FNDC5_RAT
ID FNDC5_RAT Reviewed; 209 AA.
AC Q8K3V5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Fibronectin type III domain-containing protein 5;
DE Contains:
DE RecName: Full=Irisin;
DE Flags: Precursor;
GN Name=Fndc5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-209.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Desai B.J., McKinney K.Q., Meyer M.H., Bahrani-Mostafavi Z.,
RA Meyer R.A. Jr.;
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: [Irisin]: Mediates beneficial effects of muscular exercise.
CC Induces browning of white adipose tissue by stimulating UCP1
CC expression, at least in part, via the nuclear receptor PPARA (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}. Note=Imported in
CC peroxisomes through the PEX5 receptor pathway.
CC -!- SUBCELLULAR LOCATION: [Irisin]: Secreted {ECO:0000250}. Note=Detected
CC in the blood of individuals subjected to endurance exercise.
CC {ECO:0000250}.
CC -!- PTM: N-Glycosylated. {ECO:0000250}.
CC -!- PTM: The extracellular domain is cleaved and released from the cell
CC membrane. {ECO:0000250}.
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DR EMBL; AABR03042295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03047757; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF529211; AAM94408.1; -; mRNA.
DR RefSeq; NP_001257910.1; NM_001270981.1.
DR AlphaFoldDB; Q8K3V5; -.
DR SMR; Q8K3V5; -.
DR STRING; 10116.ENSRNOP00000048830; -.
DR GlyGen; Q8K3V5; 2 sites.
DR iPTMnet; Q8K3V5; -.
DR PhosphoSitePlus; Q8K3V5; -.
DR PaxDb; Q8K3V5; -.
DR PRIDE; Q8K3V5; -.
DR GeneID; 260327; -.
DR KEGG; rno:260327; -.
DR CTD; 252995; -.
DR RGD; 708525; Fndc5.
DR VEuPathDB; HostDB:ENSRNOG00000030238; -.
DR eggNOG; ENOG502QQCU; Eukaryota.
DR HOGENOM; CLU_089166_1_0_1; -.
DR InParanoid; Q8K3V5; -.
DR OMA; TTHSCAL; -.
DR OrthoDB; 1198350at2759; -.
DR PhylomeDB; Q8K3V5; -.
DR TreeFam; TF325415; -.
DR PRO; PR:Q8K3V5; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000030238; Expressed in heart and 20 other tissues.
DR Genevisible; Q8K3V5; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0090336; P:positive regulation of brown fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0014850; P:response to muscle activity; ISS:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR032073; FNDC5_C.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF16066; DUF4808; 1.
DR Pfam; PF00041; fn3; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Hormone; Membrane; Peroxisome;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..209
FT /note="Fibronectin type III domain-containing protein 5"
FT /id="PRO_0000328973"
FT CHAIN 29..140
FT /note="Irisin"
FT /id="PRO_0000415859"
FT TOPO_DOM 29..149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..209
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..124
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 179..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 207..209
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 179..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 209 AA; 23321 MW; 86A33DE8E4616507 CRC64;
MPPGPCAWPP RAALRLWLGC VCFALVQADS PSAPVNVTVR HLKANSAVVS WDVLEDEVVI
GFAISQQKKD VRMLRFIQEV NTTTRSCALW DLEEDTEYIV HVQAISIQGQ SPASEPVLFK
TPREAEKMAS KNKDEVTMKE MGRNQQLRTG EVLIIVVVLF MWAGVIALFC RQYDIIKDNE
PNNNKEKTKS ASETSTPEHQ GGGLLRSKI
