC VAANKLGVTN
ASLVLFRPGS VRGINGSISL AVPLWLLAAS LFCLLSKC
