LRFN5_HUMAN
ID LRFN5_HUMAN Reviewed; 719 AA.
AC Q96NI6; B3KU78; Q86XL2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 5;
DE Flags: Precursor;
GN Name=LRFN5; Synonyms=C14orf146, SALM5;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
RN [4]
RP LACK OF INTERACTION WITH DLG1; DLG2; DLG3 AND DLG4.
RX PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
RA Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H., Kaang B.-K.,
RA Kim E.;
RT "SALM synaptic cell adhesion-like molecules regulate the differentiation of
RT excitatory synapses.";
RL Neuron 50:233-245(2006).
RN [5]
RP FUNCTION, AND INTERACTION WITH LRFN1; LRFN2; LRFN3; LRFN4 AND LRFN5.
RX PubMed=18227064; DOI=10.1074/jbc.m709456200;
RA Seabold G.K., Wang P.Y., Chang K., Wang C.Y., Wang Y.X., Petralia R.S.,
RA Wenthold R.J.;
RT "The SALM family of adhesion-like molecules forms heteromeric and homomeric
RT complexes.";
RL J. Biol. Chem. 283:8395-8405(2008).
RN [6]
RP FUNCTION.
RX PubMed=18585462; DOI=10.1016/j.mcn.2008.05.019;
RA Wang P.Y., Seabold G.K., Wenthold R.J.;
RT "Synaptic adhesion-like molecules (SALMs) promote neurite outgrowth.";
RL Mol. Cell. Neurosci. 39:83-94(2008).
CC -!- FUNCTION: Cell adhesion molecule that mediates homophilic cell-cell
CC adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in
CC hippocampal neurons. {ECO:0000269|PubMed:18227064,
CC ECO:0000269|PubMed:18585462}.
CC -!- SUBUNIT: Can form heteromeric complexes with LRFN1, LRFN2, LRFN3 and
CC LFRN4. Able to form homomeric complexes across cell junctions, between
CC adjacent cells. Does not interact with DLG1, DLG2, DLG3 and DLG4.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DOMAIN: Lacks a cytoplasmic PDZ-binding motif, which has been
CC implicated in function of related LRFN proteins.
CC -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
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DR EMBL; AK055365; BAB70910.1; -; mRNA.
DR EMBL; AK096627; BAG53340.1; -; mRNA.
DR EMBL; AL138498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC043165; AAH43165.1; -; mRNA.
DR CCDS; CCDS9678.1; -.
DR RefSeq; NP_001333102.1; NM_001346173.1.
DR RefSeq; NP_689660.2; NM_152447.4.
DR RefSeq; XP_016876537.1; XM_017021048.1.
DR PDB; 5XNP; X-ray; 3.73 A; A/B=18-374.
DR PDB; 5XNQ; X-ray; 2.80 A; A=18-375.
DR PDB; 5XWS; X-ray; 3.08 A; A=18-379.
DR PDB; 5XWT; X-ray; 4.18 A; B/D=18-379.
DR PDBsum; 5XNP; -.
DR PDBsum; 5XNQ; -.
DR PDBsum; 5XWS; -.
DR PDBsum; 5XWT; -.
DR AlphaFoldDB; Q96NI6; -.
DR SMR; Q96NI6; -.
DR BioGRID; 126923; 1.
DR STRING; 9606.ENSP00000298119; -.
DR GlyGen; Q96NI6; 6 sites.
DR iPTMnet; Q96NI6; -.
DR PhosphoSitePlus; Q96NI6; -.
DR BioMuta; LRFN5; -.
DR DMDM; 116242620; -.
DR jPOST; Q96NI6; -.
DR MassIVE; Q96NI6; -.
DR PaxDb; Q96NI6; -.
DR PeptideAtlas; Q96NI6; -.
DR PRIDE; Q96NI6; -.
DR ProteomicsDB; 77517; -.
DR Antibodypedia; 78; 72 antibodies from 23 providers.
DR DNASU; 145581; -.
DR Ensembl; ENST00000298119.9; ENSP00000298119.4; ENSG00000165379.14.
DR GeneID; 145581; -.
DR KEGG; hsa:145581; -.
DR MANE-Select; ENST00000298119.9; ENSP00000298119.4; NM_152447.5; NP_689660.2.
DR UCSC; uc001wvm.5; human.
DR CTD; 145581; -.
DR DisGeNET; 145581; -.
DR GeneCards; LRFN5; -.
DR HGNC; HGNC:20360; LRFN5.
DR HPA; ENSG00000165379; Tissue enhanced (brain, parathyroid gland).
DR MIM; 612811; gene.
DR neXtProt; NX_Q96NI6; -.
DR OpenTargets; ENSG00000165379; -.
DR PharmGKB; PA134888453; -.
DR VEuPathDB; HostDB:ENSG00000165379; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000158296; -.
DR HOGENOM; CLU_016998_0_0_1; -.
DR InParanoid; Q96NI6; -.
DR OMA; NGQHKAT; -.
DR OrthoDB; 151757at2759; -.
DR PhylomeDB; Q96NI6; -.
DR TreeFam; TF350185; -.
DR PathwayCommons; Q96NI6; -.
DR SIGNOR; Q96NI6; -.
DR BioGRID-ORCS; 145581; 6 hits in 1067 CRISPR screens.
DR ChiTaRS; LRFN5; human.
DR GenomeRNAi; 145581; -.
DR Pharos; Q96NI6; Tbio.
DR PRO; PR:Q96NI6; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q96NI6; protein.
DR Bgee; ENSG00000165379; Expressed in middle temporal gyrus and 135 other tissues.
DR ExpressionAtlas; Q96NI6; baseline and differential.
DR Genevisible; Q96NI6; HS.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IBA:GO_Central.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; IBA:GO_Central.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:0043031; P:negative regulation of macrophage activation; ISS:UniProtKB.
DR GO; GO:1905606; P:regulation of presynapse assembly; IBA:GO_Central.
DR GO; GO:0099560; P:synaptic membrane adhesion; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.80.10.10; -; 2.
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; IPR026879; Lrfn5.
DR InterPro; IPR026906; LRR_5.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR45842:SF10; PTHR45842:SF10; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13306; LRR_5; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..719
FT /note="Leucine-rich repeat and fibronectin type-III domain-
FT containing protein 5"
FT /id="PRO_0000014845"
FT TOPO_DOM 18..529
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 551..719
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..51
FT /note="LRRNT"
FT REPEAT 52..73
FT /note="LRR 1"
FT REPEAT 76..97
FT /note="LRR 2"
FT REPEAT 100..121
FT /note="LRR 3"
FT REPEAT 124..145
FT /note="LRR 4"
FT REPEAT 148..169
FT /note="LRR 5"
FT REPEAT 172..193
FT /note="LRR 6"
FT REPEAT 196..217
FT /note="LRR 7"
FT DOMAIN 240..286
FT /note="LRRCT"
FT DOMAIN 287..373
FT /note="Ig-like"
FT DOMAIN 414..503
FT /note="Fibronectin type-III"
FT REGION 385..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
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 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 308..357
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 544
FT /note="F -> L (in Ref. 1; BAG53340)"
FT /evidence="ECO:0000305"
FT CONFLICT 679
FT /note="A -> V (in Ref. 1; BAB70910)"
FT /evidence="ECO:0000305"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:5XNQ"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5XNQ"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:5XNQ"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:5XWS"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5XNQ"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5XNQ"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:5XNQ"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:5XNQ"
FT TURN 140..145
FT /evidence="ECO:0007829|PDB:5XNQ"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:5XNQ"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:5XNQ"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:5XNQ"
FT TURN 188..193
FT /evidence="ECO:0007829|PDB:5XNQ"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:5XNQ"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:5XNQ"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:5XNQ"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:5XNQ"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:5XNQ"
FT HELIX 249..253
FT /evidence="ECO:0007829|PDB:5XNQ"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:5XNQ"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:5XNQ"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:5XNQ"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:5XNQ"
SQ SEQUENCE 719 AA; 79445 MW; DD92951A9705FF4B CRC64;
MEKILFYLFL IGIAVKAQIC PKRCVCQILS PNLATLCAKK GLLFVPPNID RRTVELRLAD
NFVTNIKRKD FANMTSLVDL TLSRNTISFI TPHAFADLRN LRALHLNSNR LTKITNDMFS
GLSNLHHLIL NNNQLTLISS TAFDDVFALE ELDLSYNNLE TIPWDAVEKM VSLHTLSLDH
NMIDNIPKGT FSHLHKMTRL DVTSNKLQKL PPDPLFQRAQ VLATSGIISP STFALSFGGN
PLHCNCELLW LRRLSREDDL ETCASPPLLT GRYFWSIPEE EFLCEPPLIT RHTHEMRVLE
GQRATLRCKA RGDPEPAIHW ISPEGKLISN ATRSLVYDNG TLDILITTVK DTGAFTCIAS
NPAGEATQIV DLHIIKLPHL LNSTNHIHEP DPGSSDISTS TKSGSNTSSS NGDTKLSQDK
IVVAEATSST ALLKFNFQRN IPGIRMFQIQ YNGTYDDTLV YRMIPPTSKT FLVNNLAAGT
MYDLCVLAIY DDGITSLTAT RVVGCIQFTT EQDYVRCHFM QSQFLGGTMI IIIGGIIVAS
VLVFIIILMI RYKVCNNNGQ HKVTKVSNVY SQTNGAQIQG CSVTLPQSVS KQAVGHEENA
QCCKATSDNV IQSSETCSSQ DSSTTTSALP PSWTSSTSVS QKQKRKTGTK PSTEPQNEAV
TNVESQNTNR NNSTALQLAS RPPDSVTEGP TSKRAHIKPN ALLTNVDQIV QETQRLELI
