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LRRN3_MOUSE
ID   LRRN3_MOUSE             Reviewed;         707 AA.
AC   Q8CBC6; P97860;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 161.
DE   RecName: Full=Leucine-rich repeat neuronal protein 3;
DE   AltName: Full=Neuronal leucine-rich repeat protein 3;
DE            Short=NLRR-3;
DE   Flags: Precursor;
GN   Name=Lrrn3;
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 [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9011764; DOI=10.1016/0169-328x(95)00243-l;
RA   Taniguchi H., Tohyama M., Takagi T.;
RT   "Cloning and expression of a novel gene for a protein with leucine-rich
RT   repeats in the developing mouse nervous system.";
RL   Brain Res. Mol. Brain Res. 36:45-52(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, in Stronger expression in
CC       the ventricular zone and anlage of thalamus, spinal cord, and dorsal
CC       root ganglion in 11-17 dpc cerebellum and cerebral cortex in adults.
CC       {ECO:0000269|PubMed:9011764}.
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DR   EMBL; D49802; BAA08622.1; -; mRNA.
DR   EMBL; AK036316; BAC29381.1; -; mRNA.
DR   EMBL; BC069041; AAH69041.1; -; mRNA.
DR   CCDS; CCDS25896.1; -.
DR   RefSeq; NP_001258637.1; NM_001271708.1.
DR   RefSeq; NP_001258638.1; NM_001271709.1.
DR   RefSeq; NP_034863.1; NM_010733.3.
DR   AlphaFoldDB; Q8CBC6; -.
DR   SMR; Q8CBC6; -.
DR   STRING; 10090.ENSMUSP00000043818; -.
DR   GlyConnect; 2472; 1 N-Linked glycan (1 site).
DR   GlyGen; Q8CBC6; 8 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; Q8CBC6; -.
DR   PhosphoSitePlus; Q8CBC6; -.
DR   SwissPalm; Q8CBC6; -.
DR   MaxQB; Q8CBC6; -.
DR   PaxDb; Q8CBC6; -.
DR   PRIDE; Q8CBC6; -.
DR   ProteomicsDB; 292117; -.
DR   Antibodypedia; 31483; 186 antibodies from 22 providers.
DR   DNASU; 16981; -.
DR   Ensembl; ENSMUST00000043884; ENSMUSP00000043818; ENSMUSG00000036295.
DR   GeneID; 16981; -.
DR   KEGG; mmu:16981; -.
DR   UCSC; uc007nln.2; mouse.
DR   CTD; 54674; -.
DR   MGI; MGI:106036; Lrrn3.
DR   VEuPathDB; HostDB:ENSMUSG00000036295; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000160513; -.
DR   HOGENOM; CLU_000288_18_18_1; -.
DR   InParanoid; Q8CBC6; -.
DR   OMA; DKFYMHP; -.
DR   OrthoDB; 998247at2759; -.
DR   PhylomeDB; Q8CBC6; -.
DR   TreeFam; TF334360; -.
DR   BioGRID-ORCS; 16981; 3 hits in 71 CRISPR screens.
DR   ChiTaRS; Lrrn3; mouse.
DR   PRO; PR:Q8CBC6; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q8CBC6; protein.
DR   Bgee; ENSMUSG00000036295; Expressed in superior cervical ganglion and 196 other tissues.
DR   Genevisible; Q8CBC6; MM.
DR   GO; GO:0030131; C:clathrin adaptor complex; ISO:MGI.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IDA:MGI.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 3.80.10.10; -; 3.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR000372; LRRNT.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51450; LRR; 9.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Leucine-rich repeat;
KW   Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..707
FT                   /note="Leucine-rich repeat neuronal protein 3"
FT                   /id="PRO_0000045824"
FT   TOPO_DOM        23..626
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        627..647
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        648..707
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          23..69
FT                   /note="LRRNT"
FT   REPEAT          70..91
FT                   /note="LRR 1"
FT   REPEAT          93..114
FT                   /note="LRR 2"
FT   REPEAT          117..138
FT                   /note="LRR 3"
FT   REPEAT          141..162
FT                   /note="LRR 4"
FT   REPEAT          165..186
FT                   /note="LRR 5"
FT   REPEAT          189..210
FT                   /note="LRR 6"
FT   REPEAT          213..234
FT                   /note="LRR 7"
FT   REPEAT          237..258
FT                   /note="LRR 8"
FT   REPEAT          261..282
FT                   /note="LRR 9"
FT   REPEAT          285..304
FT                   /note="LRR 10"
FT   REPEAT          310..332
FT                   /note="LRR 11"
FT   REPEAT          335..358
FT                   /note="LRR 12"
FT   DOMAIN          368..421
FT                   /note="LRRCT"
FT   DOMAIN          421..514
FT                   /note="Ig-like C2-type"
FT   DOMAIN          523..614
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        522
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        579
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        608
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        624
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        444..496
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        551
FT                   /note="S -> R (in Ref. 1; BAA08622)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        556
FT                   /note="A -> G (in Ref. 1; BAA08622)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        573
FT                   /note="F -> S (in Ref. 1; BAA08622)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        639
FT                   /note="I -> V (in Ref. 1; BAA08622)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   707 AA;  79176 MW;  DFCA009A2553E0FC CRC64;
     MKDTPLQVHV LLGLAITTLV QAIDKKVDCP QLCTCEIRPW FTPRSIYMEA STVDCNDLGL
     LNFPARLPAD TQILLLQTNN IARIEHSTDF PVNLTGLDLS QNNLSSVTNI NVQKMSQLLS
     VYLEENKLTE LPEKCLYGLS NLQELYVNHN LLSTISPGAF IGLHNLLRLH LNSNRLQMIN
     SQWFDALPNL EILMLGDNPI IRIKDMNFQP LVKLRSLVIA GINLTEIPDD ALAGLENLES
     ISFYDNRLSK VPQVALQKAV NLKFLDLNKN PINRIRRGDF SNMLHLKELG INNMPELVSI
     DSLAVDNLPD LRKIEATNNP RLSYIHPNAF FRLPKLESLM LNTNALSALY HGTIESLPNL
     KEISIHSNPI RCDCVIRWIN MNKTNIRFME PDSLFCVDPP EFQGQNVRQV HFRDMMEICL
     PLIAPESFPS DLDVEADSYV SLHCRATAEP QPEIYWITPS GKKLLPNTMR EKFYVHSEGT
     LEIRGITPKE GGLYTCIATN LVGADLKSIM IKVGGSVPQD NNGSLNIKIR DIRANSVLVS
     WKASSKILKS SVKWTAFVKT EDSHAAQSAR IPFDVKVYNL THLKPSTEYK ICIDIPTVYQ
     KSRKQCVNVT TKSLEHDGKE YGKNHTVFVA CVGGLLGIIG VMCLFSCVSQ EGSSEGEHSY
     AVNHCHKPAL AFSELYPPLI NLWESSKEKR ATLEVKATAI GVPTNMS
 
 
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