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Q96NI6

- LRFN5_HUMAN

UniProt

Q96NI6 - LRFN5_HUMAN

Protein

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

Gene

LRFN5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca2+-independent manner. Promotes neurite outgrowth in hippocampal neurons.2 Publications

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Leucine-rich repeat and fibronectin type-III domain-containing protein 5
    Gene namesi
    Name:LRFN5
    Synonyms:C14orf146, SALM5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:20360. LRFN5.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134888453.

    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_0000014845Add
    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

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ96NI6.
    PRIDEiQ96NI6.

    PTM databases

    PhosphoSiteiQ96NI6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96NI6.
    BgeeiQ96NI6.
    CleanExiHS_LRFN5.
    GenevestigatoriQ96NI6.

    Organism-specific databases

    HPAiHPA001177.

    Interactioni

    Subunit structurei

    Can form heteromeric complexes with LRFN1, LRFN2, LRFN3 and LFRN4. Able to form homomeric complexes across cell junctions, between adjacent cells. Does not interact with DLG1, DLG2, DLG3 and DLG4.

    Protein-protein interaction databases

    STRINGi9606.ENSP00000298119.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96NI6.
    SMRiQ96NI6. Positions 19-436.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini18 – 529512ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini551 – 719169CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei530 – 55021HelicalSequence AnalysisAdd
    BLAST

    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

    eggNOGiNOG249839.
    HOGENOMiHOG000237343.
    HOVERGENiHBG052352.
    InParanoidiQ96NI6.
    KOiK16358.
    OMAiTNVESQN.
    OrthoDBiEOG75B84P.
    PhylomeDBiQ96NI6.
    TreeFamiTF350185.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    InterProiIPR000483. Cys-rich_flank_reg_C.
    IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR026879. Lrfn5.
    IPR000372. LRR-contain_N.
    IPR026906. LRR_5.
    [Graphical view]
    PANTHERiPTHR24373:SF3. PTHR24373:SF3. 1 hit.
    PfamiPF07679. I-set. 1 hit.
    PF13306. LRR_5. 1 hit.
    [Graphical view]
    SMARTiSM00408. IGc2. 1 hit.
    SM00369. LRR_TYP. 3 hits.
    SM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 1 hit.
    PROSITEiPS50835. IG_LIKE. 1 hit.
    PS51450. LRR. 6 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q96NI6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKILFYLFL IGIAVKAQIC PKRCVCQILS PNLATLCAKK GLLFVPPNID    50
    RRTVELRLAD NFVTNIKRKD FANMTSLVDL TLSRNTISFI TPHAFADLRN 100
    LRALHLNSNR LTKITNDMFS GLSNLHHLIL NNNQLTLISS TAFDDVFALE 150
    ELDLSYNNLE TIPWDAVEKM VSLHTLSLDH NMIDNIPKGT FSHLHKMTRL 200
    DVTSNKLQKL PPDPLFQRAQ VLATSGIISP STFALSFGGN PLHCNCELLW 250
    LRRLSREDDL ETCASPPLLT GRYFWSIPEE EFLCEPPLIT RHTHEMRVLE 300
    GQRATLRCKA RGDPEPAIHW ISPEGKLISN ATRSLVYDNG TLDILITTVK 350
    DTGAFTCIAS NPAGEATQIV DLHIIKLPHL LNSTNHIHEP DPGSSDISTS 400
    TKSGSNTSSS NGDTKLSQDK IVVAEATSST ALLKFNFQRN IPGIRMFQIQ 450
    YNGTYDDTLV YRMIPPTSKT FLVNNLAAGT MYDLCVLAIY DDGITSLTAT 500
    RVVGCIQFTT EQDYVRCHFM QSQFLGGTMI IIIGGIIVAS VLVFIIILMI 550
    RYKVCNNNGQ HKVTKVSNVY SQTNGAQIQG CSVTLPQSVS KQAVGHEENA 600
    QCCKATSDNV IQSSETCSSQ DSSTTTSALP PSWTSSTSVS QKQKRKTGTK 650
    PSTEPQNEAV TNVESQNTNR NNSTALQLAS RPPDSVTEGP TSKRAHIKPN 700
    ALLTNVDQIV QETQRLELI 719
    Length:719
    Mass (Da):79,445
    Last modified:October 17, 2006 - v2
    Checksum:iDD92951A9705FF4B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti544 – 5441F → L in BAG53340. (PubMed:14702039)Curated
    Sequence conflicti679 – 6791A → V in BAB70910. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK055365 mRNA. Translation: BAB70910.1.
    AK096627 mRNA. Translation: BAG53340.1.
    AL138498 Genomic DNA. No translation available.
    BC043165 mRNA. Translation: AAH43165.1.
    CCDSiCCDS9678.1.
    RefSeqiNP_689660.2. NM_152447.3.
    UniGeneiHs.136893.

    Genome annotation databases

    EnsembliENST00000298119; ENSP00000298119; ENSG00000165379.
    GeneIDi145581.
    KEGGihsa:145581.
    UCSCiuc001wvm.3. human.

    Polymorphism databases

    DMDMi116242620.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK055365 mRNA. Translation: BAB70910.1 .
    AK096627 mRNA. Translation: BAG53340.1 .
    AL138498 Genomic DNA. No translation available.
    BC043165 mRNA. Translation: AAH43165.1 .
    CCDSi CCDS9678.1.
    RefSeqi NP_689660.2. NM_152447.3.
    UniGenei Hs.136893.

    3D structure databases

    ProteinModelPortali Q96NI6.
    SMRi Q96NI6. Positions 19-436.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000298119.

    PTM databases

    PhosphoSitei Q96NI6.

    Polymorphism databases

    DMDMi 116242620.

    Proteomic databases

    PaxDbi Q96NI6.
    PRIDEi Q96NI6.

    Protocols and materials databases

    DNASUi 145581.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000298119 ; ENSP00000298119 ; ENSG00000165379 .
    GeneIDi 145581.
    KEGGi hsa:145581.
    UCSCi uc001wvm.3. human.

    Organism-specific databases

    CTDi 145581.
    GeneCardsi GC14P042076.
    HGNCi HGNC:20360. LRFN5.
    HPAi HPA001177.
    MIMi 612811. gene.
    neXtProti NX_Q96NI6.
    PharmGKBi PA134888453.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249839.
    HOGENOMi HOG000237343.
    HOVERGENi HBG052352.
    InParanoidi Q96NI6.
    KOi K16358.
    OMAi TNVESQN.
    OrthoDBi EOG75B84P.
    PhylomeDBi Q96NI6.
    TreeFami TF350185.

    Miscellaneous databases

    GenomeRNAii 145581.
    NextBioi 85141.
    PROi Q96NI6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96NI6.
    Bgeei Q96NI6.
    CleanExi HS_LRFN5.
    Genevestigatori Q96NI6.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR000483. Cys-rich_flank_reg_C.
    IPR003961. Fibronectin_type3.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR026879. Lrfn5.
    IPR000372. LRR-contain_N.
    IPR026906. LRR_5.
    [Graphical view ]
    PANTHERi PTHR24373:SF3. PTHR24373:SF3. 1 hit.
    Pfami PF07679. I-set. 1 hit.
    PF13306. LRR_5. 1 hit.
    [Graphical view ]
    SMARTi SM00408. IGc2. 1 hit.
    SM00369. LRR_TYP. 3 hits.
    SM00082. LRRCT. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 1 hit.
    PROSITEi PS50835. IG_LIKE. 1 hit.
    PS51450. LRR. 6 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Fetal brain.
    2. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Brain.
    4. "SALM synaptic cell adhesion-like molecules regulate the differentiation of excitatory synapses."
      Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K., Kim E.
      Neuron 50:233-245(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: LACK OF INTERACTION WITH DLG1; DLG2; DLG3 AND DLG4.
    5. "The SALM family of adhesion-like molecules forms heteromeric and homomeric complexes."
      Seabold G.K., Wang P.Y., Chang K., Wang C.Y., Wang Y.X., Petralia R.S., Wenthold R.J.
      J. Biol. Chem. 283:8395-8405(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH LRFN1; LRFN2; LRFN3; LRFN4 AND LRFN5.
    6. "Synaptic adhesion-like molecules (SALMs) promote neurite outgrowth."
      Wang P.Y., Seabold G.K., Wenthold R.J.
      Mol. Cell. Neurosci. 39:83-94(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiLRFN5_HUMAN
    AccessioniPrimary (citable) accession number: Q96NI6
    Secondary accession number(s): B3KU78, Q86XL2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3