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Protein

Fibulin-7

Gene

FBLN7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

An adhesion molecule that interacts with extracellular matrix molecules in developing teeth and may play important roles in differentiation and maintenance of odontoblasts as well as in dentin formation.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fibulin-7
Short name:
FIBL-7
Gene namesi
Name:FBLN7
Synonyms:TM14
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:26740. FBLN7.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162388107.

Polymorphism and mutation databases

BioMutaiFBLN7.
DMDMi74726569.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 439415Fibulin-7PRO_0000313655Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi81 ↔ 121By similarity
Disulfide bondi107 ↔ 134By similarity
Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi140 ↔ 151By similarity
Disulfide bondi145 ↔ 160By similarity
Disulfide bondi162 ↔ 171By similarity
Disulfide bondi228 ↔ 244By similarity
Disulfide bondi240 ↔ 253By similarity
Disulfide bondi255 ↔ 268By similarity
Disulfide bondi274 ↔ 287By similarity
Disulfide bondi281 ↔ 296By similarity
Disulfide bondi301 ↔ 318By similarity
Glycosylationi307 – 3071N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ53RD9.
PRIDEiQ53RD9.

PTM databases

PhosphoSiteiQ53RD9.

Expressioni

Gene expression databases

BgeeiQ53RD9.
CleanExiHS_FBLN7.
ExpressionAtlasiQ53RD9. baseline and differential.
GenevisibleiQ53RD9. HS.

Organism-specific databases

HPAiHPA034992.

Interactioni

Subunit structurei

Interacts with heparin, FBLN1, FN1 and DSPP. Preferentially binds dental mesenchyme cells and odontoblasts but not dental epithelial cells or nondental cells. Binding requires a heparan sulfate-containing receptor on the cell surface as well as an integrin (By similarity).By similarity

Protein-protein interaction databases

BioGridi126208. 5 interactions.
STRINGi9606.ENSP00000331411.

Structurei

3D structure databases

ProteinModelPortaliQ53RD9.
SMRiQ53RD9. Positions 138-300.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini79 – 13658SushiPROSITE-ProRule annotationAdd
BLAST
Domaini136 – 17237EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini224 – 26946EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini270 – 31950EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili28 – 5326Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the fibulin family.Curated
Contains 3 EGF-like domains.PROSITE-ProRule annotation
Contains 1 Sushi (CCP/SCR) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, EGF-like domain, Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiNOG240186.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000089983.
HOVERGENiHBG107003.
InParanoidiQ53RD9.
KOiK17342.
OMAiSICQDVN.
OrthoDBiEOG74XS6C.
PhylomeDBiQ53RD9.
TreeFamiTF330076.

Family and domain databases

InterProiIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00084. Sushi. 1 hit.
[Graphical view]
SMARTiSM00032. CCP. 1 hit.
SM00181. EGF. 1 hit.
SM00179. EGF_CA. 2 hits.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 2 hits.
PS50923. SUSHI. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q53RD9-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVPSSPRALF LLLLILACPE PRASQNCLSK QQLLSAIRQL QQLLKGQETR
60 70 80 90 100
FAEGIRHMKS RLAALQNSVG RVGPDALPVS CPALNTPADG RKFGSKYLVD
110 120 130 140 150
HEVHFTCNPG FRLVGPSSVV CLPNGTWTGE QPHCRGISEC SSQPCQNGGT
160 170 180 190 200
CVEGVNQYRC ICPPGRTGNR CQHQAQTAAP EGSVAGDSAF SRAPRCAQVE
210 220 230 240 250
RAQHCSCEAG FHLSGAAGDS VCQDVNECEL YGQEGRPRLC MHACVNTPGS
260 270 280 290 300
YRCTCPGGYR TLADGKSCED VDECVGLQPV CPQGTTCINT GGSFQCVSPE
310 320 330 340 350
CPEGSGNVSY VKTSPFQCER NPCPMDSRPC RHLPKTISFH YLSLPSNLKT
360 370 380 390 400
PITLFRMATA SAPGRAGPNS LRFGIVGGNS RGHFVMQRSD RQTGDLILVQ
410 420 430
NLEGPQTLEV DVDMSEYLDR SFQANHVSKV TIFVSPYDF
Length:439
Mass (Da):47,376
Last modified:May 24, 2005 - v1
Checksum:i905C12B76B78E2EE
GO
Isoform 2 (identifier: Q53RD9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     178-223: Missing.

Show »
Length:393
Mass (Da):42,801
Checksum:i309F379792EC9ED6
GO
Isoform 3 (identifier: Q53RD9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: Missing.

Show »
Length:382
Mass (Da):40,980
Checksum:i000F84ED82599AFA
GO
Isoform 4 (identifier: Q53RD9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     136-269: Missing.

Show »
Length:305
Mass (Da):33,326
Checksum:i8A8246ACAF379DDD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti119 – 1191V → M.1 Publication
Corresponds to variant rs35586251 [ dbSNP | Ensembl ].
VAR_037689

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5757Missing in isoform 3. 1 PublicationVSP_030084Add
BLAST
Alternative sequencei136 – 269134Missing in isoform 4. 1 PublicationVSP_030085Add
BLAST
Alternative sequencei178 – 22346Missing in isoform 2. 1 PublicationVSP_030086Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK094759 mRNA. Translation: BAC04416.1.
AC092645 Genomic DNA. Translation: AAY14854.1.
CH471245 Genomic DNA. Translation: EAW52100.1.
BC035784 mRNA. Translation: AAH35784.1.
BC126986 mRNA. Translation: AAI26987.1.
BC126987 mRNA. Translation: AAI26988.1.
CR933697 mRNA. Translation: CAI46168.1.
CCDSiCCDS2095.1. [Q53RD9-1]
CCDS46391.1. [Q53RD9-2]
RefSeqiNP_001121637.1. NM_001128165.1. [Q53RD9-2]
NP_694946.2. NM_153214.2. [Q53RD9-1]
UniGeneiHs.437696.

Genome annotation databases

EnsembliENST00000331203; ENSP00000331411; ENSG00000144152. [Q53RD9-1]
ENST00000409450; ENSP00000387000; ENSG00000144152. [Q53RD9-2]
ENST00000409667; ENSP00000386822; ENSG00000144152. [Q53RD9-4]
GeneIDi129804.
KEGGihsa:129804.
UCSCiuc002tho.1. human. [Q53RD9-1]
uc010fki.1. human. [Q53RD9-2]
uc010fkj.1. human. [Q53RD9-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK094759 mRNA. Translation: BAC04416.1.
AC092645 Genomic DNA. Translation: AAY14854.1.
CH471245 Genomic DNA. Translation: EAW52100.1.
BC035784 mRNA. Translation: AAH35784.1.
BC126986 mRNA. Translation: AAI26987.1.
BC126987 mRNA. Translation: AAI26988.1.
CR933697 mRNA. Translation: CAI46168.1.
CCDSiCCDS2095.1. [Q53RD9-1]
CCDS46391.1. [Q53RD9-2]
RefSeqiNP_001121637.1. NM_001128165.1. [Q53RD9-2]
NP_694946.2. NM_153214.2. [Q53RD9-1]
UniGeneiHs.437696.

3D structure databases

ProteinModelPortaliQ53RD9.
SMRiQ53RD9. Positions 138-300.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126208. 5 interactions.
STRINGi9606.ENSP00000331411.

PTM databases

PhosphoSiteiQ53RD9.

Polymorphism and mutation databases

BioMutaiFBLN7.
DMDMi74726569.

Proteomic databases

PaxDbiQ53RD9.
PRIDEiQ53RD9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331203; ENSP00000331411; ENSG00000144152. [Q53RD9-1]
ENST00000409450; ENSP00000387000; ENSG00000144152. [Q53RD9-2]
ENST00000409667; ENSP00000386822; ENSG00000144152. [Q53RD9-4]
GeneIDi129804.
KEGGihsa:129804.
UCSCiuc002tho.1. human. [Q53RD9-1]
uc010fki.1. human. [Q53RD9-2]
uc010fkj.1. human. [Q53RD9-4]

Organism-specific databases

CTDi129804.
GeneCardsiGC02P112895.
H-InvDBHIX0002376.
HGNCiHGNC:26740. FBLN7.
HPAiHPA034992.
MIMi611551. gene.
neXtProtiNX_Q53RD9.
PharmGKBiPA162388107.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG240186.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000089983.
HOVERGENiHBG107003.
InParanoidiQ53RD9.
KOiK17342.
OMAiSICQDVN.
OrthoDBiEOG74XS6C.
PhylomeDBiQ53RD9.
TreeFamiTF330076.

Miscellaneous databases

ChiTaRSiFBLN7. human.
GenomeRNAii129804.
NextBioi82641.
PROiQ53RD9.
SOURCEiSearch...

Gene expression databases

BgeeiQ53RD9.
CleanExiHS_FBLN7.
ExpressionAtlasiQ53RD9. baseline and differential.
GenevisibleiQ53RD9. HS.

Family and domain databases

InterProiIPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00084. Sushi. 1 hit.
[Graphical view]
SMARTiSM00032. CCP. 1 hit.
SM00181. EGF. 1 hit.
SM00179. EGF_CA. 2 hits.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 2 hits.
PS50923. SUSHI. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-119.
    Tissue: Brain.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
    Tissue: Ovary.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-176 (ISOFORM 3).
    Tissue: Brain.

Entry informationi

Entry nameiFBLN7_HUMAN
AccessioniPrimary (citable) accession number: Q53RD9
Secondary accession number(s): A0JNV1
, A0JNV2, Q5H9P5, Q8N9G0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 24, 2005
Last modified: June 24, 2015
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.