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LSAMP_HUMAN
ID   LSAMP_HUMAN             Reviewed;         338 AA.
AC   Q13449; Q8IV49;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=Limbic system-associated membrane protein;
DE            Short=LSAMP;
DE   AltName: Full=IgLON family member 3;
DE   Flags: Precursor;
GN   Name=LSAMP; Synonyms=IGLON3, LAMP;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8666243; DOI=10.1016/0378-1119(96)84698-1;
RA   Pimenta A.F., Fischer I., Levitt P.;
RT   "cDNA cloning and structural analysis of the human limbic-system-associated
RT   membrane protein (LAMP).";
RL   Gene 170:189-195(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-300.
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [4]
RP   VARIANT GLU-225.
RX   PubMed=32383616; DOI=10.34172/aim.2020.21;
RA   Mehrjoo Z., Kahrizi K., Mohseni M., Akbari M., Arzhangi S., Jalalvand K.,
RA   Najmabadi H., Farhadi M., Mohseni M., Asghari A., Mohebbi S., Daneshi A.;
RT   "Limbic System Associated Membrane Protein Mutation in an Iranian Family
RT   Diagnosed with Meniere's Disease.";
RL   Arch. Iran. Med. 23:319-325(2020).
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   -!- INTERACTION:
CC       Q13449; Q14457: BECN1; NbExp=3; IntAct=EBI-4314821, EBI-949378;
CC       Q13449; Q9HCU0: CD248; NbExp=3; IntAct=EBI-4314821, EBI-9680942;
CC       Q13449; Q7Z7K6: CENPV; NbExp=3; IntAct=EBI-4314821, EBI-1210604;
CC       Q13449; Q14154: DELE1; NbExp=3; IntAct=EBI-4314821, EBI-2805660;
CC       Q13449; P41970: ELK3; NbExp=3; IntAct=EBI-4314821, EBI-1758534;
CC       Q13449; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-4314821, EBI-2868501;
CC       Q13449; Q13352: ITGB3BP; NbExp=3; IntAct=EBI-4314821, EBI-712105;
CC       Q13449; Q9BV99: LRRC61; NbExp=3; IntAct=EBI-4314821, EBI-2350424;
CC       Q13449; Q13503: MED21; NbExp=3; IntAct=EBI-4314821, EBI-394678;
CC       Q13449; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-4314821, EBI-8487781;
CC       Q13449; Q7Z3B1: NEGR1; NbExp=2; IntAct=EBI-4314821, EBI-4314838;
CC       Q13449; Q9P121: NTM; NbExp=2; IntAct=EBI-4314821, EBI-4315078;
CC       Q13449; Q9BR81: PCDHGC3; NbExp=3; IntAct=EBI-4314821, EBI-22012354;
CC       Q13449; Q6P1J6-2: PLB1; NbExp=3; IntAct=EBI-4314821, EBI-10694821;
CC       Q13449; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-4314821, EBI-358489;
CC       Q13449; Q92783-2: STAM; NbExp=3; IntAct=EBI-4314821, EBI-12025738;
CC       Q13449; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-4314821, EBI-17438286;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- TISSUE SPECIFICITY: Expressed on limbic neurons and fiber tracts as
CC       well as in single layers of the superior colliculus, spinal cord and
CC       cerebellum.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON family.
CC       {ECO:0000305}.
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DR   EMBL; U41901; AAC50569.1; -; mRNA.
DR   EMBL; BC033803; AAH33803.1; -; mRNA.
DR   CCDS; CCDS2982.1; -.
DR   PIR; JC4776; JC4776.
DR   RefSeq; NP_001305844.1; NM_001318915.1.
DR   RefSeq; NP_002329.2; NM_002338.4.
DR   AlphaFoldDB; Q13449; -.
DR   SMR; Q13449; -.
DR   BioGRID; 110223; 5.
DR   IntAct; Q13449; 20.
DR   STRING; 9606.ENSP00000419000; -.
DR   GlyGen; Q13449; 9 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q13449; -.
DR   PhosphoSitePlus; Q13449; -.
DR   BioMuta; LSAMP; -.
DR   DMDM; 116242621; -.
DR   EPD; Q13449; -.
DR   jPOST; Q13449; -.
DR   MassIVE; Q13449; -.
DR   MaxQB; Q13449; -.
DR   PaxDb; Q13449; -.
DR   PeptideAtlas; Q13449; -.
DR   PRIDE; Q13449; -.
DR   ProteomicsDB; 59454; -.
DR   Antibodypedia; 16507; 123 antibodies from 23 providers.
DR   DNASU; 4045; -.
DR   Ensembl; ENST00000490035.7; ENSP00000419000.1; ENSG00000185565.12.
DR   GeneID; 4045; -.
DR   KEGG; hsa:4045; -.
DR   MANE-Select; ENST00000490035.7; ENSP00000419000.1; NM_002338.5; NP_002329.2.
DR   UCSC; uc003ebs.4; human.
DR   CTD; 4045; -.
DR   DisGeNET; 4045; -.
DR   GeneCards; LSAMP; -.
DR   HGNC; HGNC:6705; LSAMP.
DR   HPA; ENSG00000185565; Tissue enhanced (brain, retina).
DR   MIM; 603241; gene.
DR   neXtProt; NX_Q13449; -.
DR   OpenTargets; ENSG00000185565; -.
DR   PharmGKB; PA30470; -.
DR   VEuPathDB; HostDB:ENSG00000185565; -.
DR   eggNOG; KOG3510; Eukaryota.
DR   GeneTree; ENSGT00940000158516; -.
DR   InParanoid; Q13449; -.
DR   OMA; QCEAVAV; -.
DR   OrthoDB; 583722at2759; -.
DR   PhylomeDB; Q13449; -.
DR   TreeFam; TF325565; -.
DR   PathwayCommons; Q13449; -.
DR   Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   SignaLink; Q13449; -.
DR   BioGRID-ORCS; 4045; 5 hits in 1062 CRISPR screens.
DR   ChiTaRS; LSAMP; human.
DR   GenomeRNAi; 4045; -.
DR   Pharos; Q13449; Tbio.
DR   PRO; PR:Q13449; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q13449; protein.
DR   Bgee; ENSG00000185565; Expressed in postcentral gyrus and 145 other tissues.
DR   ExpressionAtlas; Q13449; baseline and differential.
DR   Genevisible; Q13449; HS.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
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; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Immunoglobulin domain; Lipoprotein; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..315
FT                   /note="Limbic system-associated membrane protein"
FT                   /id="PRO_0000015102"
FT   PROPEP          316..338
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000015103"
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:0000269|PubMed:19349973"
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   VARIANT         225
FT                   /note="K -> E"
FT                   /evidence="ECO:0000269|PubMed:32383616"
FT                   /id="VAR_083713"
FT   CONFLICT        3
FT                   /note="R -> G (in Ref. 1; AAC50569)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55
FT                   /note="V -> L (in Ref. 1; AAC50569)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   338 AA;  37393 MW;  88CF00E07302817B CRC64;
     MVRRVQPDRK QLPLVLLRLL CLLPTGLPVR SVDFNRGTDN ITVRQGDTAI LRCVVEDKNS
     KVAWLNRSGI IFAGHDKWSL DPRVELEKRH SLEYSLRIQK VDVYDEGSYT CSVQTQHEPK
     TSQVYLIVQV PPKISNISSD VTVNEGSNVT LVCMANGRPE PVITWRHLTP TGREFEGEEE
     YLEILGITRE QSGKYECKAA NEVSSADVKQ VKVTVNYPPT ITESKSNEAT TGRQASLKCE
     ASAVPAPDFE WYRDDTRINS ANGLEIKSTE GQSSLTVTNV TEEHYGNYTC VAANKLGVTN
     ASLVLFRPGS VRGINGSISL AVPLWLLAAS LLCLLSKC
 
 
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