LYNX1_MACMU
ID LYNX1_MACMU Reviewed; 118 AA.
AC P0DP62; F6VEA7; F6VEB6; F6VED0; P61050;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2017, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Ly-6/neurotoxin-like protein 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=LYNX1 {ECO:0000250|UniProtKB:Q9BZG9};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RX PubMed=15778850; DOI=10.1007/s00441-005-1077-9;
RA Sekhon H.S., Song P., Jia Y., Lindstrom J., Spindel E.R.;
RT "Expression of lynx1 in developing lung and its modulation by prenatal
RT nicotine exposure.";
RL Cell Tissue Res. 320:287-297(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus, and Testis;
RA Pandey S., Maudhoo M.D., Guda C., Ferguson B., Fox H., Norgren R.B.;
RT "De novo assembly of the rhesus macaque transcriptome from NextGen mRNA
RT sequences.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573;
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
CC -!- FUNCTION: Acts in different tissues through interaction to nicotinic
CC acetylcholine receptors (nAChRs). The proposed role as modulator of
CC nAChR activity seems to be dependent on the nAChR subtype and
CC stoichiometry, and to involve an effect on nAChR trafficking and its
CC cell surface expression, and on single channel properties of the nAChR
CC inserted in the plasma membrane.Modulates functional properties of
CC nicotinic acetylcholine receptors (nAChRs) to prevent excessive
CC excitation, and hence neurodegeneration. Enhances desensitization by
CC increasing both the rate and extent of desensitization of alpha-4:beta-
CC 2-containing nAChRs and slowing recovery from desensitization. Promotes
CC large amplitude ACh-evoked currents through alpha-4:beta-2 nAChRs. Is
CC involved in regulation of the nAChR pentameric assembly in the
CC endoplasmic reticulum. Shifts stoichiometry from high sensitivity
CC alpha-4(2):beta-2(3) to low sensitivity alpha-4(3):beta-2(2) nAChR. In
CC vitro modulates alpha-3:beta-4-containing nAChRs. Reduces cell surface
CC expression of (alpha-3:beta-4)(2):beta-4 and (alpha-3:beta-4)(2):alpha-
CC 5 nAChRs suggesting an interaction with nAChR alpha-3(-):(+)beta-4
CC subunit interfaces and an allosteric mode. Corresponding single channel
CC effects characterized by decreased unitary conductance, altered burst
CC proportions and enhanced desensitization/inactivation seem to depend on
CC nAChR alpha:alpha subunit interfaces and are greater in (alpha-3:beta-
CC 2)(2):alpha-3 when compared to (alpha-3:beta-2)(2):alpha-5 nAChRs.
CC Prevents plasticity in the primary visual cortex late in life.
CC {ECO:0000250|UniProtKB:P0DP58, ECO:0000250|UniProtKB:P0DP60}.
CC -!- SUBUNIT: Interacts with nAChRs containing alpha-4:beta-2
CC (CHRNA4:CHRNB2) and alpha-7 (CHRNA7) subunits. Interacts with CHRNA4
CC probably in the endoplasmic reticulum prior to nAChR pentameric
CC assembly. {ECO:0000250|UniProtKB:P0DP60}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P0DP60}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DP60}. Note=Detected in Purkinje cells soma
CC and proximal dendrites. {ECO:0000250|UniProtKB:P0DP60}.
CC -!- TISSUE SPECIFICITY: Expressed in lung predominantly in airway
CC epithelial cells, submucous glands, and smooth muscle cells, in
CC endothelial and smooth muscle cells in vessel walls and in alveolar
CC type II cells (at protein level). Also expressed in brain.
CC {ECO:0000269|PubMed:15778850}.
CC -!- DEVELOPMENTAL STAGE: Detected as early as day 71 of gestation.
CC Expression increases consistently in lungs throughout the prenatal
CC period. After birth, expression continues well into adulthood. At 71
CC days of gestation (pseudoglandular phase), expression is detected in
CC tracheal and proximal conducting airway epithelium. Expression
CC decreases gradually toward the distal airways. Strong expression in the
CC epithelium lining the tips of the dichotomous and monopodial airway
CC buds. Weakly expressed in smooth muscle cells around the large airways.
CC Weakly expressed in mesenchymal cells and not at all in the mesenchymal
CC cells surrounding the airway buds. Not detected in vessels associated
CC with large airways (at protein level). At 94 days of gestation, similar
CC expression pattern, but expression increases and extends toward distal
CC airway epithelium. Strong expression in type II cells that line the
CC primitive air spaces of late canalicular and early saccular phase. More
CC prominent expression in the smooth muscle cells surrounding the large
CC airways. Begins to be weakly expressed in endothelial and smooth muscle
CC cells in large vessels, but not in small distal vessels (at protein
CC level). At day 134 of gestation, further increase in expression in the
CC distal airway epithelium. In large airways, predominantly expressed in
CC the ciliated epithelium. Expressed at low levels in the mucus-secreting
CC cells and at high levels in the submucosal gland cells. Weakly
CC expressed in paracartilaginous cells, but not in cells in the extra-
CC cartilaginous layer. Not detected in type I alveolar cells. Strongly
CC expressed in endothelial and smooth muscle cells increased in large
CC vessels and in distal vessels (at protein level). At birth, similar
CC pattern of expression. Slightly decreased expression in the proximal
CC airways (at protein level). {ECO:0000269|PubMed:15778850}.
CC -!- INDUCTION: Up-regulated by prenatal nicotine exposure.
CC {ECO:0000269|PubMed:15778850}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EHH28801.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY422956; AAR00319.1; -; mRNA.
DR EMBL; JU336026; AFE79779.1; -; mRNA.
DR EMBL; JV047999; AFI38070.1; -; mRNA.
DR EMBL; CM001260; EHH28801.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_001028116.1; NM_001032944.1.
DR RefSeq; XP_015001580.1; XM_015146094.1.
DR RefSeq; XP_015001581.1; XM_015146095.1.
DR RefSeq; XP_015001582.1; XM_015146096.1.
DR AlphaFoldDB; P0DP62; -.
DR SMR; P0DP62; -.
DR STRING; 9544.ENSMMUP00000019650; -.
DR GeneID; 574359; -.
DR KEGG; mcc:574359; -.
DR CTD; 66004; -.
DR eggNOG; ENOG502T3MP; Eukaryota.
DR OMA; YTPYRMK; -.
DR OrthoDB; 1593386at2759; -.
DR Proteomes; UP000006718; Unplaced.
DR Proteomes; UP000013456; Chromosome 8.
DR GO; GO:0031225; C:anchored component of membrane; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0033130; F:acetylcholine receptor binding; ISS:UniProtKB.
DR GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IBA:GO_Central.
DR GO; GO:0030548; F:acetylcholine receptor regulator activity; ISS:UniProtKB.
DR GO; GO:0099601; P:regulation of neurotransmitter receptor activity; ISS:UniProtKB.
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 InterPro; IPR035076; Toxin/TOLIP.
DR Pfam; PF00087; Toxin_TOLIP; 1.
DR SMART; SM00134; LU; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..95
FT /note="Ly-6/neurotoxin-like protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000440675"
FT PROPEP 96..118
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000440642"
FT DOMAIN 23..107
FT /note="UPAR/Ly6"
FT /evidence="ECO:0000255"
FT LIPID 95
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT DISULFID 25..48
FT /evidence="ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 28..35
FT /evidence="ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 41..66
FT /evidence="ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 70..87
FT /evidence="ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 88..93
FT /evidence="ECO:0000250|UniProtKB:P0DP58"
FT CONFLICT 97
FT /note="G -> S (in Ref. 1; AAR00319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 118 AA; 12800 MW; 9C24103499AF19F6 CRC64;
MTPLLTLFLV VLMGLPLAPV QALDCHVCAY NGDNCFNPMR CPAMVAYCMT TRTYYTPTRM
KVSKSCVPSC FETVYDGYSK HASTTSCCQY DLCNSAGLAI PATLALAPVL LATLWGLL
