GenomeNet

Database: UniProt
Entry: Q501P1
LinkDB: Q501P1
Original site: Q501P1 
ID   FBLN7_MOUSE             Reviewed;         440 AA.
AC   Q501P1; Q9DAW5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   10-APR-2019, entry version 116.
DE   RecName: Full=Fibulin-7;
DE            Short=FIBL-7;
DE   AltName: Full=Protein TM14;
DE   Flags: Precursor;
GN   Name=Fbln7; Synonyms=Tm14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, GLYCOSYLATION, AND INTERACTION WITH HEPARIN;
RP   FBLN1; FN1 AND DSPP.
RC   TISSUE=Incisor;
RX   PubMed=17699513; DOI=10.1074/jbc.M705847200;
RA   de Vega S., Iwamoto T., Nakamura T., Hozumi K., McKnight D.A.,
RA   Fisher L.W., Fukumoto S., Yamada Y.;
RT   "TM14 is a new member of the fibulin family (fibulin-7) that interacts
RT   with extracellular matrix molecules and is active for cell binding.";
RL   J. Biol. Chem. 282:30878-30888(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: An adhesion molecule that interacts with extracellular
CC       matrix molecules in developing teeth and may play important roles
CC       in differentiation and maintenance of odontoblasts as well as in
CC       dentin formation. {ECO:0000269|PubMed:17699513}.
CC   -!- SUBUNIT: Interacts with heparin, FBLN1, FN1 and DSPP.
CC       Preferentially binds dental mesenchyme cells and odontoblasts but
CC       not dental epithelial cells or nondental cells. Binding requires a
CC       heparan sulfate-containing receptor on the cell surface as well as
CC       an integrin. {ECO:0000269|PubMed:17699513}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- TISSUE SPECIFICITY: Highly expressed in newborn incisors and
CC       molars. A weaker expression is seen in the brain, kidneys, muscles
CC       and bones. {ECO:0000269|PubMed:17699513}.
CC   -!- DEVELOPMENTAL STAGE: Expressed by preodontoblasts and odontoblasts
CC       in developing teeth. Localizes to the apical pericellular regions
CC       of preodontoblasts. When the dentin matrix is fully formed and
CC       dentin mineralization occurs, it is present in the predentin
CC       matrix and along the dentinal tubules. It is also expressed in the
CC       developing growth plate cartilage, hair follicles and
CC       extraembryonic areas of the placenta.
CC       {ECO:0000269|PubMed:17699513}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17699513}.
CC   -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABU48629.1; Type=Frameshift; Positions=186, 189, 195; Evidence={ECO:0000305};
CC       Sequence=BAB24056.1; Type=Frameshift; Positions=186, 189, 195; Evidence={ECO:0000305};
DR   EMBL; EF668007; ABU48629.1; ALT_FRAME; mRNA.
DR   EMBL; AK005465; BAB24056.1; ALT_FRAME; mRNA.
DR   EMBL; AL808104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC095941; AAH95941.1; -; mRNA.
DR   CCDS; CCDS38235.1; -.
DR   RefSeq; NP_077199.2; NM_024237.4.
DR   UniGene; Mm.5107; -.
DR   ProteinModelPortal; Q501P1; -.
DR   SMR; Q501P1; -.
DR   STRING; 10090.ENSMUSP00000105953; -.
DR   PhosphoSitePlus; Q501P1; -.
DR   PaxDb; Q501P1; -.
DR   PeptideAtlas; Q501P1; -.
DR   PRIDE; Q501P1; -.
DR   Ensembl; ENSMUST00000028864; ENSMUSP00000028864; ENSMUSG00000027386.
DR   Ensembl; ENSMUST00000110324; ENSMUSP00000105953; ENSMUSG00000027386.
DR   GeneID; 70370; -.
DR   KEGG; mmu:70370; -.
DR   UCSC; uc008mgy.1; mouse.
DR   CTD; 129804; -.
DR   MGI; MGI:1917620; Fbln7.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; ENOG410XP6K; LUCA.
DR   GeneTree; ENSGT00830000128368; -.
DR   HOGENOM; HOG000089983; -.
DR   HOVERGEN; HBG107003; -.
DR   InParanoid; Q501P1; -.
DR   KO; K17342; -.
DR   OMA; CPMDSRS; -.
DR   OrthoDB; 626946at2759; -.
DR   PhylomeDB; Q501P1; -.
DR   TreeFam; TF330076; -.
DR   PRO; PR:Q501P1; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000027386; Expressed in 125 organ(s), highest expression level in placenta.
DR   Genevisible; Q501P1; MM.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd00033; CCP; 1.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   SMART; SM00032; CCP; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 3.
DR   SUPFAM; SSF57535; SSF57535; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS50923; SUSHI; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Coiled coil; Complete proteome;
KW   Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Heparin-binding; Reference proteome; Repeat; Secreted; Signal; Sushi.
FT   SIGNAL        1     24       {ECO:0000255}.
FT   CHAIN        25    440       Fibulin-7.
FT                                /FTId=PRO_0000313656.
FT   DOMAIN       79    136       Sushi. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      136    172       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      225    270       EGF-like 2; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      271    320       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   COILED       28     73       {ECO:0000255}.
FT   CARBOHYD    124    124       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    308    308       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     81    121       {ECO:0000250}.
FT   DISULFID    107    134       {ECO:0000250}.
FT   DISULFID    140    151       {ECO:0000250}.
FT   DISULFID    145    160       {ECO:0000250}.
FT   DISULFID    162    171       {ECO:0000250}.
FT   DISULFID    229    245       {ECO:0000250}.
FT   DISULFID    241    254       {ECO:0000250}.
FT   DISULFID    256    269       {ECO:0000250}.
FT   DISULFID    275    288       {ECO:0000250}.
FT   DISULFID    282    297       {ECO:0000250}.
FT   DISULFID    302    319       {ECO:0000250}.
FT   CONFLICT     54     54       G -> A (in Ref. 1; ABU48629 and 2;
FT                                BAB24056). {ECO:0000305}.
FT   CONFLICT    170    170       R -> G (in Ref. 1; ABU48629 and 2;
FT                                BAB24056). {ECO:0000305}.
SQ   SEQUENCE   440 AA;  47927 MW;  AC79BC5D1D077DF9 CRC64;
     MGPGSQRALF LLLLLLASPG ARAFQSCLNK QQLLTTIRQL QQLLKGQETR FTEGIRNMKS
     RLAALQNTVN KMTPDAPPVS CPALEAPPDG KKFGSKYLVD HEVYFTCNPG FQLVGPSSVV
     CLANGSWTGE QPRCRDISEC SSQPCHNGGT CVEGINHYRC ICPPGKTGNR CQHQTQAAAP
     DGGEAGDPAF SRAPRCAQVE REQHCSCEAG FHLSSTTGGH SVCQDVNECE IYGQKGRPRL
     CMHACVNTPG SYRCTCPSGY RILADGKSCE DVDECAGPQH MCPRGTTCIN TGGGFQCVNP
     ECPEGSGNIS YVKTSPFQCE RNPCPMDSRP CRHLPKTISF HYLSLPSKLK TPITLFRMAT
     ASIPGHPGPN SLRFGIVGGN SRGHFVMQRS DRQTGELILT QTLEGPQTLE VDVDMSEYLE
     RSFQANHVSK VTIFVSRYDF
//
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