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Leucine-rich repeat and fibronectin type-III domain-containing protein 5

 LRFN5_MOUSE             Reviewed;         719 AA.
Q8BXA0; Q5DTH4; Q8BJH4; Q8BZL0;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
12-SEP-2018, entry version 134.
RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 5;
Flags: Precursor;
Name=Lrfn5; Synonyms=Kiaa4208, Salm5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Diencephalon, and Embryonic head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene.
The complete nucleotide sequences of mouse KIAA-homologous cDNAs
identified by screening of terminal sequences of cDNA clones randomly
sampled from size-fractionated libraries.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, GLYCOSYLATION, LACK OF
INTERACTION WITH DLG4, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=16828986; DOI=10.1016/j.gene.2006.05.014;
Morimura N., Inoue T., Katayama K., Aruga J.;
"Comparative analysis of structure, expression and PSD95-binding
capacity of Lrfn, a novel family of neuronal transmembrane proteins.";
Gene 380:72-83(2006).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Cell adhesion molecule that mediates homophilic cell-
cell adhesion in a Ca(2+)-independent manner. Promotes neurite
outgrowth in hippocampal neurons (By similarity). {ECO:0000250}.
-!- SUBUNIT: Can form heteromeric complexes with LRFN1, LRFN2, LRFN3
and LFRN4 (By similarity). Able to form homomeric complexes across
cell junctions, between adjacent cells (By similarity). Does not
interact with DLG1, DLG2 or DLG3 (By similarity). Does not
interact with DLG4. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16828986};
Single-pass type I membrane protein {ECO:0000269|PubMed:16828986}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8BXA0-1; Sequence=Displayed;
Name=2;
IsoId=Q8BXA0-2; Sequence=VSP_009299;
Note=Due to intron retention. No experimental confirmation
available.;
-!- TISSUE SPECIFICITY: Predominantly expressed in the brain, with a
weak, but broad expression in the cerebral cortex and diencephalic
nuclei. Strongly expressed in both the pyramidal layer and the
dentate gyrus of the hippocampus. Also detected in other parts of
the central nervous system, including the olfactory bulb, pons,
cerebellum, and medulla oblongata, as well as in the peripheral
nervous system, such as the ganglia of cranial nerves and the
dorsal root ganglion during gestation.
{ECO:0000269|PubMed:16828986}.
-!- DEVELOPMENTAL STAGE: Expression starts around 11.5-12.5 dpc. At
11.5 dpc, detected in the outer layer of the telencephalic
vesicles. This pattern of expression continues until 17.5 dpc with
expression in the cortical plate, but not in the inner layer of
the cerebral cortex, including subplate, ventricular zone, and
subventricular zone. As also detected in the hippocampus, amygdala
and widely in diencephalic nuclei. {ECO:0000269|PubMed:16828986}.
-!- DOMAIN: Lacks a cytoplasmic PDZ-binding motif, which has been
implicated in function of related LRFN proteins.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:16828986}.
-!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD90535.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK034245; BAC28645.1; -; mRNA.
EMBL; AK048443; BAC33339.1; -; mRNA.
EMBL; AK220546; BAD90535.1; ALT_INIT; mRNA.
EMBL; BC052038; AAH52038.1; -; mRNA.
CCDS; CCDS25936.1; -. [Q8BXA0-2]
CCDS; CCDS79117.1; -. [Q8BXA0-1]
RefSeq; NP_001297515.1; NM_001310586.1. [Q8BXA0-1]
RefSeq; NP_848829.2; NM_178714.5. [Q8BXA0-2]
RefSeq; XP_006515893.1; XM_006515830.2. [Q8BXA0-2]
RefSeq; XP_006515894.1; XM_006515831.3. [Q8BXA0-2]
RefSeq; XP_017170545.1; XM_017315056.1. [Q8BXA0-1]
UniGene; Mm.28802; -.
PDB; 6F2O; X-ray; 3.00 A; A=18-376.
PDBsum; 6F2O; -.
ProteinModelPortal; Q8BXA0; -.
SMR; Q8BXA0; -.
STRING; 10090.ENSMUSP00000051546; -.
iPTMnet; Q8BXA0; -.
PhosphoSitePlus; Q8BXA0; -.
PaxDb; Q8BXA0; -.
PeptideAtlas; Q8BXA0; -.
PRIDE; Q8BXA0; -.
Ensembl; ENSMUST00000055815; ENSMUSP00000051546; ENSMUSG00000035653. [Q8BXA0-2]
Ensembl; ENSMUST00000119481; ENSMUSP00000113123; ENSMUSG00000035653. [Q8BXA0-1]
GeneID; 238205; -.
KEGG; mmu:238205; -.
UCSC; uc007nqm.1; mouse. [Q8BXA0-2]
UCSC; uc007nqn.1; mouse. [Q8BXA0-1]
CTD; 145581; -.
MGI; MGI:2144814; Lrfn5.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00760000118831; -.
HOGENOM; HOG000237343; -.
HOVERGEN; HBG052352; -.
InParanoid; Q8BXA0; -.
KO; K16358; -.
OMA; TNVESQN; -.
OrthoDB; EOG091G01R2; -.
PhylomeDB; Q8BXA0; -.
TreeFam; TF350185; -.
PRO; PR:Q8BXA0; -.
Proteomes; UP000000589; Chromosome 12.
Bgee; ENSMUSG00000035653; Expressed in 116 organ(s), highest expression level in visual cortex.
Genevisible; Q8BXA0; MM.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 3.80.10.10; -; 2.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR026879; Lrfn5.
InterPro; IPR026906; LRR_5.
InterPro; IPR032675; LRR_dom_sf.
PANTHER; PTHR24373:SF3; PTHR24373:SF3; 1.
Pfam; PF07679; I-set; 1.
Pfam; PF13306; LRR_5; 1.
SMART; SM00409; IG; 1.
SMART; SM00408; IGc2; 1.
SMART; SM00369; LRR_TYP; 6.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF49265; SSF49265; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS51450; LRR; 6.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Leucine-rich repeat; Membrane;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 17 {ECO:0000255}.
CHAIN 18 719 Leucine-rich repeat and fibronectin type-
III domain-containing protein 5.
/FTId=PRO_0000014846.
TOPO_DOM 18 529 Extracellular. {ECO:0000255}.
TRANSMEM 530 550 Helical. {ECO:0000255}.
TOPO_DOM 551 719 Cytoplasmic. {ECO:0000255}.
DOMAIN 18 51 LRRNT.
REPEAT 52 73 LRR 1.
REPEAT 76 97 LRR 2.
REPEAT 100 121 LRR 3.
REPEAT 124 145 LRR 4.
REPEAT 148 169 LRR 5.
REPEAT 172 193 LRR 6.
REPEAT 196 217 LRR 7.
DOMAIN 240 286 LRRCT.
DOMAIN 287 373 Ig-like.
DOMAIN 414 503 Fibronectin type-III.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 339 339 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 382 382 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 452 452 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 308 357 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 700 719 NALLTNVDQNVQETQRLESI -> SKFLTVPAEGSRARHRA
SLSGGLKDSFHYGNSQLSLKRSMSMNAMWT (in
isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_009299.
SEQUENCE 719 AA; 79371 MW; DCA5D8C68F7D6FEC CRC64;
MEKFLFYLFL IGIAVRAQIC PKRCVCQILS PNLATLCAKK GLLFVPPNID RRTVELRLAD
NFVTNIKRKD FANMTSLVDL TLSRNTISFI TPHAFADLRN LRALHLNSNR LTKITNDMFS
GLSNLHHLIL NNNQLTLISS TAFDDVFALE ELDLSYNNLE TIPWDAVEKM VSLHTLSLDH
NMIDNIPKGT FSHLHKMTRL DVTSNKLQKL PPDPLFQRAQ VLATSGIISP STFALSFGGN
PLHCNCELLW LRRLSREDDL ETCASPALLT GRYFWSIPEE EFLCEPPLIT RHTHEMRVLE
GQRATLRCKA RGDPEPAIHW ISPEGKLISN ATRSLVYDNG TLDILITTVK DTGAFTCIAS
NPAGEATQTV DLHIIKLPHL LNSTNHIHEP DPGSSDISTS TKSGSNASSS NGDTKMSQDK
IVVAEATSST ALLKFNFQRN IPGIRMFQIQ YNGTYDDTLV YRMIPPTSKT FLVNNLASGT
MYDLCVLAIY DDGITSLTAT RVVGCIQFTT EQDYVRCHFM QSQFLGGTMI IIIGGIIVAS
VLVFIIILMI RYKVCNNNGQ HKVTKVSNVY SQTNGAQMQG CSVTLPQSMS KQAMGHEENA
QCCKVASDNA IQSSETCSSQ DSSTTTSALP PTWTSSAPVS QKQKRKTGTK PSAEPQSEAV
TNVESQNTNR NNSTALQLAS CPPDSVTEGP TSQRAHTKPN ALLTNVDQNV QETQRLESI


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