LSAMP_MOUSE
ID LSAMP_MOUSE Reviewed; 341 AA.
AC Q8BLK3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Limbic system-associated membrane protein;
DE Short=LSAMP;
DE Flags: Precursor;
GN Name=Lsamp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PROTEIN SEQUENCE OF 101-120 AND 174-189, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (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; AK044845; BAC32117.1; -; mRNA.
DR RefSeq; NP_780757.1; NM_175548.3.
DR AlphaFoldDB; Q8BLK3; -.
DR SMR; Q8BLK3; -.
DR BioGRID; 234574; 4.
DR IntAct; Q8BLK3; 2.
DR MINT; Q8BLK3; -.
DR STRING; 10090.ENSMUSP00000077913; -.
DR GlyConnect; 2480; 4 N-Linked glycans (2 sites).
DR GlyGen; Q8BLK3; 7 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q8BLK3; -.
DR PhosphoSitePlus; Q8BLK3; -.
DR MaxQB; Q8BLK3; -.
DR PaxDb; Q8BLK3; -.
DR PRIDE; Q8BLK3; -.
DR ProteomicsDB; 293400; -.
DR Antibodypedia; 16507; 123 antibodies from 23 providers.
DR DNASU; 268890; -.
DR Ensembl; ENSMUST00000078873; ENSMUSP00000077913; ENSMUSG00000061080.
DR UCSC; uc007zfs.1; mouse.
DR MGI; MGI:1261760; Lsamp.
DR VEuPathDB; HostDB:ENSMUSG00000061080; -.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000158516; -.
DR InParanoid; Q8BLK3; -.
DR OrthoDB; 583722at2759; -.
DR PhylomeDB; Q8BLK3; -.
DR TreeFam; TF325565; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 268890; 0 hits in 58 CRISPR screens.
DR ChiTaRS; Lsamp; mouse.
DR PRO; PR:Q8BLK3; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BLK3; protein.
DR Bgee; ENSMUSG00000061080; Expressed in dentate gyrus of hippocampal formation granule cell and 161 other tissues.
DR ExpressionAtlas; Q8BLK3; baseline and differential.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; IMP:MGI.
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 Cell adhesion; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000250"
FT CHAIN 29..?
FT /note="Limbic system-associated membrane protein"
FT /id="PRO_0000015104"
FT PROPEP ?..341
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000015105"
FT DOMAIN 29..122
FT /note="Ig-like 1"
FT DOMAIN 132..214
FT /note="Ig-like 2"
FT DOMAIN 219..304
FT /note="Ig-like 3"
FT MOD_RES 94
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
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 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 341 AA; 38086 MW; 949CE792C67E25C3 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
ASLVLFSKYA KTEPDSMQVI EFLHIDLKSI RHPLKVNPIQ K
