FBLN7_MOUSE
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 03-AUG-2022, entry version 133.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, GLYCOSYLATION, AND INTERACTION WITH HEPARIN; 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., Fisher L.W.,
RA Fukumoto S., Yamada Y.;
RT "TM14 is a new member of the fibulin family (fibulin-7) that interacts with
RT 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., 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 [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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: An adhesion molecule that interacts with extracellular matrix
CC molecules in developing teeth and may play important roles in
CC differentiation and maintenance of odontoblasts as well as in dentin
CC formation. {ECO:0000269|PubMed:17699513}.
CC -!- SUBUNIT: Interacts with heparin, FBLN1, FN1 and DSPP. Preferentially
CC binds dental mesenchyme cells and odontoblasts but not dental
CC epithelial cells or nondental cells. Binding requires a heparan
CC sulfate-containing receptor on the cell surface as well as an integrin.
CC {ECO:0000269|PubMed:17699513}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: Highly expressed in newborn incisors and molars. A
CC weaker expression is seen in the brain, kidneys, muscles and bones.
CC {ECO:0000269|PubMed:17699513}.
CC -!- DEVELOPMENTAL STAGE: Expressed by preodontoblasts and odontoblasts in
CC developing teeth. Localizes to the apical pericellular regions of
CC preodontoblasts. When the dentin matrix is fully formed and dentin
CC mineralization occurs, it is present in the predentin matrix and along
CC the dentinal tubules. It is also expressed in the developing growth
CC plate cartilage, hair follicles and extraembryonic areas of the
CC placenta. {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; Evidence={ECO:0000305};
CC Sequence=BAB24056.1; Type=Frameshift; Evidence={ECO:0000305};
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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 AlphaFoldDB; Q501P1; -.
DR BioGRID; 214006; 2.
DR STRING; 10090.ENSMUSP00000105953; -.
DR GlyGen; Q501P1; 2 sites.
DR PhosphoSitePlus; Q501P1; -.
DR PaxDb; Q501P1; -.
DR PeptideAtlas; Q501P1; -.
DR PRIDE; Q501P1; -.
DR ProteomicsDB; 271876; -.
DR Antibodypedia; 33261; 138 antibodies from 21 providers.
DR DNASU; 70370; -.
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 VEuPathDB; HostDB:ENSMUSG00000027386; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00830000128368; -.
DR HOGENOM; CLU_043541_0_0_1; -.
DR InParanoid; Q501P1; -.
DR OMA; GNNRGHF; -.
DR OrthoDB; 626946at2759; -.
DR PhylomeDB; Q501P1; -.
DR TreeFam; TF330076; -.
DR BioGRID-ORCS; 70370; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Fbln7; mouse.
DR PRO; PR:Q501P1; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q501P1; protein.
DR Bgee; ENSMUSG00000027386; Expressed in placenta labyrinth and 133 other tissues.
DR Genevisible; Q501P1; MM.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:MGI.
DR GO; GO:0008201; F:heparin binding; IDA:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0110151; P:positive regulation of biomineralization; IDA:MGI.
DR CDD; cd00033; CCP; 1.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
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; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Heparin-binding; Reference proteome;
KW Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..440
FT /note="Fibulin-7"
FT /id="PRO_0000313656"
FT DOMAIN 79..136
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 136..172
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 225..270
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 271..320
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT COILED 28..73
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 81..121
FT /evidence="ECO:0000250"
FT DISULFID 107..134
FT /evidence="ECO:0000250"
FT DISULFID 140..151
FT /evidence="ECO:0000250"
FT DISULFID 145..160
FT /evidence="ECO:0000250"
FT DISULFID 162..171
FT /evidence="ECO:0000250"
FT DISULFID 229..245
FT /evidence="ECO:0000250"
FT DISULFID 241..254
FT /evidence="ECO:0000250"
FT DISULFID 256..269
FT /evidence="ECO:0000250"
FT DISULFID 275..288
FT /evidence="ECO:0000250"
FT DISULFID 282..297
FT /evidence="ECO:0000250"
FT DISULFID 302..319
FT /evidence="ECO:0000250"
FT CONFLICT 54
FT /note="G -> A (in Ref. 1; ABU48629 and 2; BAB24056)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="R -> G (in Ref. 1; ABU48629 and 2; BAB24056)"
FT /evidence="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
