LRRN3_PONAB
ID LRRN3_PONAB Reviewed; 708 AA.
AC Q5R482;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 79.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR861375; CAH93434.1; -; mRNA.
DR RefSeq; NP_001127011.1; NM_001133539.1.
DR AlphaFoldDB; Q5R482; -.
DR SMR; Q5R482; -.
DR STRING; 9601.ENSPPYP00000020082; -.
DR PRIDE; Q5R482; -.
DR GeneID; 100174035; -.
DR KEGG; pon:100174035; -.
DR CTD; 54674; -.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; Q5R482; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 10.
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..708
FT /note="Leucine-rich repeat neuronal protein 3"
FT /id="PRO_0000045826"
FT TOPO_DOM 23..628
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 629..649
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 650..708
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..617
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 625
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 444..496
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 708 AA; 79233 MW; BEE284113F7CE212 CRC64;
MKDMPLQIHV LLGLAITTLV QAVDKKVDCP QLCTCEIRPW FTPTSIYMEA STVDCNDLGL
LTFPARLPAN TQILLLQTND IAKIEYSTDF PVNLTGLDLS QNNLSSVTNI NVKKMPQLLS
VYLEENKLTE LPEKCLSELS NLQELYINHN LLSTISPGAF IGLHNLLRLH LNSNRLQMIN
SKWFDALPNL EILMIGENPI IRIKDMNFKP LINLRSLVIA GINLTEIPDN ALVGLENLES
ISFYDNRLIK VPHAALQKVV NLKFLDLNKN PINRIRRGDF SNMLHLKELG INNMPELISI
DSLAVDNLPD LRKIEATNNP RLSYIHPNAF FRLPKLESLM LNSNALSALY HGTIESLPNL
KEISIHSNPI RCDCVIRWIN MNKTNIRFME PDSLFCVDPP EFQGQNVRQV HFRDMMEICL
PLIAPESFPS NLNVEAGSYV SFHCRATAEP QPEIYWITPS GQKLLPNTLT DKFYVHSEGT
LDINGVTPKE GGLYTCIATN LVGADLKSVM IKVDGSFPQD NNGSLNIKIR DIQANSVLVS
WKASSKILKS SVKWTAFVKT ENSHAAQSAR IPSDIKVYNL THLNPSTEYK ICIDIPTIYQ
KNRKKCVNVT TKGLDPDQKE YEKSNTTTLM ACLGGLLGII GVICLISCLS PEMNCDGGHS
YVRNYLQKPT FALGELYPPL INLWEAGKEK STSLKVKATV IGLPTNMS
