FBLN7_HUMAN
ID FBLN7_HUMAN Reviewed; 439 AA.
AC Q53RD9; A0JNV1; A0JNV2; Q5H9P5; Q8N9G0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Fibulin-7;
DE Short=FIBL-7;
DE Flags: Precursor;
GN Name=FBLN7; Synonyms=TM14;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-119.
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Ovary;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-176 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
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:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q53RD9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q53RD9-2; Sequence=VSP_030086;
CC Name=3;
CC IsoId=Q53RD9-3; Sequence=VSP_030084;
CC Name=4;
CC IsoId=Q53RD9-4; Sequence=VSP_030085;
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
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DR EMBL; AK094759; BAC04416.1; -; mRNA.
DR EMBL; AC092645; AAY14854.1; -; Genomic_DNA.
DR EMBL; CH471245; EAW52100.1; -; Genomic_DNA.
DR EMBL; BC035784; AAH35784.1; -; mRNA.
DR EMBL; BC126986; AAI26987.1; -; mRNA.
DR EMBL; BC126987; AAI26988.1; -; mRNA.
DR EMBL; CR933697; CAI46168.1; -; mRNA.
DR CCDS; CCDS2095.1; -. [Q53RD9-1]
DR CCDS; CCDS46391.1; -. [Q53RD9-2]
DR RefSeq; NP_001121637.1; NM_001128165.1. [Q53RD9-2]
DR RefSeq; NP_694946.2; NM_153214.2. [Q53RD9-1]
DR AlphaFoldDB; Q53RD9; -.
DR BioGRID; 126208; 20.
DR IntAct; Q53RD9; 4.
DR STRING; 9606.ENSP00000331411; -.
DR GlyConnect; 1246; 1 N-Linked glycan (1 site).
DR GlyGen; Q53RD9; 3 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q53RD9; -.
DR PhosphoSitePlus; Q53RD9; -.
DR BioMuta; FBLN7; -.
DR DMDM; 74726569; -.
DR jPOST; Q53RD9; -.
DR MassIVE; Q53RD9; -.
DR PaxDb; Q53RD9; -.
DR PeptideAtlas; Q53RD9; -.
DR PRIDE; Q53RD9; -.
DR ProteomicsDB; 62519; -. [Q53RD9-1]
DR ProteomicsDB; 62520; -. [Q53RD9-2]
DR ProteomicsDB; 62521; -. [Q53RD9-3]
DR ProteomicsDB; 62522; -. [Q53RD9-4]
DR Antibodypedia; 33261; 138 antibodies from 21 providers.
DR DNASU; 129804; -.
DR Ensembl; ENST00000331203.7; ENSP00000331411.2; ENSG00000144152.13. [Q53RD9-1]
DR Ensembl; ENST00000409450.7; ENSP00000387000.3; ENSG00000144152.13. [Q53RD9-2]
DR Ensembl; ENST00000409667.7; ENSP00000386822.3; ENSG00000144152.13. [Q53RD9-4]
DR GeneID; 129804; -.
DR KEGG; hsa:129804; -.
DR MANE-Select; ENST00000331203.7; ENSP00000331411.2; NM_153214.3; NP_694946.2.
DR UCSC; uc002tho.2; human. [Q53RD9-1]
DR CTD; 129804; -.
DR DisGeNET; 129804; -.
DR GeneCards; FBLN7; -.
DR HGNC; HGNC:26740; FBLN7.
DR HPA; ENSG00000144152; Low tissue specificity.
DR MIM; 611551; gene.
DR neXtProt; NX_Q53RD9; -.
DR OpenTargets; ENSG00000144152; -.
DR PharmGKB; PA162388107; -.
DR VEuPathDB; HostDB:ENSG00000144152; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00830000128368; -.
DR HOGENOM; CLU_043541_0_0_1; -.
DR InParanoid; Q53RD9; -.
DR OMA; GNNRGHF; -.
DR OrthoDB; 626946at2759; -.
DR PhylomeDB; Q53RD9; -.
DR TreeFam; TF330076; -.
DR PathwayCommons; Q53RD9; -.
DR SignaLink; Q53RD9; -.
DR BioGRID-ORCS; 129804; 14 hits in 1069 CRISPR screens.
DR ChiTaRS; FBLN7; human.
DR GenomeRNAi; 129804; -.
DR Pharos; Q53RD9; Tbio.
DR PRO; PR:Q53RD9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q53RD9; protein.
DR Bgee; ENSG00000144152; Expressed in secondary oocyte and 123 other tissues.
DR ExpressionAtlas; Q53RD9; baseline and differential.
DR Genevisible; Q53RD9; HS.
DR GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IEA:Ensembl.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0110151; P:positive regulation of biomineralization; IEA:Ensembl.
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; 2.
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 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell adhesion; Coiled coil; Disulfide bond;
KW EGF-like domain; Extracellular matrix; Glycoprotein; Heparin-binding;
KW Reference proteome; Repeat; Secreted; Signal; Sushi.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..439
FT /note="Fibulin-7"
FT /id="PRO_0000313655"
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 224..269
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 270..319
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT COILED 28..53
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
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 228..244
FT /evidence="ECO:0000250"
FT DISULFID 240..253
FT /evidence="ECO:0000250"
FT DISULFID 255..268
FT /evidence="ECO:0000250"
FT DISULFID 274..287
FT /evidence="ECO:0000250"
FT DISULFID 281..296
FT /evidence="ECO:0000250"
FT DISULFID 301..318
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..57
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_030084"
FT VAR_SEQ 136..269
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030085"
FT VAR_SEQ 178..223
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030086"
FT VARIANT 119
FT /note="V -> M (in dbSNP:rs35586251)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_037689"
SQ SEQUENCE 439 AA; 47376 MW; 905C12B76B78E2EE CRC64;
MVPSSPRALF LLLLILACPE PRASQNCLSK QQLLSAIRQL QQLLKGQETR FAEGIRHMKS
RLAALQNSVG RVGPDALPVS CPALNTPADG RKFGSKYLVD HEVHFTCNPG FRLVGPSSVV
CLPNGTWTGE QPHCRGISEC SSQPCQNGGT CVEGVNQYRC ICPPGRTGNR CQHQAQTAAP
EGSVAGDSAF SRAPRCAQVE RAQHCSCEAG FHLSGAAGDS VCQDVNECEL YGQEGRPRLC
MHACVNTPGS YRCTCPGGYR TLADGKSCED VDECVGLQPV CPQGTTCINT GGSFQCVSPE
CPEGSGNVSY VKTSPFQCER NPCPMDSRPC RHLPKTISFH YLSLPSNLKT PITLFRMATA
SAPGRAGPNS LRFGIVGGNS RGHFVMQRSD RQTGDLILVQ NLEGPQTLEV DVDMSEYLDR
SFQANHVSKV TIFVSPYDF
