LYNX1_BOVIN
ID LYNX1_BOVIN Reviewed; 116 AA.
AC Q1RMQ4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ly-6/neurotoxin-like protein 1 {ECO:0000305};
DE Flags: Precursor;
GN Name=LYNX1 {ECO:0000250|UniProtKB:Q9BZG9};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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:P0DP58}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P0DP60}. Note=Detected in Purkinje cells soma
CC and proximal dendrites. {ECO:0000250|UniProtKB:P0DP58}.
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DR EMBL; BC114776; AAI14777.1; -; mRNA.
DR RefSeq; NP_001039686.1; NM_001046221.2.
DR RefSeq; XP_005215253.1; XM_005215196.3.
DR AlphaFoldDB; Q1RMQ4; -.
DR SMR; Q1RMQ4; -.
DR STRING; 9913.ENSBTAP00000007573; -.
DR PaxDb; Q1RMQ4; -.
DR Ensembl; ENSBTAT00000007573; ENSBTAP00000007573; ENSBTAG00000005762.
DR Ensembl; ENSBTAT00000079415; ENSBTAP00000061449; ENSBTAG00000005762.
DR GeneID; 516158; -.
DR KEGG; bta:516158; -.
DR CTD; 66004; -.
DR VEuPathDB; HostDB:ENSBTAG00000005762; -.
DR VGNC; VGNC:108094; LYNX1.
DR eggNOG; ENOG502SD2S; Eukaryota.
DR GeneTree; ENSGT00730000111571; -.
DR HOGENOM; CLU_161471_0_1_1; -.
DR InParanoid; Q1RMQ4; -.
DR OMA; YTPYRMK; -.
DR OrthoDB; 1593386at2759; -.
DR TreeFam; TF336080; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000005762; Expressed in cardiac ventricle and 99 other tissues.
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:0045202; C:synapse; IEA:GOC.
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:0008200; F:ion channel inhibitor activity; IEA:Ensembl.
DR GO; GO:0099601; P:regulation of neurotransmitter receptor activity; ISS:UniProtKB.
DR GO; GO:0007271; P:synaptic transmission, cholinergic; IEA:Ensembl.
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 3: Inferred from homology;
KW Cell membrane; Cell projection; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; GPI-anchor; Lipoprotein; Membrane; Reference proteome;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..92
FT /note="Ly-6/neurotoxin-like protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000259349"
FT PROPEP 93..116
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000440640"
FT DOMAIN 21..105
FT /note="UPAR/Ly6"
FT /evidence="ECO:0000255"
FT LIPID 92
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 23..46
FT /evidence="ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 26..33
FT /evidence="ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 39..64
FT /evidence="ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 68..85
FT /evidence="ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 86..91
FT /evidence="ECO:0000250|UniProtKB:P0DP58"
SQ SEQUENCE 116 AA; 12552 MW; 35B09267D081199E CRC64;
MTPLLALFLV ALVGLPVAQA LDCHVCAYNG ENCFNPMRCP AMVSYCMTTR TYYTPTRMKV
SKSCVPSCFE TVYDGYSKHA STTSCCQYDL CNGAGLATPA TLALALILLA TLWGLF
