LRRN1_RAT
ID LRRN1_RAT Reviewed; 716 AA.
AC Q32Q07;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
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;
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 MRNA].
RC TISSUE=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}.
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DR EMBL; BC107902; AAI07903.1; -; mRNA.
DR RefSeq; NP_001032440.1; NM_001037363.1.
DR RefSeq; XP_006237046.1; XM_006236984.3.
DR RefSeq; XP_017448322.1; XM_017592833.1.
DR AlphaFoldDB; Q32Q07; -.
DR SMR; Q32Q07; -.
DR BioGRID; 271588; 1.
DR STRING; 10116.ENSRNOP00000008879; -.
DR GlyGen; Q32Q07; 8 sites.
DR iPTMnet; Q32Q07; -.
DR PhosphoSitePlus; Q32Q07; -.
DR PaxDb; Q32Q07; -.
DR Ensembl; ENSRNOT00000008879; ENSRNOP00000008879; ENSRNOG00000006802.
DR Ensembl; ENSRNOT00000114168; ENSRNOP00000082837; ENSRNOG00000006802.
DR GeneID; 500280; -.
DR KEGG; rno:500280; -.
DR UCSC; RGD:1564145; rat.
DR CTD; 57633; -.
DR RGD; 1564145; Lrrn1.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000157154; -.
DR HOGENOM; CLU_000288_18_18_1; -.
DR InParanoid; Q32Q07; -.
DR OMA; KTTVRFM; -.
DR OrthoDB; 998247at2759; -.
DR PhylomeDB; Q32Q07; -.
DR TreeFam; TF334360; -.
DR PRO; PR:Q32Q07; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000006802; Expressed in cerebellum and 15 other tissues.
DR Genevisible; Q32Q07; RN.
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; ISO:RGD.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.80.10.10; -; 2.
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_0000045822"
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 691..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 106
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 CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 611
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; 80629 MW; 2CCDCF04BF070C09 CRC64;
MARLSPGKAA CWMVLGLLIP SLTESSILNS ECPQLCVCEI RPWFTPQSTY REATTVDCND
LRLTRIPGNL SSDTQVLLLQ SNNIAKTVDE LQQLFNLTEL DFSQNNFTNI KEVGLANLTQ
LTTLHLEENQ ISEMTDYCLQ DLSNLQELYI NHNQISSISA NAFSGLKNLL RLHLNSNKLK
VIDSRWFDST PNLEILMIGE NPVIGILDMN FRPLSNLRSL VLAGMYLTDI 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 YPPLINLWEG DSDKDKDGSA DTKPTQVDTS RSYYMW
