LPD6B_MOUSE
ID LPD6B_MOUSE Reviewed; 172 AA.
AC Q9D7F2; A0JNT6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Ly6/PLAUR domain-containing protein 6B;
DE Flags: Precursor;
GN Name=Lypd6b;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
CC -!- FUNCTION: Believed to act as a modulator of nicotinic acetylcholine
CC receptors (nAChRs) activity. In vitro acts on nAChRs in a subtype- and
CC stoichiometry-dependent manner. Modulates specifically alpha-3(3):beta-
CC 4(2) nAChRs by enhancing the sensitivity to ACh, decreasing ACh-induced
CC maximal current response and increasing the rate of desensitization to
CC ACh; has no effect on alpha-7 homomeric nAChRs.
CC {ECO:0000250|UniProtKB:Q8NI32}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q9D7F2-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q9D7F2-1; Sequence=VSP_060613;
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DR EMBL; AK009282; BAB26192.1; -; mRNA.
DR EMBL; BC126943; AAI26944.1; -; mRNA.
DR CCDS; CCDS16025.1; -. [Q9D7F2-2]
DR RefSeq; NP_082266.1; NM_027990.3. [Q9D7F2-2]
DR RefSeq; XP_006498413.1; XM_006498350.3. [Q9D7F2-1]
DR RefSeq; XP_006498414.1; XM_006498351.3. [Q9D7F2-1]
DR RefSeq; XP_006498415.1; XM_006498352.3. [Q9D7F2-1]
DR RefSeq; XP_006498416.1; XM_006498353.3. [Q9D7F2-1]
DR RefSeq; XP_006498417.1; XM_006498354.3. [Q9D7F2-1]
DR RefSeq; XP_006498418.1; XM_006498355.3.
DR RefSeq; XP_006498419.1; XM_006498356.3.
DR RefSeq; XP_006498420.1; XM_006498357.3.
DR RefSeq; XP_006498421.1; XM_006498358.3.
DR RefSeq; XP_006498422.1; XM_006498359.3. [Q9D7F2-2]
DR RefSeq; XP_017174756.1; XM_017319267.1. [Q9D7F2-1]
DR AlphaFoldDB; Q9D7F2; -.
DR SMR; Q9D7F2; -.
DR BioGRID; 215013; 1.
DR STRING; 10090.ENSMUSP00000028103; -.
DR PaxDb; Q9D7F2; -.
DR PRIDE; Q9D7F2; -.
DR ProteomicsDB; 291965; -. [Q9D7F2-2]
DR ProteomicsDB; 291966; -. [Q9D7F2-2]
DR Antibodypedia; 62112; 27 antibodies from 12 providers.
DR DNASU; 71897; -.
DR Ensembl; ENSMUST00000028103; ENSMUSP00000028103; ENSMUSG00000026765. [Q9D7F2-1]
DR GeneID; 71897; -.
DR KEGG; mmu:71897; -.
DR UCSC; uc008jpz.1; mouse. [Q9D7F2-2]
DR CTD; 130576; -.
DR MGI; MGI:1919147; Lypd6b.
DR VEuPathDB; HostDB:ENSMUSG00000026765; -.
DR eggNOG; ENOG502RXMG; Eukaryota.
DR GeneTree; ENSGT00390000000220; -.
DR HOGENOM; CLU_105474_0_0_1; -.
DR InParanoid; Q9D7F2; -.
DR OMA; DCNRWAE; -.
DR OrthoDB; 1296179at2759; -.
DR PhylomeDB; Q9D7F2; -.
DR TreeFam; TF332443; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 71897; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Lypd6b; mouse.
DR PRO; PR:Q9D7F2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9D7F2; protein.
DR Bgee; ENSMUSG00000026765; Expressed in renal medulla collecting duct and 163 other tissues.
DR Genevisible; Q9D7F2; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030548; F:acetylcholine receptor regulator activity; ISO:MGI.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR039457; LYPD6-like.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR PANTHER; PTHR31171; PTHR31171; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..148
FT /note="Ly6/PLAUR domain-containing protein 6B"
FT /id="PRO_0000321952"
FT PROPEP 149..172
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000321953"
FT DOMAIN 46..137
FT /note="UPAR/Ly6"
FT LIPID 148
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT DISULFID 48..76
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 51..60
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 69..95
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 101..120
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58"
FT DISULFID 121..126
FT /evidence="ECO:0000250|UniProtKB:P0DP57,
FT ECO:0000250|UniProtKB:P0DP58"
FT VAR_SEQ 1
FT /note="M -> MCSSFQRHTTLTCPIRVDRM (in isoform 1)"
FT /id="VSP_060613"
SQ SEQUENCE 172 AA; 19528 MW; 849BF46AE75B90B1 CRC64;
MLLLCHILAV TILQILIISE NWVFAKNINF YNVRPPLDPT PFPNSFKCFT CENAGDNYNC
NRWAEDKWCP QDTQYCLTVH HFTSHGRSTS ITKKCASKNE CHFVGCRHSR DSEHTECRSC
CEGMICNVEL PTNHTNAVFA VMHAQRTSGS SVSSVPSPYL LVLAWLFMLP LL
