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LAYN_MOUSE
ID   LAYN_MOUSE              Reviewed;         381 AA.
AC   Q8C351; E9QQ23; Q3TMU7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 4.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Layilin;
DE   Flags: Precursor;
GN   Name=Layn;
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 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-212 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Medulla oblongata;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   INTERACTION WITH NF2 AND RDX.
RX   PubMed=15913605; DOI=10.1016/j.yexcr.2005.04.017;
RA   Bono P., Cordero E., Johnson K., Borowsky M., Ramesh V., Jacks T.,
RA   Hynes R.O.;
RT   "Layilin, a cell surface hyaluronan receptor, interacts with merlin and
RT   radixin.";
RL   Exp. Cell Res. 308:177-187(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286 AND SER-299, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Receptor for hyaluronate. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TLN1 (By similarity). Interacts with NF2 and
CC       RDX. {ECO:0000250, ECO:0000269|PubMed:15913605}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Note=Colocalizes with TLN1 at the
CC       membrane ruffles. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C351-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C351-2; Sequence=VSP_021782, VSP_021783;
CC   -!- DOMAIN: The C-terminal domain interacts with the N-terminal domain of
CC       RDX.
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DR   EMBL; AK086930; BAC39765.2; -; mRNA.
DR   EMBL; AK165695; BAE38343.1; -; mRNA.
DR   EMBL; AC119831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS52791.1; -. [Q8C351-1]
DR   RefSeq; NP_001028706.1; NM_001033534.1. [Q8C351-1]
DR   PDB; 2K00; NMR; -; B=367-381.
DR   PDBsum; 2K00; -.
DR   AlphaFoldDB; Q8C351; -.
DR   SMR; Q8C351; -.
DR   ELM; Q8C351; -.
DR   STRING; 10090.ENSMUSP00000096379; -.
DR   GlyGen; Q8C351; 1 site.
DR   iPTMnet; Q8C351; -.
DR   PhosphoSitePlus; Q8C351; -.
DR   jPOST; Q8C351; -.
DR   MaxQB; Q8C351; -.
DR   PaxDb; Q8C351; -.
DR   PeptideAtlas; Q8C351; -.
DR   PRIDE; Q8C351; -.
DR   ProteomicsDB; 264843; -. [Q8C351-1]
DR   ProteomicsDB; 264844; -. [Q8C351-2]
DR   Antibodypedia; 32045; 375 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000098782; ENSMUSP00000096379; ENSMUSG00000060594. [Q8C351-1]
DR   GeneID; 244864; -.
DR   KEGG; mmu:244864; -.
DR   UCSC; uc012gtc.1; mouse. [Q8C351-1]
DR   CTD; 143903; -.
DR   MGI; MGI:2685357; Layn.
DR   VEuPathDB; HostDB:ENSMUSG00000060594; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00390000001844; -.
DR   HOGENOM; CLU_045492_1_1_1; -.
DR   InParanoid; Q8C351; -.
DR   OMA; VHSGEAT; -.
DR   OrthoDB; 1005951at2759; -.
DR   PhylomeDB; Q8C351; -.
DR   TreeFam; TF330715; -.
DR   BioGRID-ORCS; 244864; 0 hits in 72 CRISPR screens.
DR   ChiTaRS; Layn; mouse.
DR   EvolutionaryTrace; Q8C351; -.
DR   PRO; PR:Q8C351; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q8C351; protein.
DR   Bgee; ENSMUSG00000060594; Expressed in aortic valve and 113 other tissues.
DR   ExpressionAtlas; Q8C351; baseline and differential.
DR   Genevisible; Q8C351; MM.
DR   GO; GO:0009986; C:cell surface; ISS:HGNC-UCL.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001726; C:ruffle; ISS:HGNC-UCL.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0005540; F:hyaluronic acid binding; ISS:HGNC-UCL.
DR   Gene3D; 3.10.100.10; -; 1.
DR   IDEAL; IID50232; -.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Disulfide bond; Glycoprotein; Lectin;
KW   Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..381
FT                   /note="Layilin"
FT                   /id="PRO_0000262509"
FT   TOPO_DOM        25..235
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..381
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          45..185
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   REPEAT          340..344
FT                   /note="1-1"
FT   REPEAT          350..354
FT                   /note="1-2"
FT   REPEAT          356..359
FT                   /note="2-1"
FT   REPEAT          371..375
FT                   /note="1-3"
FT   REPEAT          377..380
FT                   /note="2-2"
FT   REGION          330..374
FT                   /note="Interaction with NF2"
FT                   /evidence="ECO:0000269|PubMed:15913605"
FT   REGION          337..381
FT                   /note="Interaction with TLN1"
FT                   /evidence="ECO:0000250"
FT   REGION          340..375
FT                   /note="3 X 5 AA repeats of E-S-G-X-V"
FT   REGION          356..380
FT                   /note="2 X 4 AA repeats of N-X-I-Y"
FT   MOD_RES         286
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         299
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        71..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        150..176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   VAR_SEQ         136..137
FT                   /note="RN -> SG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_021782"
FT   VAR_SEQ         138..381
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_021783"
FT   STRAND          372..376
FT                   /evidence="ECO:0007829|PDB:2K00"
SQ   SEQUENCE   381 AA;  43269 MW;  CF20C2EE708A5E07 CRC64;
     MQPGAALQAM LLAVLLAKPR DSKGRLLSAS DLDPRGGQLV CRGGTRRPCY KVIYFHDAFQ
     RLNFEEAKET CMEDGGQLVS IETEDEQRLI EKFIENLLAS DGDFWIGLKR LEEKQSNNTA
     CQDLYAWTDG STSQFRNWYV DEPSCGSEVC VVMYHQPSAP PGIGGSYMFQ WNDDRCNMKN
     NFICKYHDDK PSTTPSIWPG GEATEPATPL LPEETQKEDT KETFKERREA ALNLAYILIP
     SIPLFLLLVV TSAVCWVWIC RRKREQTDPS TKEQHTIWPT PRQENSPNLD VYNVIRKQSE
     ADLAEPRPDL KNISFRVCSG EAMPDDMSCD YENIAVNPSE SGFVTLASME SGFVTNDIYE
     FSPDRMGRSK ESGWVENEIY Y
 
 
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