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Q53RD9

- FBLN7_HUMAN

UniProt

Q53RD9 - FBLN7_HUMAN

Protein

Fibulin-7

Gene

FBLN7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
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    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

    1. calcium ion binding Source: InterPro
    2. heparin binding Source: UniProtKB-KW

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW

    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: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:26740. FBLN7.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162388107.

    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

    ArrayExpressiQ53RD9.
    BgeeiQ53RD9.
    CleanExiHS_FBLN7.
    GenevestigatoriQ53RD9.

    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

    Structurei

    3D structure databases

    ProteinModelPortaliQ53RD9.
    SMRiQ53RD9. Positions 121-300.
    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.
    HOGENOMiHOG000089983.
    HOVERGENiHBG107003.
    InParanoidiQ53RD9.
    KOiK17342.
    OMAiQHCSCEA.
    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.
    [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. Align

    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

    MVPSSPRALF LLLLILACPE PRASQNCLSK QQLLSAIRQL QQLLKGQETR    50
    FAEGIRHMKS RLAALQNSVG RVGPDALPVS CPALNTPADG RKFGSKYLVD 100
    HEVHFTCNPG FRLVGPSSVV CLPNGTWTGE QPHCRGISEC SSQPCQNGGT 150
    CVEGVNQYRC ICPPGRTGNR CQHQAQTAAP EGSVAGDSAF SRAPRCAQVE 200
    RAQHCSCEAG FHLSGAAGDS VCQDVNECEL YGQEGRPRLC MHACVNTPGS 250
    YRCTCPGGYR TLADGKSCED VDECVGLQPV CPQGTTCINT GGSFQCVSPE 300
    CPEGSGNVSY VKTSPFQCER NPCPMDSRPC RHLPKTISFH YLSLPSNLKT 350
    PITLFRMATA SAPGRAGPNS LRFGIVGGNS RGHFVMQRSD RQTGDLILVQ 400
    NLEGPQTLEV DVDMSEYLDR SFQANHVSKV TIFVSPYDF 439
    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:
    EMBL
    GenBank
    DDBJ
    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]

    Polymorphism databases

    DMDMi74726569.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS2095.1. [Q53RD9-1 ]
    CCDS46391.1. [Q53RD9-2 ]
    RefSeqi NP_001121637.1. NM_001128165.1. [Q53RD9-2 ]
    NP_694946.2. NM_153214.2. [Q53RD9-1 ]
    UniGenei Hs.437696.

    3D structure databases

    ProteinModelPortali Q53RD9.
    SMRi Q53RD9. Positions 121-300.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q53RD9.

    Polymorphism databases

    DMDMi 74726569.

    Proteomic databases

    PaxDbi Q53RD9.
    PRIDEi Q53RD9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331203 ; ENSP00000331411 ; ENSG00000144152 . [Q53RD9-1 ]
    ENST00000409450 ; ENSP00000387000 ; ENSG00000144152 . [Q53RD9-2 ]
    ENST00000409667 ; ENSP00000386822 ; ENSG00000144152 . [Q53RD9-4 ]
    GeneIDi 129804.
    KEGGi hsa:129804.
    UCSCi uc002tho.1. human. [Q53RD9-1 ]
    uc010fki.1. human. [Q53RD9-2 ]
    uc010fkj.1. human. [Q53RD9-4 ]

    Organism-specific databases

    CTDi 129804.
    GeneCardsi GC02P112895.
    H-InvDB HIX0002376.
    HGNCi HGNC:26740. FBLN7.
    HPAi HPA034992.
    MIMi 611551. gene.
    neXtProti NX_Q53RD9.
    PharmGKBi PA162388107.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG240186.
    HOGENOMi HOG000089983.
    HOVERGENi HBG107003.
    InParanoidi Q53RD9.
    KOi K17342.
    OMAi QHCSCEA.
    OrthoDBi EOG74XS6C.
    PhylomeDBi Q53RD9.
    TreeFami TF330076.

    Miscellaneous databases

    GenomeRNAii 129804.
    NextBioi 82641.
    PROi Q53RD9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q53RD9.
    Bgeei Q53RD9.
    CleanExi HS_FBLN7.
    Genevestigatori Q53RD9.

    Family and domain databases

    InterProi IPR000742. 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.
    [Graphical view ]
    Pfami PF00008. EGF. 1 hit.
    PF07645. EGF_CA. 2 hits.
    PF00084. Sushi. 1 hit.
    [Graphical view ]
    SMARTi SM00032. CCP. 1 hit.
    SM00181. EGF. 1 hit.
    SM00179. EGF_CA. 2 hits.
    [Graphical view ]
    SUPFAMi SSF57535. SSF57535. 1 hit.
    PROSITEi PS00010. 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 ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 94 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