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LRFN5_MOUSE
ID   LRFN5_MOUSE             Reviewed;         719 AA.
AC   Q8BXA0; Q5DTH4; Q8BJH4; Q8BZL0;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 5;
DE   Flags: Precursor;
GN   Name=Lrfn5; Synonyms=Kiaa4208, Salm5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, and Embryonic head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; 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   DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, GLYCOSYLATION, LACK OF INTERACTION
RP   WITH DLG4, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=16828986; DOI=10.1016/j.gene.2006.05.014;
RA   Morimura N., Inoue T., Katayama K., Aruga J.;
RT   "Comparative analysis of structure, expression and PSD95-binding capacity
RT   of Lrfn, a novel family of neuronal transmembrane proteins.";
RL   Gene 380:72-83(2006).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Can form heteromeric complexes with LRFN1, LRFN2, LRFN3 and
CC       LFRN4 (By similarity). Able to form homomeric complexes across cell
CC       junctions, between adjacent cells (By similarity). Does not interact
CC       with DLG1, DLG2 or DLG3 (By similarity). Does not interact with DLG4.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:16828986}; Single-
CC       pass type I membrane protein {ECO:0000269|PubMed:16828986}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BXA0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BXA0-2; Sequence=VSP_009299;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the brain, with a weak,
CC       but broad expression in the cerebral cortex and diencephalic nuclei.
CC       Strongly expressed in both the pyramidal layer and the dentate gyrus of
CC       the hippocampus. Also detected in other parts of the central nervous
CC       system, including the olfactory bulb, pons, cerebellum, and medulla
CC       oblongata, as well as in the peripheral nervous system, such as the
CC       ganglia of cranial nerves and the dorsal root ganglion during
CC       gestation. {ECO:0000269|PubMed:16828986}.
CC   -!- DEVELOPMENTAL STAGE: Expression starts around 11.5-12.5 dpc. At 11.5
CC       dpc, detected in the outer layer of the telencephalic vesicles. This
CC       pattern of expression continues until 17.5 dpc with expression in the
CC       cortical plate, but not in the inner layer of the cerebral cortex,
CC       including subplate, ventricular zone, and subventricular zone. As also
CC       detected in the hippocampus, amygdala and widely in diencephalic
CC       nuclei. {ECO:0000269|PubMed:16828986}.
CC   -!- DOMAIN: Lacks a cytoplasmic PDZ-binding motif, which has been
CC       implicated in function of related LRFN proteins.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:16828986}.
CC   -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the LRFN family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90535.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK034245; BAC28645.1; -; mRNA.
DR   EMBL; AK048443; BAC33339.1; -; mRNA.
DR   EMBL; AK220546; BAD90535.1; ALT_INIT; mRNA.
DR   EMBL; BC052038; AAH52038.1; -; mRNA.
DR   CCDS; CCDS25936.1; -. [Q8BXA0-2]
DR   CCDS; CCDS79117.1; -. [Q8BXA0-1]
DR   RefSeq; NP_001297515.1; NM_001310586.1. [Q8BXA0-1]
DR   RefSeq; NP_848829.2; NM_178714.5. [Q8BXA0-2]
DR   RefSeq; XP_006515893.1; XM_006515830.2. [Q8BXA0-2]
DR   RefSeq; XP_006515894.1; XM_006515831.3. [Q8BXA0-2]
DR   RefSeq; XP_017170545.1; XM_017315056.1. [Q8BXA0-1]
DR   PDB; 6F2O; X-ray; 3.00 A; A=18-376.
DR   PDBsum; 6F2O; -.
DR   AlphaFoldDB; Q8BXA0; -.
DR   SASBDB; Q8BXA0; -.
DR   SMR; Q8BXA0; -.
DR   STRING; 10090.ENSMUSP00000051546; -.
DR   GlyConnect; 2424; 3 N-Linked glycans (1 site). [Q8BXA0-2]
DR   GlyGen; Q8BXA0; 6 sites, 3 N-linked glycans (1 site).
DR   iPTMnet; Q8BXA0; -.
DR   PhosphoSitePlus; Q8BXA0; -.
DR   PaxDb; Q8BXA0; -.
DR   PeptideAtlas; Q8BXA0; -.
DR   PRIDE; Q8BXA0; -.
DR   ProteomicsDB; 290167; -. [Q8BXA0-1]
DR   ProteomicsDB; 290168; -. [Q8BXA0-2]
DR   ABCD; Q8BXA0; 1 sequenced antibody.
DR   Antibodypedia; 78; 72 antibodies from 23 providers.
DR   Ensembl; ENSMUST00000055815; ENSMUSP00000051546; ENSMUSG00000035653. [Q8BXA0-2]
DR   Ensembl; ENSMUST00000119481; ENSMUSP00000113123; ENSMUSG00000035653. [Q8BXA0-1]
DR   GeneID; 238205; -.
DR   KEGG; mmu:238205; -.
DR   UCSC; uc007nqm.1; mouse. [Q8BXA0-2]
DR   UCSC; uc007nqn.1; mouse. [Q8BXA0-1]
DR   CTD; 145581; -.
DR   MGI; MGI:2144814; Lrfn5.
DR   VEuPathDB; HostDB:ENSMUSG00000035653; -.
DR   eggNOG; KOG0619; Eukaryota.
DR   GeneTree; ENSGT00940000158296; -.
DR   HOGENOM; CLU_016998_0_0_1; -.
DR   InParanoid; Q8BXA0; -.
DR   OMA; NGQHKAT; -.
DR   OrthoDB; 151757at2759; -.
DR   PhylomeDB; Q8BXA0; -.
DR   TreeFam; TF350185; -.
DR   BioGRID-ORCS; 238205; 2 hits in 57 CRISPR screens.
DR   ChiTaRS; Lrfn5; mouse.
DR   PRO; PR:Q8BXA0; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q8BXA0; protein.
DR   Bgee; ENSMUSG00000035653; Expressed in cortical plate and 98 other tissues.
DR   Genevisible; Q8BXA0; MM.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:MGI.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:0043031; P:negative regulation of macrophage activation; IMP:UniProtKB.
DR   GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR   GO; GO:0099560; P:synaptic membrane adhesion; ISO:MGI.
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; Alternative splicing; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Leucine-rich repeat; Membrane; Reference proteome;
KW   Repeat; Signal; 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_0000014846"
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..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..416
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   VAR_SEQ         700..719
FT                   /note="NALLTNVDQNVQETQRLESI -> SKFLTVPAEGSRARHRASLSGGLKDSFH
FT                   YGNSQLSLKRSMSMNAMWT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_009299"
FT   STRAND          32..36
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   STRAND          54..57
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   HELIX           68..71
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   TURN            92..97
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   TURN            116..121
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   HELIX           140..143
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   STRAND          150..153
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   HELIX           164..167
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   HELIX           249..253
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   TURN            266..268
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   STRAND          269..274
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   STRAND          285..292
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   STRAND          304..314
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   STRAND          317..322
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   TURN            338..340
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   STRAND          341..344
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   HELIX           349..351
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   STRAND          355..361
FT                   /evidence="ECO:0007829|PDB:6F2O"
FT   STRAND          364..370
FT                   /evidence="ECO:0007829|PDB:6F2O"
SQ   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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