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Protein

Fibronectin type III domain-containing protein 1

Gene

Fndc1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be an activator of G protein signaling.1 Publication

GO - Biological processi

  • cellular response to hypoxia Source: MGI
  • positive regulation of cardiac muscle cell apoptotic process Source: MGI
  • positive regulation of protein phosphorylation Source: MGI
  • regulation of protein transport Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Fibronectin type III domain-containing protein 1
Alternative name(s):
Activator of G-protein signaling 8
Gene namesi
Name:Fndc1
Synonyms:Ags8
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi1310640. Fndc1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell junction Source: MGI
  • cytoplasm Source: MGI
  • extracellular region Source: UniProtKB-SubCell
  • mitochondrial membrane Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence analysisAdd
BLAST
Chaini30 – 17791750Fibronectin type III domain-containing protein 1PRO_0000284832Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei651 – 6511PhosphoserineCombined sources
Modified residuei699 – 6991PhosphoserineCombined sources
Glycosylationi1546 – 15461N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ2Q0I9.
PRIDEiQ2Q0I9.

PTM databases

iPTMnetiQ2Q0I9.
PhosphoSiteiQ2Q0I9.

Expressioni

Inductioni

By ischemia.1 Publication

Gene expression databases

ExpressionAtlasiQ2Q0I9. baseline and differential.
GenevisibleiQ2Q0I9. RN.

Interactioni

Protein-protein interaction databases

DIPiDIP-61094N.
STRINGi10116.ENSRNOP00000029878.

Structurei

3D structure databases

ProteinModelPortaliQ2Q0I9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 12694Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini103 – 203101Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini207 – 30296Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini307 – 40296Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini1543 – 163795Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi557 – 693137Ser-richAdd
BLAST
Compositional biasi1325 – 140177Thr-richAdd
BLAST

Sequence similaritiesi

Contains 5 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG4221. Eukaryota.
ENOG410Z913. LUCA.
GeneTreeiENSGT00530000063558.
HOGENOMiHOG000082445.
HOVERGENiHBG107924.
InParanoidiQ2Q0I9.
OMAiNLNVWPV.
OrthoDBiEOG7MH0XD.
PhylomeDBiQ2Q0I9.
TreeFamiTF337588.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00041. fn3. 3 hits.
[Graphical view]
SMARTiSM00060. FN3. 3 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 4 hits.
PROSITEiPS50853. FN3. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q2Q0I9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPEARASPR LLLRAALLLL AALLPVASSA GPPVDHPLKP RHVKLLSANM
60 70 80 90 100
GLKVTWDPPK DATSRPVEHY NIAYGKSLKS LKSIKVNAET HSFLIKDVEK
110 120 130 140 150
EVPNKPLRMR VRASDDRLSV AWKAPRLSGA KSPRRSRGFL LGYGESGRKM
160 170 180 190 200
NYVPLTRDER SHEIKKLASE SVYVVSLQST NSQGQSQPVY RAALTKRKNA
210 220 230 240 250
EEDELDVPED ISVRVMSSQS VLVAWVDPLV EKQKRVVASR QYTVRYREKG
260 270 280 290 300
ESARWDYKQV SNRRALVDSL IPDTVYEFAV RISQGERDGK WSASVFQRTP
310 320 330 340 350
ESAPTTAPEN LRVWPVNGKP TVVTVSWDAL PESEGKVKEY ILSYAPALKP
360 370 380 390 400
FGAKSLTFSG HTTSALVDGL QPGERYLFKI RATNRRGQGP HSKAFIVAIP
410 420 430 440 450
TTSSTEASVQ PNGRDNGKPE KPQQPSSSAP KVAASSQHMP PAKNVKDALS
460 470 480 490 500
DLKNKIQTNG VAPGRTQLHS KVGELDPQST EVTGEEELDS LENPRSSRLE
510 520 530 540 550
TLNQKQPLRV PSRSGHGALA PGRTPARAGL PVLSRKEGMD RRGPSLDPHP
560 570 580 590 600
HPRVEPSASS AYHQLSSTDN DSVDRKEDDQ AGSPDPKAAS SGSSPKNPGR
610 620 630 640 650
SRPTSAPSRH AASNMLRDKS RVHPGTKAAS SSTSRQSHSS TSEEDSSAQP
660 670 680 690 700
SRHFPLHRGS STSPLSRGWK DRQDTHASSS HTTSRTASSS HPSALTEGSE
710 720 730 740 750
EEDGGADSDR AAEDTIRRAE ATAQIQQTRP GLGHFSLIRN KPFTPHSRNP
760 770 780 790 800
NRFPRLRGPR LQPSVSPQST SASKVLTRSP SLPASHTRPG SDVYGDGEDE
810 820 830 840 850
EPLPATVIND RTPSYPRHPI SGSSDTLRRG PQRGASLYRK EPIPENSKAA
860 870 880 890 900
GADVPPGGRS PLSSKAQGFQ QSTTDEGAPQ TSPASTSRQP SPARPPASRS
910 920 930 940 950
QPSPGSTVPR RMTPDRSSEL SSSQSKDRSL SQPKLSVAHA GHDHPHTANS
960 970 980 990 1000
RGVLPSAPQN QNEGAQSTYE DNSTEIEGPD SRTPTHSARA KDTTPPILKP
1010 1020 1030 1040 1050
RQVGSQSWSS DNRPQPSQAG ASERPIRPGS THPRAQVPGR AGVQATSVKK
1060 1070 1080 1090 1100
VSPSKRPLPL ESQQSVFAEE EEENEGMLKG KEDSLSTSVK KWPSSSSPRD
1110 1120 1130 1140 1150
KYADRNLDKD KAAIGLLVQE ENTVPGRRPP GSPAIASHPS TRHQPRNPAT
1160 1170 1180 1190 1200
ASPIANTHSW PRYTTRAPSS YSSTTPMLSL RQRMQRRFRT PVSRQPPPPR
1210 1220 1230 1240 1250
PVLTPGYNGR PNAEENIPPG SIGKPNGQRI INGPQGTKWV VDLDRGLVLN
1260 1270 1280 1290 1300
AEGRYLQDSH GNPLRVRLGG DGRTIVDLGG TPMVSPDGLP LFGQGRHGKP
1310 1320 1330 1340 1350
VASAQDKPIL SLGGKPLVGL EVVRTTTQVP TTTMPPSTTT TTVPPTTTLP
1360 1370 1380 1390 1400
PTTTTTRRTT TTRRTTTTRR PTTTTRATRR TTTTTTTPEP TTPSPTCPPG
1410 1420 1430 1440 1450
TLEHRDEAGN LIMGSNGIPE CYPEEDDFSG LEIDTALPTE EDYVVYDDDY
1460 1470 1480 1490 1500
GLETTRPPTS TMPSTTAATP KVVPEQGTVS SFPEEEFDLA GKRRFVAPYV
1510 1520 1530 1540 1550
TYLSKDPAAP CSLTDALDHF QVESLDELIP NDLTKNDLPP QHAPRNITVV
1560 1570 1580 1590 1600
AMEGCHSFVI VDWNKAIPGD VVTGYLVYSA SYEDFIRNKW STQTSSVTHL
1610 1620 1630 1640 1650
PIENLKPNTR YYFKVQAKNP HGYGPVSPSV SFVTESDNPL LVVRPPGGEP
1660 1670 1680 1690 1700
IWIPFAFKHD PGYTDCHGRQ YVKRTWYKKF VGVVLCNSLR YKIYLSDNLK
1710 1720 1730 1740 1750
DTFYSIGDSW GRGEDHCQFV DSHLDGRTGP QSYVEALPTI QGYYRQYRQE
1760 1770
PVSFGHIGFG TPYYYVGWYE CGVSIPGKW
Length:1,779
Mass (Da):194,049
Last modified:November 25, 2008 - v2
Checksum:iB9F21FBEAF3233A4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti439 – 4391M → T in ABB82299 (PubMed:16407149).Curated
Sequence conflicti441 – 4411P → S in ABB82299 (PubMed:16407149).Curated
Sequence conflicti493 – 4931N → D in ABB82299 (PubMed:16407149).Curated
Sequence conflicti1016 – 10161P → R in ABB82299 (PubMed:16407149).Curated
Sequence conflicti1423 – 14231P → L in ABB82299 (PubMed:16407149).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03000391 Genomic DNA. No translation available.
AABR03002558 Genomic DNA. No translation available.
AABR03004065 Genomic DNA. No translation available.
DQ256268 mRNA. Translation: ABB82299.1.
RefSeqiNP_001033704.1. NM_001038615.1.
UniGeneiRn.20633.

Genome annotation databases

EnsembliENSRNOT00000034842; ENSRNOP00000029878; ENSRNOG00000030210.
GeneIDi308099.
KEGGirno:308099.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03000391 Genomic DNA. No translation available.
AABR03002558 Genomic DNA. No translation available.
AABR03004065 Genomic DNA. No translation available.
DQ256268 mRNA. Translation: ABB82299.1.
RefSeqiNP_001033704.1. NM_001038615.1.
UniGeneiRn.20633.

3D structure databases

ProteinModelPortaliQ2Q0I9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-61094N.
STRINGi10116.ENSRNOP00000029878.

PTM databases

iPTMnetiQ2Q0I9.
PhosphoSiteiQ2Q0I9.

Proteomic databases

PaxDbiQ2Q0I9.
PRIDEiQ2Q0I9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000034842; ENSRNOP00000029878; ENSRNOG00000030210.
GeneIDi308099.
KEGGirno:308099.

Organism-specific databases

CTDi84624.
RGDi1310640. Fndc1.

Phylogenomic databases

eggNOGiKOG4221. Eukaryota.
ENOG410Z913. LUCA.
GeneTreeiENSGT00530000063558.
HOGENOMiHOG000082445.
HOVERGENiHBG107924.
InParanoidiQ2Q0I9.
OMAiNLNVWPV.
OrthoDBiEOG7MH0XD.
PhylomeDBiQ2Q0I9.
TreeFamiTF337588.

Miscellaneous databases

NextBioi658338.
PROiQ2Q0I9.

Gene expression databases

ExpressionAtlasiQ2Q0I9. baseline and differential.
GenevisibleiQ2Q0I9. RN.

Family and domain databases

Gene3Di2.60.40.10. 4 hits.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF00041. fn3. 3 hits.
[Graphical view]
SMARTiSM00060. FN3. 3 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 4 hits.
PROSITEiPS50853. FN3. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Identification of a receptor-independent activator of G protein signaling (AGS8) in ischemic heart and its interaction with Gbetagamma."
    Sato M., Cismowski M.J., Toyota E., Smrcka A.V., Lucchesi P.A., Chilian W.M., Lanier S.M.
    Proc. Natl. Acad. Sci. U.S.A. 103:797-802(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 50-1779, FUNCTION, INDUCTION BY ISCHEMIA.
    Strain: Wistar.
    Tissue: Heart.
  3. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-699, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFNDC1_RAT
AccessioniPrimary (citable) accession number: Q2Q0I9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: November 25, 2008
Last modified: February 17, 2016
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-50 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.