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LY6H_MOUSE
ID   LY6H_MOUSE              Reviewed;         139 AA.
AC   Q9WUC3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Lymphocyte antigen 6H;
DE            Short=Ly-6H;
DE   Flags: Precursor;
GN   Name=Ly6h;
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 [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=10501842; DOI=10.1007/s002510050583;
RA   Apostolopoulos J., Chisholm L.J., Sandrin M.S.;
RT   "Identification of mouse Ly6H and its expression in normal tissue.";
RL   Immunogenetics 49:987-990(1999).
RN   [2]
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).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH CHRNA4.
RX   PubMed=26276394; DOI=10.1074/jbc.m115.647248;
RA   Wu M., Puddifoot C.A., Taylor P., Joiner W.J.;
RT   "Mechanisms of inhibition and potentiation of alpha4beta2 nicotinic
RT   acetylcholine receptors by members of the Ly6 protein family.";
RL   J. Biol. Chem. 290:24509-24518(2015).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH CHRNA7.
RX   PubMed=25716842; DOI=10.1523/jneurosci.3630-14.2015;
RA   Puddifoot C.A., Wu M., Sung R.J., Joiner W.J.;
RT   "Ly6h regulates trafficking of alpha7 nicotinic acetylcholine receptors and
RT   nicotine-induced potentiation of glutamatergic signaling.";
RL   J. Neurosci. 35:3420-3430(2015).
CC   -!- FUNCTION: Believed to act as modulator of nicotinic acetylcholine
CC       receptors (nAChRs) activity. In vitro inhibits alpha-3:beta-4-
CC       containing nAChRs maximum response. In vitro inhibits alpha-3:beta-4-
CC       containing nAChRs maximum response (PubMed:26276394). May play a role
CC       in the intracellular trafficking of alpha-7-containing nAChRs and may
CC       inhibit their expression at the cell surface (PubMed:25716842). Seems
CC       to inhibit alpha-7/CHRNA7 signaling in hippocampal neurons (By
CC       similarity). {ECO:0000250|UniProtKB:F1LNW6,
CC       ECO:0000269|PubMed:25716842, ECO:0000269|PubMed:26276394}.
CC   -!- SUBUNIT: Interacts with CHRNA4 and CHRNA7.
CC       {ECO:0000269|PubMed:25716842, ECO:0000269|PubMed:26276394}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in brain, also found in lower
CC       levels in eye and reproductive tissues.
CC   -!- DEVELOPMENTAL STAGE: Expression increases during embryonic development.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD28600.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF127091; AAD28600.1; ALT_INIT; mRNA.
DR   CCDS; CCDS49640.1; -.
DR   RefSeq; NP_001129160.1; NM_001135688.1.
DR   RefSeq; NP_001129161.1; NM_001135689.1.
DR   RefSeq; NP_035967.1; NM_011837.3.
DR   RefSeq; XP_006520962.1; XM_006520899.1.
DR   RefSeq; XP_006520963.1; XM_006520900.2.
DR   RefSeq; XP_006520964.1; XM_006520901.2.
DR   RefSeq; XP_011243908.1; XM_011245606.2.
DR   AlphaFoldDB; Q9WUC3; -.
DR   BioGRID; 204802; 1.
DR   IntAct; Q9WUC3; 1.
DR   STRING; 10090.ENSMUSP00000122061; -.
DR   GlyGen; Q9WUC3; 1 site.
DR   PhosphoSitePlus; Q9WUC3; -.
DR   MaxQB; Q9WUC3; -.
DR   PaxDb; Q9WUC3; -.
DR   PRIDE; Q9WUC3; -.
DR   ProteomicsDB; 290198; -.
DR   Antibodypedia; 27844; 74 antibodies from 16 providers.
DR   DNASU; 23934; -.
DR   Ensembl; ENSMUST00000023241; ENSMUSP00000023241; ENSMUSG00000022577.
DR   Ensembl; ENSMUST00000065417; ENSMUSP00000070646; ENSMUSG00000022577.
DR   Ensembl; ENSMUST00000126129; ENSMUSP00000121951; ENSMUSG00000022577.
DR   Ensembl; ENSMUST00000163116; ENSMUSP00000130781; ENSMUSG00000022577.
DR   GeneID; 23934; -.
DR   KEGG; mmu:23934; -.
DR   UCSC; uc011zuk.1; mouse.
DR   CTD; 4062; -.
DR   MGI; MGI:1346030; Ly6h.
DR   VEuPathDB; HostDB:ENSMUSG00000022577; -.
DR   eggNOG; ENOG502RVP9; Eukaryota.
DR   GeneTree; ENSGT00940000154560; -.
DR   HOGENOM; CLU_106772_1_1_1; -.
DR   InParanoid; Q9WUC3; -.
DR   OMA; DVECCEK; -.
DR   OrthoDB; 1482771at2759; -.
DR   Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   BioGRID-ORCS; 23934; 1 hit in 73 CRISPR screens.
DR   PRO; PR:Q9WUC3; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q9WUC3; protein.
DR   Bgee; ENSMUSG00000022577; Expressed in subiculum and 159 other tissues.
DR   ExpressionAtlas; Q9WUC3; baseline and differential.
DR   Genevisible; Q9WUC3; MM.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0033130; F:acetylcholine receptor binding; IDA:MGI.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IDA:MGI.
DR   GO; GO:0095500; P:acetylcholine receptor signaling pathway; IDA:MGI.
DR   CDD; cd00117; LU; 1.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR016054; LY6_UPA_recep-like.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   Pfam; PF00021; UPAR_LY6; 1.
DR   SMART; SM00134; LU; 1.
DR   SUPFAM; SSF57302; SSF57302; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; GPI-anchor; Lipoprotein;
KW   Membrane; Reference proteome; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..110
FT                   /note="Lymphocyte antigen 6H"
FT                   /id="PRO_0000036150"
FT   PROPEP          111..139
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000036151"
FT   DOMAIN          26..113
FT                   /note="UPAR/Ly6"
FT   LIPID           110
FT                   /note="GPI-anchor amidated asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..51
FT                   /evidence="ECO:0000250|UniProtKB:P0DP57,
FT                   ECO:0000250|UniProtKB:P0DP58"
FT   DISULFID        31..39
FT                   /evidence="ECO:0000250|UniProtKB:P0DP57,
FT                   ECO:0000250|UniProtKB:P0DP58"
FT   DISULFID        44..72
FT                   /evidence="ECO:0000250|UniProtKB:P0DP57,
FT                   ECO:0000250|UniProtKB:P0DP58"
FT   DISULFID        76..103
FT                   /evidence="ECO:0000250|UniProtKB:P0DP57,
FT                   ECO:0000250|UniProtKB:P0DP58"
FT   DISULFID        104..109
FT                   /evidence="ECO:0000250|UniProtKB:P0DP57,
FT                   ECO:0000250|UniProtKB:P0DP58"
SQ   SEQUENCE   139 AA;  14669 MW;  FDEEC13591EF219C CRC64;
     MLPAAMKSLG LALLALLLCP SPAHGLWCQD CTLANSSHCA PKQCQPTDTV CASVRITDPS
     SSRKDHSVNK MCASSCDFVK RHFFSDYLMG FINSGILKVD VDCCEKDLCN GASVAGRSPW
     ALAGGLLLSL GPALLWAGP
 
 
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