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LRRN1_MOUSE
ID   LRRN1_MOUSE             Reviewed;         716 AA.
AC   Q61809; Q3USY1; Q69ZI0;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=Leucine-rich repeat neuronal protein 1;
DE   AltName: Full=Neuronal leucine-rich repeat protein 1;
DE            Short=NLRR-1;
DE   Flags: Precursor;
GN   Name=Lrrn1; Synonyms=Kiaa1497;
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   STRAIN=ICR; TISSUE=Brain;
RX   PubMed=8717337; DOI=10.1016/0169-328x(95)00178-u;
RA   Taguchi A., Wanaka A., Mori T., Matsumoto K., Imai Y., Takagi T.,
RA   Tohyama M.;
RT   "Molecular cloning of novel leucine-rich repeat proteins and their
RT   expression in the developing mouse nervous system.";
RL   Brain Res. Mol. Brain Res. 35:31-40(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, Brain cortex, and Corpora quadrigemina;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
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 brain. {ECO:0000269|PubMed:8717337}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32464.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D45913; BAA08341.1; -; mRNA.
DR   EMBL; AK173186; BAD32464.1; ALT_INIT; mRNA.
DR   EMBL; AK139355; BAE23973.1; -; mRNA.
DR   EMBL; AK139965; BAE24199.1; -; mRNA.
DR   EMBL; AK160841; BAE36040.1; -; mRNA.
DR   EMBL; BC031122; AAH31122.1; -; mRNA.
DR   EMBL; BC058701; AAH58701.1; -; mRNA.
DR   CCDS; CCDS20399.1; -.
DR   RefSeq; NP_032542.1; NM_008516.4.
DR   AlphaFoldDB; Q61809; -.
DR   SMR; Q61809; -.
DR   STRING; 10090.ENSMUSP00000037096; -.
DR   GlyGen; Q61809; 5 sites.
DR   iPTMnet; Q61809; -.
DR   PhosphoSitePlus; Q61809; -.
DR   MaxQB; Q61809; -.
DR   PaxDb; Q61809; -.
DR   PRIDE; Q61809; -.
DR   ProteomicsDB; 290174; -.
DR   ABCD; Q61809; 6 sequenced antibodies.
DR   Antibodypedia; 2639; 86 antibodies from 21 providers.
DR   DNASU; 16979; -.
DR   Ensembl; ENSMUST00000049285; ENSMUSP00000037096; ENSMUSG00000034648.
DR   GeneID; 16979; -.
DR   KEGG; mmu:16979; -.
DR   UCSC; uc009ddd.2; mouse.
DR   CTD; 57633; -.
DR   MGI; MGI:106038; Lrrn1.
DR   VEuPathDB; HostDB:ENSMUSG00000034648; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000157154; -.
DR   HOGENOM; CLU_000288_18_18_1; -.
DR   InParanoid; Q61809; -.
DR   OMA; KTTVRFM; -.
DR   OrthoDB; 998247at2759; -.
DR   PhylomeDB; Q61809; -.
DR   TreeFam; TF334360; -.
DR   BioGRID-ORCS; 16979; 0 hits in 70 CRISPR screens.
DR   ChiTaRS; Lrrn1; mouse.
DR   PRO; PR:Q61809; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q61809; protein.
DR   Bgee; ENSMUSG00000034648; Expressed in pontine nuclear group and 228 other tissues.
DR   Genevisible; Q61809; MM.
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: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   Pfam; PF07679; I-set; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF01463; LRRCT; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00369; LRR_TYP; 9.
DR   SMART; SM00082; LRRCT; 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..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..716
FT                   /note="Leucine-rich repeat neuronal protein 1"
FT                   /id="PRO_0000014848"
FT   TOPO_DOM        26..631
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        632..652
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        653..716
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          26..72
FT                   /note="LRRNT"
FT   REPEAT          73..95
FT                   /note="LRR 1"
FT   REPEAT          96..117
FT                   /note="LRR 2"
FT   REPEAT          120..141
FT                   /note="LRR 3"
FT   REPEAT          144..165
FT                   /note="LRR 4"
FT   REPEAT          168..189
FT                   /note="LRR 5"
FT   REPEAT          192..213
FT                   /note="LRR 6"
FT   REPEAT          216..237
FT                   /note="LRR 7"
FT   REPEAT          240..261
FT                   /note="LRR 8"
FT   REPEAT          264..285
FT                   /note="LRR 9"
FT   DOMAIN          371..424
FT                   /note="LRRCT"
FT   DOMAIN          424..515
FT                   /note="Ig-like C2-type"
FT   DOMAIN          525..619
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          692..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        69
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        385
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        447..499
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   716 AA;  80548 MW;  5073FB4801D08F58 CRC64;
     MARLSTGKAA CQVVLGLLIT SLTESSILTS ECPQLCVCEI RPWFTPQSTY REATTVDCND
     LRLTRIPGNL SSDTQVLLLQ SNNIAKTVDE LQQLFNLTEL DFSQNNFTNI KEVGLANLTQ
     LTTLHLEENQ ISEMTDYCLQ DLSNLQELYI NHNQISTISA NAFSGLKNLL RLHLNSNKLK
     VIDSRWFDST PNLEILMIGE NPVIGILDMN FRPLSNLRSL VLAGMYLTDV PGNALVGLDS
     LESLSFYDNK LIKVPQLALQ KVPNLKFLDL NKNPIHKIQE GDFKNMLRLK ELGINNMGEL
     VSVDRYALDN LPELTKLEAT NNPKLSYIHR LAFRSVPALE SLMLNNNALN AVYQKTVESL
     PNLREISIHS NPLRCDCVIH WINSNKTNIR FMEPLSMFCA MPPEYRGQQV KEVLIQDSSE
     QCLPMISHDT FPNHLNMDIG TTLFLDCRAM AEPEPEIYWV TPIGNKITVE TLSDKYKLSS
     EGTLEIANIQ IEDSGRYTCV AQNVQGADTR VATIKVNGTL LDGAQVLKIY VKQTESHSIL
     VSWKVNSNVM TSNLKWSSAT MKIDNPHITY TARVPVDVHE YNLTHLQPST DYEVCLTVSN
     IHQQTQKSCV NVTTKTAAFA LDISDHETST ALAAVMGSMF AVISLASIAI YIAKRFKRKN
     YHHSLKKYMQ KTSSIPLNEL YPPLINLWEA DSDKDKDGSA DTKPTQVDTS RSYYMW
 
 
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