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Protein

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

Gene

Lrfn5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca2+-independent manner. Promotes neurite outgrowth in hippocampal neurons (By similarity).By similarity

Enzyme and pathway databases

ReactomeiR-MMU-8849932. SALM protein interactions at the synapse.

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine-rich repeat and fibronectin type-III domain-containing protein 5
Gene namesi
Name:Lrfn5
Synonyms:Kiaa4208, Salm5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:2144814. Lrfn5.

Subcellular locationi

  • Membrane 1 Publication; Single-pass type I membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 529512ExtracellularSequence analysisAdd
BLAST
Transmembranei530 – 55021HelicalSequence analysisAdd
BLAST
Topological domaini551 – 719169CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: MGI
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence analysisAdd
BLAST
Chaini18 – 719702Leucine-rich repeat and fibronectin type-III domain-containing protein 5PRO_0000014846Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi73 – 731N-linked (GlcNAc...)Sequence analysis
Disulfide bondi308 ↔ 357PROSITE-ProRule annotation
Glycosylationi330 – 3301N-linked (GlcNAc...)Sequence analysis
Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence analysis
Glycosylationi382 – 3821N-linked (GlcNAc...)Sequence analysis
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence analysis
Glycosylationi452 – 4521N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ8BXA0.
PaxDbiQ8BXA0.
PRIDEiQ8BXA0.

PTM databases

iPTMnetiQ8BXA0.
PhosphoSiteiQ8BXA0.

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ8BXA0.
GenevisibleiQ8BXA0. MM.

Interactioni

Subunit structurei

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.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000051546.

Structurei

3D structure databases

ProteinModelPortaliQ8BXA0.
SMRiQ8BXA0. Positions 20-436.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 5134LRRNTAdd
BLAST
Repeati52 – 7322LRR 1Add
BLAST
Repeati76 – 9722LRR 2Add
BLAST
Repeati100 – 12122LRR 3Add
BLAST
Repeati124 – 14522LRR 4Add
BLAST
Repeati148 – 16922LRR 5Add
BLAST
Repeati172 – 19322LRR 6Add
BLAST
Repeati196 – 21722LRR 7Add
BLAST
Domaini240 – 28647LRRCTAdd
BLAST
Domaini287 – 37387Ig-likeAdd
BLAST
Domaini414 – 50390Fibronectin type-IIIAdd
BLAST

Domaini

Lacks a cytoplasmic PDZ-binding motif, which has been implicated in function of related LRFN proteins.

Sequence similaritiesi

Belongs to the LRFN family.Curated
Contains 1 fibronectin type-III domain.Curated
Contains 7 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated
Contains 1 LRRNT domain.Curated

Keywords - Domaini

Immunoglobulin domain, Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118831.
HOGENOMiHOG000237343.
HOVERGENiHBG052352.
InParanoidiQ8BXA0.
KOiK16358.
OMAiTNVESQN.
OrthoDBiEOG75B84P.
PhylomeDBiQ8BXA0.
TreeFamiTF350185.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR026879. Lrfn5.
IPR026906. LRR_5.
[Graphical view]
PANTHERiPTHR24373:SF3. PTHR24373:SF3. 1 hit.
PfamiPF07679. I-set. 1 hit.
PF13306. LRR_5. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00369. LRR_TYP. 6 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51450. LRR. 6 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BXA0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEKFLFYLFL IGIAVRAQIC PKRCVCQILS PNLATLCAKK GLLFVPPNID
60 70 80 90 100
RRTVELRLAD NFVTNIKRKD FANMTSLVDL TLSRNTISFI TPHAFADLRN
110 120 130 140 150
LRALHLNSNR LTKITNDMFS GLSNLHHLIL NNNQLTLISS TAFDDVFALE
160 170 180 190 200
ELDLSYNNLE TIPWDAVEKM VSLHTLSLDH NMIDNIPKGT FSHLHKMTRL
210 220 230 240 250
DVTSNKLQKL PPDPLFQRAQ VLATSGIISP STFALSFGGN PLHCNCELLW
260 270 280 290 300
LRRLSREDDL ETCASPALLT GRYFWSIPEE EFLCEPPLIT RHTHEMRVLE
310 320 330 340 350
GQRATLRCKA RGDPEPAIHW ISPEGKLISN ATRSLVYDNG TLDILITTVK
360 370 380 390 400
DTGAFTCIAS NPAGEATQTV DLHIIKLPHL LNSTNHIHEP DPGSSDISTS
410 420 430 440 450
TKSGSNASSS NGDTKMSQDK IVVAEATSST ALLKFNFQRN IPGIRMFQIQ
460 470 480 490 500
YNGTYDDTLV YRMIPPTSKT FLVNNLASGT MYDLCVLAIY DDGITSLTAT
510 520 530 540 550
RVVGCIQFTT EQDYVRCHFM QSQFLGGTMI IIIGGIIVAS VLVFIIILMI
560 570 580 590 600
RYKVCNNNGQ HKVTKVSNVY SQTNGAQMQG CSVTLPQSMS KQAMGHEENA
610 620 630 640 650
QCCKVASDNA IQSSETCSSQ DSSTTTSALP PTWTSSAPVS QKQKRKTGTK
660 670 680 690 700
PSAEPQSEAV TNVESQNTNR NNSTALQLAS CPPDSVTEGP TSQRAHTKPN
710
ALLTNVDQNV QETQRLESI
Length:719
Mass (Da):79,371
Last modified:March 1, 2003 - v1
Checksum:iDCA5D8C68F7D6FEC
GO
Isoform 2 (identifier: Q8BXA0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     700-719: NALLTNVDQNVQETQRLESI → SKFLTVPAEGSRARHRASLSGGLKDSFHYGNSQLSLKRSMSMNAMWT

Note: Due to intron retention. No experimental confirmation available.
Show »
Length:746
Mass (Da):82,286
Checksum:i00AA4767BA19908E
GO

Sequence cautioni

The sequence BAD90535.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei700 – 71920NALLT…RLESI → SKFLTVPAEGSRARHRASLS GGLKDSFHYGNSQLSLKRSM SMNAMWT in isoform 2. 1 PublicationVSP_009299Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034245 mRNA. Translation: BAC28645.1.
AK048443 mRNA. Translation: BAC33339.1.
AK220546 mRNA. Translation: BAD90535.1. Different initiation.
BC052038 mRNA. Translation: AAH52038.1.
CCDSiCCDS25936.1. [Q8BXA0-2]
CCDS79117.1. [Q8BXA0-1]
RefSeqiNP_001297515.1. NM_001310586.1. [Q8BXA0-1]
NP_848829.2. NM_178714.5. [Q8BXA0-2]
XP_006515893.1. XM_006515830.1. [Q8BXA0-2]
XP_006515894.1. XM_006515831.2. [Q8BXA0-2]
UniGeneiMm.28802.

Genome annotation databases

EnsembliENSMUST00000055815; ENSMUSP00000051546; ENSMUSG00000035653. [Q8BXA0-2]
ENSMUST00000119481; ENSMUSP00000113123; ENSMUSG00000035653. [Q8BXA0-1]
GeneIDi238205.
KEGGimmu:238205.
UCSCiuc007nqm.1. mouse. [Q8BXA0-2]
uc007nqn.1. mouse. [Q8BXA0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK034245 mRNA. Translation: BAC28645.1.
AK048443 mRNA. Translation: BAC33339.1.
AK220546 mRNA. Translation: BAD90535.1. Different initiation.
BC052038 mRNA. Translation: AAH52038.1.
CCDSiCCDS25936.1. [Q8BXA0-2]
CCDS79117.1. [Q8BXA0-1]
RefSeqiNP_001297515.1. NM_001310586.1. [Q8BXA0-1]
NP_848829.2. NM_178714.5. [Q8BXA0-2]
XP_006515893.1. XM_006515830.1. [Q8BXA0-2]
XP_006515894.1. XM_006515831.2. [Q8BXA0-2]
UniGeneiMm.28802.

3D structure databases

ProteinModelPortaliQ8BXA0.
SMRiQ8BXA0. Positions 20-436.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000051546.

PTM databases

iPTMnetiQ8BXA0.
PhosphoSiteiQ8BXA0.

Proteomic databases

MaxQBiQ8BXA0.
PaxDbiQ8BXA0.
PRIDEiQ8BXA0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000055815; ENSMUSP00000051546; ENSMUSG00000035653. [Q8BXA0-2]
ENSMUST00000119481; ENSMUSP00000113123; ENSMUSG00000035653. [Q8BXA0-1]
GeneIDi238205.
KEGGimmu:238205.
UCSCiuc007nqm.1. mouse. [Q8BXA0-2]
uc007nqn.1. mouse. [Q8BXA0-1]

Organism-specific databases

CTDi145581.
MGIiMGI:2144814. Lrfn5.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0619. Eukaryota.
COG4886. LUCA.
GeneTreeiENSGT00760000118831.
HOGENOMiHOG000237343.
HOVERGENiHBG052352.
InParanoidiQ8BXA0.
KOiK16358.
OMAiTNVESQN.
OrthoDBiEOG75B84P.
PhylomeDBiQ8BXA0.
TreeFamiTF350185.

Enzyme and pathway databases

ReactomeiR-MMU-8849932. SALM protein interactions at the synapse.

Miscellaneous databases

PROiQ8BXA0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BXA0.
GenevisibleiQ8BXA0. MM.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR026879. Lrfn5.
IPR026906. LRR_5.
[Graphical view]
PANTHERiPTHR24373:SF3. PTHR24373:SF3. 1 hit.
PfamiPF07679. I-set. 1 hit.
PF13306. LRR_5. 1 hit.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
SM00408. IGc2. 1 hit.
SM00369. LRR_TYP. 6 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 1 hit.
SSF49265. SSF49265. 1 hit.
SSF52058. SSF52058. 1 hit.
PROSITEiPS50835. IG_LIKE. 1 hit.
PS51450. LRR. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Diencephalon and Embryonic head.
  2. "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."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "Comparative analysis of structure, expression and PSD95-binding capacity of Lrfn, a novel family of neuronal transmembrane proteins."
    Morimura N., Inoue T., Katayama K., Aruga J.
    Gene 380:72-83(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, GLYCOSYLATION, LACK OF INTERACTION WITH DLG4, SUBCELLULAR LOCATION, TOPOLOGY.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiLRFN5_MOUSE
AccessioniPrimary (citable) accession number: Q8BXA0
Secondary accession number(s): Q5DTH4, Q8BJH4, Q8BZL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.