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LYPD6_RAT
ID   LYPD6_RAT               Reviewed;         171 AA.
AC   D3ZTT2;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2013, sequence version 2.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Ly6/PLAUR domain-containing protein 6;
DE   Flags: Precursor;
GN   Name=Lypd6;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA   Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA   Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA   Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA   Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=27344019; DOI=10.1111/jnc.13718;
RA   Arvaniti M., Jensen M.M., Soni N., Wang H., Klein A.B., Thiriet N.,
RA   Pinborg L.H., Muldoon P.P., Wienecke J., Imad Damaj M., Kohlmeier K.A.,
RA   Gondre-Lewis M.C., Mikkelsen J.D., Thomsen M.S.;
RT   "Functional interaction between Lypd6 and nicotinic acetylcholine
RT   receptors.";
RL   J. Neurochem. 138:806-820(2016).
CC   -!- FUNCTION: Acts as a modulator of nicotinic acetylcholine receptors
CC       (nAChRs) function in the brain. Enhances nicotine-induced Ca(2+) influx
CC       through nAChRs (PubMed:27344019). Acts as a positive regulator of
CC       Wnt/beta-catenin signaling (By similarity).
CC       {ECO:0000250|UniProtKB:Q66IA6, ECO:0000269|PubMed:27344019}.
CC   -!- SUBUNIT: Interacts with nicotinic acetylcholine receptors (nAChRs)
CC       including CHRNA3, CHRNA4, CHRNA5, CHRNA6, CHRNA7, CHRNB2 and CHRNB4.
CC       {ECO:0000250|UniProtKB:Q86Y78}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q86Y78}.
CC       Cytoplasm {ECO:0000250|UniProtKB:Q86Y78}. Membrane
CC       {ECO:0000269|PubMed:27344019}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q66IA6}; Lipid-anchor, GPI-anchor
CC       {ECO:0000250|UniProtKB:Q66IA6}. Synapse, synaptosome
CC       {ECO:0000269|PubMed:27344019}. Membrane raft
CC       {ECO:0000250|UniProtKB:Q66IA6}.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in the cortex and
CC       cerebellum of the brain, at moderate levels in the lung, kidney, and
CC       liver, and at low levels in the heart and prostate (at protein level).
CC       {ECO:0000269|PubMed:27344019}.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed during early development, showing
CC       high levels in the first postnatal days, followed by a decrease toward
CC       adulthood. {ECO:0000269|PubMed:27344019}.
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DR   EMBL; AABR07052085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH473983; EDM00460.1; -; Genomic_DNA.
DR   EMBL; CH473983; EDM00461.1; -; Genomic_DNA.
DR   RefSeq; XP_001053512.3; XM_001053512.5.
DR   RefSeq; XP_003753769.1; XM_003753721.3.
DR   RefSeq; XP_006224472.1; XM_006224410.3.
DR   RefSeq; XP_006234222.1; XM_006234160.3.
DR   RefSeq; XP_008773595.1; XM_008775373.2.
DR   AlphaFoldDB; D3ZTT2; -.
DR   SMR; D3ZTT2; -.
DR   STRING; 10116.ENSRNOP00000056346; -.
DR   GlyGen; D3ZTT2; 2 sites.
DR   PaxDb; D3ZTT2; -.
DR   Ensembl; ENSRNOT00000095416; ENSRNOP00000096059; ENSRNOG00000068044.
DR   GeneID; 679564; -.
DR   KEGG; rno:679564; -.
DR   CTD; 130574; -.
DR   RGD; 1587119; Lypd6.
DR   eggNOG; ENOG502RYB5; Eukaryota.
DR   GeneTree; ENSGT00390000000220; -.
DR   HOGENOM; CLU_105474_1_0_1; -.
DR   InParanoid; D3ZTT2; -.
DR   OMA; AWPTVAW; -.
DR   OrthoDB; 1296179at2759; -.
DR   TreeFam; TF332443; -.
DR   PRO; PR:D3ZTT2; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Proteomes; UP000234681; Chromosome 3.
DR   Bgee; ENSRNOG00000038980; Expressed in frontal cortex and 10 other tissues.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0030548; F:acetylcholine receptor regulator activity; ISO:RGD.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR031574; LYPD6.
DR   InterPro; IPR039457; LYPD6-like.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   PANTHER; PTHR31171; PTHR31171; 1.
DR   PANTHER; PTHR31171:SF0; PTHR31171:SF0; 1.
DR   SUPFAM; SSF57302; SSF57302; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Glycoprotein; GPI-anchor; Lipoprotein; Membrane;
KW   Reference proteome; Secreted; Signal; Synapse; Synaptosome.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..171
FT                   /note="Ly6/PLAUR domain-containing protein 6"
FT                   /id="PRO_5008161185"
FT   DOMAIN          47..141
FT                   /note="UPAR/Ly6"
FT   CARBOHYD        134
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   171 AA;  19051 MW;  2AF886868A754674 CRC64;
     MEPSPALAWL LLLSLVADCL KAAQSRDFTV KDIIYLHPST TPYPGGFKCF TCEKAADNYE
     CNRWAPDIYC PRDTRYCYTQ HTMEVTGNSI SVTKRCVPLE ECLSTGCRDS EHEGYKICTS
     CCEGNICNLP LPRNDTDATF ATTSPINQTN GHPHCVSVIV SCLWVWLGLT L
 
 
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