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P98133

- FBN1_BOVIN

UniProt

P98133 - FBN1_BOVIN

Protein

Fibrillin-1

Gene

FBN1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-1-containing microfibrils provide long-term force bearing structural support. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively By similarity.By similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. extracellular matrix structural constituent Source: InterPro

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_201925. Degradation of the extracellular matrix.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibrillin-1
    Alternative name(s):
    MP340
    Gene namesi
    Name:FBN1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 28712844Fibrillin-1PRO_0000007580Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi85 ↔ 94PROSITE-ProRule annotation
    Disulfide bondi89 ↔ 100PROSITE-ProRule annotation
    Disulfide bondi102 ↔ 111PROSITE-ProRule annotation
    Disulfide bondi119 ↔ 129PROSITE-ProRule annotation
    Disulfide bondi123 ↔ 134PROSITE-ProRule annotation
    Disulfide bondi136 ↔ 145PROSITE-ProRule annotation
    Disulfide bondi150 ↔ 160PROSITE-ProRule annotation
    Disulfide bondi154 ↔ 166PROSITE-ProRule annotation
    Disulfide bondi168 ↔ 177PROSITE-ProRule annotation
    Disulfide bondi250 ↔ 262PROSITE-ProRule annotation
    Disulfide bondi257 ↔ 271PROSITE-ProRule annotation
    Disulfide bondi273 ↔ 286PROSITE-ProRule annotation
    Disulfide bondi292 ↔ 304PROSITE-ProRule annotation
    Disulfide bondi299 ↔ 313PROSITE-ProRule annotation
    Disulfide bondi315 ↔ 328PROSITE-ProRule annotation
    Glycosylationi448 – 4481N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi453 ↔ 465PROSITE-ProRule annotation
    Disulfide bondi460 ↔ 474PROSITE-ProRule annotation
    Disulfide bondi476 ↔ 488PROSITE-ProRule annotation
    Disulfide bondi494 ↔ 504PROSITE-ProRule annotation
    Disulfide bondi499 ↔ 513PROSITE-ProRule annotation
    Disulfide bondi515 ↔ 528PROSITE-ProRule annotation
    Disulfide bondi534 ↔ 546PROSITE-ProRule annotation
    Disulfide bondi541 ↔ 555PROSITE-ProRule annotation
    Disulfide bondi557 ↔ 570PROSITE-ProRule annotation
    Disulfide bondi576 ↔ 587PROSITE-ProRule annotation
    Disulfide bondi582 ↔ 596PROSITE-ProRule annotation
    Disulfide bondi598 ↔ 611PROSITE-ProRule annotation
    Disulfide bondi617 ↔ 628PROSITE-ProRule annotation
    Disulfide bondi623 ↔ 637PROSITE-ProRule annotation
    Disulfide bondi639 ↔ 652PROSITE-ProRule annotation
    Disulfide bondi727 ↔ 739PROSITE-ProRule annotation
    Disulfide bondi734 ↔ 748PROSITE-ProRule annotation
    Disulfide bondi750 ↔ 763PROSITE-ProRule annotation
    Disulfide bondi769 ↔ 781PROSITE-ProRule annotation
    Disulfide bondi776 ↔ 790PROSITE-ProRule annotation
    Disulfide bondi792 ↔ 805PROSITE-ProRule annotation
    Disulfide bondi811 ↔ 821PROSITE-ProRule annotation
    Disulfide bondi816 ↔ 830PROSITE-ProRule annotation
    Disulfide bondi832 ↔ 845PROSITE-ProRule annotation
    Disulfide bondi853 ↔ 875PROSITE-ProRule annotation
    Disulfide bondi862 ↔ 887PROSITE-ProRule annotation
    Disulfide bondi876 ↔ 890PROSITE-ProRule annotation
    Disulfide bondi896 ↔ 908PROSITE-ProRule annotation
    Disulfide bondi914 ↔ 926PROSITE-ProRule annotation
    Disulfide bondi921 ↔ 935PROSITE-ProRule annotation
    Disulfide bondi937 ↔ 950PROSITE-ProRule annotation
    Disulfide bondi1032 ↔ 1044PROSITE-ProRule annotation
    Disulfide bondi1039 ↔ 1053PROSITE-ProRule annotation
    Disulfide bondi1055 ↔ 1068PROSITE-ProRule annotation
    Glycosylationi1067 – 10671N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1074 ↔ 1086PROSITE-ProRule annotation
    Disulfide bondi1081 ↔ 1095PROSITE-ProRule annotation
    Disulfide bondi1097 ↔ 1111PROSITE-ProRule annotation
    Disulfide bondi1117 ↔ 1129PROSITE-ProRule annotation
    Disulfide bondi1124 ↔ 1138PROSITE-ProRule annotation
    Disulfide bondi1140 ↔ 1153PROSITE-ProRule annotation
    Glycosylationi1149 – 11491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1159 ↔ 1171PROSITE-ProRule annotation
    Disulfide bondi1166 ↔ 1180PROSITE-ProRule annotation
    Disulfide bondi1182 ↔ 1195PROSITE-ProRule annotation
    Disulfide bondi1201 ↔ 1212PROSITE-ProRule annotation
    Disulfide bondi1208 ↔ 1221PROSITE-ProRule annotation
    Disulfide bondi1223 ↔ 1236PROSITE-ProRule annotation
    Disulfide bondi1242 ↔ 1254PROSITE-ProRule annotation
    Disulfide bondi1249 ↔ 1263PROSITE-ProRule annotation
    Disulfide bondi1265 ↔ 1278PROSITE-ProRule annotation
    Disulfide bondi1284 ↔ 1296PROSITE-ProRule annotation
    Disulfide bondi1291 ↔ 1305PROSITE-ProRule annotation
    Disulfide bondi1307 ↔ 1320PROSITE-ProRule annotation
    Disulfide bondi1326 ↔ 1339PROSITE-ProRule annotation
    Disulfide bondi1333 ↔ 1348PROSITE-ProRule annotation
    Disulfide bondi1350 ↔ 1361PROSITE-ProRule annotation
    Disulfide bondi1367 ↔ 1380PROSITE-ProRule annotation
    Glycosylationi1369 – 13691N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1374 ↔ 1389PROSITE-ProRule annotation
    Disulfide bondi1391 ↔ 1402PROSITE-ProRule annotation
    Disulfide bondi1408 ↔ 1420PROSITE-ProRule annotation
    Disulfide bondi1415 ↔ 1429PROSITE-ProRule annotation
    Disulfide bondi1431 ↔ 1444PROSITE-ProRule annotation
    Disulfide bondi1450 ↔ 1461PROSITE-ProRule annotation
    Disulfide bondi1456 ↔ 1470PROSITE-ProRule annotation
    Disulfide bondi1472 ↔ 1485PROSITE-ProRule annotation
    Glycosylationi1484 – 14841N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1491 ↔ 1502PROSITE-ProRule annotation
    Disulfide bondi1497 ↔ 1511PROSITE-ProRule annotation
    Disulfide bondi1513 ↔ 1526PROSITE-ProRule annotation
    Disulfide bondi1534 ↔ 1562PROSITE-ProRule annotation
    Disulfide bondi1549 ↔ 1574PROSITE-ProRule annotation
    Disulfide bondi1563 ↔ 1577PROSITE-ProRule annotation
    Disulfide bondi1564 ↔ 1589PROSITE-ProRule annotation
    Glycosylationi1581 – 15811N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1610 ↔ 1622PROSITE-ProRule annotation
    Disulfide bondi1617 ↔ 1631PROSITE-ProRule annotation
    Disulfide bondi1633 ↔ 1646PROSITE-ProRule annotation
    Disulfide bondi1652 ↔ 1663PROSITE-ProRule annotation
    Disulfide bondi1658 ↔ 1672PROSITE-ProRule annotation
    Glycosylationi1669 – 16691N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1674 ↔ 1687PROSITE-ProRule annotation
    Glycosylationi1703 – 17031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1713 – 17131N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1770 ↔ 1782PROSITE-ProRule annotation
    Disulfide bondi1777 ↔ 1791PROSITE-ProRule annotation
    Disulfide bondi1793 ↔ 1806PROSITE-ProRule annotation
    Disulfide bondi1812 ↔ 1824PROSITE-ProRule annotation
    Disulfide bondi1818 ↔ 1833PROSITE-ProRule annotation
    Disulfide bondi1835 ↔ 1847PROSITE-ProRule annotation
    Disulfide bondi1853 ↔ 1865PROSITE-ProRule annotation
    Disulfide bondi1860 ↔ 1874PROSITE-ProRule annotation
    Disulfide bondi1876 ↔ 1889PROSITE-ProRule annotation
    Disulfide bondi1895 ↔ 1905PROSITE-ProRule annotation
    Disulfide bondi1900 ↔ 1914PROSITE-ProRule annotation
    Glycosylationi1902 – 19021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1916 ↔ 1928PROSITE-ProRule annotation
    Disulfide bondi1934 ↔ 1947PROSITE-ProRule annotation
    Disulfide bondi1942 ↔ 1956PROSITE-ProRule annotation
    Disulfide bondi1958 ↔ 1971PROSITE-ProRule annotation
    Disulfide bondi1977 ↔ 1989PROSITE-ProRule annotation
    Disulfide bondi1984 ↔ 1998PROSITE-ProRule annotation
    Disulfide bondi2000 ↔ 2011PROSITE-ProRule annotation
    Disulfide bondi2017 ↔ 2029PROSITE-ProRule annotation
    Disulfide bondi2024 ↔ 2038PROSITE-ProRule annotation
    Disulfide bondi2040 ↔ 2053PROSITE-ProRule annotation
    Glycosylationi2077 – 20771N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2131 ↔ 2142PROSITE-ProRule annotation
    Disulfide bondi2137 ↔ 2151PROSITE-ProRule annotation
    Disulfide bondi2153 ↔ 2164PROSITE-ProRule annotation
    Disulfide bondi2170 ↔ 2181PROSITE-ProRule annotation
    Disulfide bondi2176 ↔ 2190PROSITE-ProRule annotation
    Glycosylationi2178 – 21781N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2192 ↔ 2204PROSITE-ProRule annotation
    Disulfide bondi2210 ↔ 2221PROSITE-ProRule annotation
    Disulfide bondi2217 ↔ 2230PROSITE-ProRule annotation
    Disulfide bondi2232 ↔ 2245PROSITE-ProRule annotation
    Disulfide bondi2251 ↔ 2265PROSITE-ProRule annotation
    Disulfide bondi2258 ↔ 2274PROSITE-ProRule annotation
    Disulfide bondi2276 ↔ 2289PROSITE-ProRule annotation
    Disulfide bondi2295 ↔ 2307PROSITE-ProRule annotation
    Disulfide bondi2302 ↔ 2316PROSITE-ProRule annotation
    Disulfide bondi2318 ↔ 2331PROSITE-ProRule annotation
    Disulfide bondi2406 ↔ 2418PROSITE-ProRule annotation
    Disulfide bondi2413 ↔ 2427PROSITE-ProRule annotation
    Disulfide bondi2429 ↔ 2442PROSITE-ProRule annotation
    Disulfide bondi2448 ↔ 2459PROSITE-ProRule annotation
    Disulfide bondi2455 ↔ 2468PROSITE-ProRule annotation
    Disulfide bondi2470 ↔ 2483PROSITE-ProRule annotation
    Disulfide bondi2489 ↔ 2500PROSITE-ProRule annotation
    Disulfide bondi2496 ↔ 2509PROSITE-ProRule annotation
    Disulfide bondi2511 ↔ 2522PROSITE-ProRule annotation
    Disulfide bondi2528 ↔ 2541PROSITE-ProRule annotation
    Disulfide bondi2535 ↔ 2550PROSITE-ProRule annotation
    Disulfide bondi2552 ↔ 2565PROSITE-ProRule annotation
    Disulfide bondi2571 ↔ 2581PROSITE-ProRule annotation
    Disulfide bondi2577 ↔ 2590PROSITE-ProRule annotation
    Disulfide bondi2592 ↔ 2605PROSITE-ProRule annotation
    Disulfide bondi2611 ↔ 2622PROSITE-ProRule annotation
    Disulfide bondi2617 ↔ 2631PROSITE-ProRule annotation
    Disulfide bondi2633 ↔ 2646PROSITE-ProRule annotation
    Disulfide bondi2652 ↔ 2663PROSITE-ProRule annotation
    Disulfide bondi2659 ↔ 2672PROSITE-ProRule annotation
    Disulfide bondi2674 ↔ 2686PROSITE-ProRule annotation
    Glycosylationi2734 – 27341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2750 – 27501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2767 – 27671N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP98133.
    PRIDEiP98133.

    Interactioni

    Subunit structurei

    Interacts with COL16A1. Interacts with ADAMTSL4 By similarity. Interacts with ADAMTS10; this interaction promotes microfibrils assembly By similarity. Interacts with THSD4; this interaction promotes fibril formation By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000035493.

    Structurei

    3D structure databases

    ProteinModelPortaliP98133.
    SMRiP98133. Positions 1069-1154, 1486-1647, 2054-2205, 2455-2484.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini81 – 11232EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini115 – 14632EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini147 – 17832EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini184 – 23653TB 1Add
    BLAST
    Domaini246 – 28742EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini288 – 32942EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini334 – 38956TB 2Add
    BLAST
    Domaini449 – 48941EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini490 – 52940EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini530 – 57142EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini572 – 61241EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini613 – 65341EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini659 – 71153TB 3Add
    BLAST
    Domaini723 – 76442EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini765 – 80642EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini807 – 84640EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini851 – 90252TB 4Add
    BLAST
    Domaini910 – 95142EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini956 – 100853TB 5Add
    BLAST
    Domaini1028 – 106942EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1070 – 111243EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1113 – 115442EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1155 – 119642EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1197 – 123741EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1238 – 127942EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1280 – 132142EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1322 – 136241EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1363 – 140341EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1404 – 144542EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1446 – 148641EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1487 – 152741EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1532 – 158958TB 6Add
    BLAST
    Domaini1606 – 164742EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1648 – 168841EGF-like 28; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1693 – 174856TB 7Add
    BLAST
    Domaini1766 – 180742EGF-like 29; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1808 – 184841EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1849 – 189042EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1891 – 192939EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1930 – 197243EGF-like 33; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1973 – 201240EGF-like 34; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2013 – 205442EGF-like 35; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2059 – 211153TB 8Add
    BLAST
    Domaini2127 – 216539EGF-like 36; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2166 – 220540EGF-like 37; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2206 – 224641EGF-like 38; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2247 – 229044EGF-like 39; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2291 – 233242EGF-like 40; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2337 – 239054TB 9Add
    BLAST
    Domaini2402 – 244342EGF-like 41; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2444 – 248441EGF-like 42; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2485 – 252339EGF-like 43; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2524 – 256643EGF-like 44; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2567 – 260640EGF-like 45; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2607 – 264741EGF-like 46; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini2648 – 268740EGF-like 47; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi392 – 44655Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the fibrillin family.Curated
    Contains 47 EGF-like domains.PROSITE-ProRule annotation
    Contains 9 TB (TGF-beta binding) domains.Curated

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOGENOMiHOG000231768.
    HOVERGENiHBG005643.
    KOiK06825.

    Family and domain databases

    Gene3Di3.90.290.10. 10 hits.
    InterProiIPR026823. cEGF.
    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.
    IPR011398. FBN/EtMIC4.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR017878. TB_dom.
    [Graphical view]
    PANTHERiPTHR24039. PTHR24039. 1 hit.
    PfamiPF12662. cEGF. 5 hits.
    PF07645. EGF_CA. 33 hits.
    PF00683. TB. 9 hits.
    [Graphical view]
    PIRSFiPIRSF036312. Fibrillin. 1 hit.
    SMARTiSM00181. EGF. 4 hits.
    SM00179. EGF_CA. 42 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 10 hits.
    SSF57581. SSF57581. 9 hits.
    PROSITEiPS00010. ASX_HYDROXYL. 43 hits.
    PS00022. EGF_1. 2 hits.
    PS01186. EGF_2. 38 hits.
    PS50026. EGF_3. 45 hits.
    PS01187. EGF_CA. 43 hits.
    PS51364. TB. 9 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P98133-1 [UniParc]FASTAAdd to Basket

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    MRRGGLLEVA LGFTVLLASY TSHGADTNLE AGNVKETRAN RAKRRGGGGH     50
    NALKGPNVCG SRYNAYCCPG WKTLPGGNQC IVPICRHSCG DGFCSRPNMC 100
    TCPSGQIAPS CGSRSIQHCN IRCMNGGSCS DDHCLCQKGY IGTHCGQPVC 150
    ESGCLNGGRC VAPNRCACTY GFTGPQCERD YRTGPCFTVI SNQMCQGQLS 200
    GIVCTKTLCC ATVGRAWGHP CEMCPAQPHP CRRGFIPNIR TGACQDVDEC 250
    QAIPGLCQGG NCINTVGSFE CKCPAGHKFN EVSQKCEDID ECSTIPGICD 300
    GGECTNTVSS YFCKCPPGFY TSPDGTRCID VRPGYCYTAL ANGRCSNQLP 350
    QSITKMQCCC DAGRCWSPGV TVAPEMCPIR ATEDFNKLCS VPMVIPERPG 400
    YPPPPLGPVP PVQPVPPGFP PGPQIMIPRP PVEYPYPSRE PPRVLPVNVT 450
    DYCQLFRYLC QNGRCIPTPG SYRCECNKGF QLDLRGECID VDECEKNPCA 500
    GGECINTQGS YTCQCRPGYQ STLTRTECRD IDECLQNGRI CNNGRCINTD 550
    GSFHCVCNAG FHVTRDGKNC EDMDECSIRN MCLNGMCINE DGSFKCICKP 600
    GFQLASDGRY CKDINECETL GICMNGRCVN TDGSYRCECF PGLAVGLDGR 650
    VCVDTHMRST CYGGYKRGQC VKPLFGAVTK SECCCASTEY AFGEPCQPCP 700
    SQNSAEYQAL CSSGPGITSA GSDINECALD PDICPNGICE NLRGTYKCIC 750
    NSGYEVDSTG KNCVDINECV LNSLLCDNGQ CRNTPGSFVC TCPKGFIYKP 800
    ELKTCEDIDE CESSPCINGV CKNSPGSFIC ECSSESTLDP TKTICIETIK 850
    GTCWQTVIDG RCEININGAT LKSQCCSSLG AAWGSPCTPC QVDPICGKGY 900
    SRIKGTQCED IDECEVFPGV CKNGLCVNSK GSFKCQCPSG MTLDATGRIC 950
    LDIRLETCFL RYEDEECTLP VAGRHRMDAC CCSVGAAWGT EECEECPVRN 1000
    TPEYEELCPR GPGFATKEIT NGKRFFKDIN ECKMIPNLCT HGKCRNTIGS 1050
    FKCRCDSGFA LDSEERNCTD IDECRISPDL CGRGQCVNTP GDFECKCDEG 1100
    YESGFMMMKN CMDIDECQRD PLLCRGGVCL NTEGSYRCEC PPGHQLAPNI 1150
    SACIDINECE LSAHLCPHGR CVNLIGKYQC ACNPGYHSTP DRLFCVDIDE 1200
    CSIMNGGCET FCTNSEGSYE CSCQPGFALM PDQRSCTDID ECEDNPNICD 1250
    GGQCTNIPGE YRCLCYDGFM ASEDMKTCVD VNECDLNPNI CLSGTCENTK 1300
    GSFICHCDMG YSGKKGKTGC TDINECEIGA HNCDRHAVCT NTAGSFKCSC 1350
    SPGWIGDGIK CTDLDECSNG THMCSQHADC KNTMGSYRCL CKEGYTGDGF 1400
    TCTDLDECSE NLNLCGNGQC LNAPGGYRCE CDMGFVPSAD GKACEDIDEC 1450
    SLPNICVFGT CHNLPGLFRC ECEIGYELDR SGGNCTDVNE CLDPTTCISG 1500
    NCVNTPGSYT CDCPPDFELN PTRVGCVDTR SGNCYLDIRP RGDNGDTACS 1550
    NEIGVGVSKA SCCCSLGKAW GTPCELCPPV NTSEYKILCP GGEGFRPNPI 1600
    TVILEDIDEC QELPGLCQGG KCINTFGSFQ CRCPTGYYLN EDTRVCDDVN 1650
    ECETPGICGP GTCYNTVGNY TCICPPDYMQ VNGGNNCMDM RRSLCYRNYY 1700
    ADNQTCDGEL LFNMTKKMCC CSYNIGRAWN KPCEQCPIPS TDEFATLCGS 1750
    QRPGFVIDIY TGLPVDIDEC REIPGVCENG VCINMVGSFR CECPVGFFYN 1800
    DKLLVCEDID ECQNGPVCQR NAECINTAGS YRCDCKPGYR FTSTGQCNDR 1850
    NECQEIPNIC SHGQCIDTVG SFYCLCHTGF KTNADQTMCL DINECERDAC 1900
    GNGTCRNTIG SFNCRCNHGF ILSHNNDCID VDECATGNGN LCRNGQCINT 1950
    VGSFQCQCNE GYEVAPDGRT CVDINECLLD PRKCAPGTCQ NLDGSYRCIC 2000
    PPGYSLQNDK CEDIDECVEE PEICALGTCS NTEGSFKCLC PDGFSLSSTG 2050
    RRCQDLRMSY CYAKFEGGKC SSPKSRNHSK QECCCALKGE GWGDPCELCP 2100
    TEPDEAFRQI CPYGSGIIVG PDDSAVDMDE CKEPDVCKHG QCINTDGSYR 2150
    CECPFGYILQ GNECVDTDEC SVGNPCGNGT CKNVIGGFEC TCEEGFEPGP 2200
    MMTCEDINEC AQNPLLCAFR CVNTYGSYEC KCPAGYVLRE DRRMCKDEDE 2250
    CEEGKHDCAE KQMECKNLIG TYLCICGPGY QRRPDGEGCV DENECQTKPG 2300
    ICENGRCLNT RGSYTCECND GFTASPNQDE CLDNREGYCF TEVLQNMCQI 2350
    GSSNRNPVTK SECCCDGGRG WGPHCEICPF QGTVAFKKLC PHGRGFMTNG 2400
    ADIDECKVIH DVCRNGECVN DRGSYHCICK TGYTPDITGT ACVDLNECNQ 2450
    APKPCNFICK NTEGSYQCSC PKGYILQEDG RSCKDLDECA TKQHNCQFLC 2500
    VNTIGSFTCK CPPGFTQHHT ACIDNNECTS DINLCGSKGI CQNTPGSFTC 2550
    ECQRGFSLDP TGASCEDVDE CEGNHRCQHG CQNIIGGYRC SCPQGYLQHY 2600
    QWNQCVDENE CLSAHICGGA SCHNTLGSYK CMCPAGFQYE QFSGGCQDIN 2650
    ECGSAQAPCS YGCSNTEGGY LCACPPGYFR IGQGHCVSGM GMGRGNPEPP 2700
    ASGEMDDNSL SPEACYECKI NGYPKRGRKR RSANETDASN IEDQPEIEAN 2750
    VSLASWDVEK TAVFAFNISH ISNKVRILEL LPALTTLTNH NRYLIESGNE 2800
    NGFFKINQKE GISYLHFTKK KPVAGTYSLQ ISSTPLYKKK ELNQLEDKYD 2850
    KDYLSGELGD NLKMKIQILL H 2871
    Length:2,871
    Mass (Da):312,250
    Last modified:October 1, 1996 - v1
    Checksum:iE77FD2A4F1451CBB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L28748 mRNA. Translation: AAA74122.1.
    PIRiA55567.
    RefSeqiNP_776478.1. NM_174053.2.
    UniGeneiBt.107024.

    Genome annotation databases

    GeneIDi281154.
    KEGGibta:281154.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L28748 mRNA. Translation: AAA74122.1 .
    PIRi A55567.
    RefSeqi NP_776478.1. NM_174053.2.
    UniGenei Bt.107024.

    3D structure databases

    ProteinModelPortali P98133.
    SMRi P98133. Positions 1069-1154, 1486-1647, 2054-2205, 2455-2484.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000035493.

    Proteomic databases

    PaxDbi P98133.
    PRIDEi P98133.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 281154.
    KEGGi bta:281154.

    Organism-specific databases

    CTDi 2200.

    Phylogenomic databases

    eggNOGi NOG12793.
    HOGENOMi HOG000231768.
    HOVERGENi HBG005643.
    KOi K06825.

    Enzyme and pathway databases

    Reactomei REACT_201925. Degradation of the extracellular matrix.

    Miscellaneous databases

    NextBioi 20805217.

    Family and domain databases

    Gene3Di 3.90.290.10. 10 hits.
    InterProi IPR026823. cEGF.
    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.
    IPR011398. FBN/EtMIC4.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR017878. TB_dom.
    [Graphical view ]
    PANTHERi PTHR24039. PTHR24039. 1 hit.
    Pfami PF12662. cEGF. 5 hits.
    PF07645. EGF_CA. 33 hits.
    PF00683. TB. 9 hits.
    [Graphical view ]
    PIRSFi PIRSF036312. Fibrillin. 1 hit.
    SMARTi SM00181. EGF. 4 hits.
    SM00179. EGF_CA. 42 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 10 hits.
    SSF57581. SSF57581. 9 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 43 hits.
    PS00022. EGF_1. 2 hits.
    PS01186. EGF_2. 38 hits.
    PS50026. EGF_3. 45 hits.
    PS01187. EGF_CA. 43 hits.
    PS51364. TB. 9 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the coding region of the bovine fibrillin cDNA and localization to bovine chromosome 10."
      Tilstra D.J., Potter K.A., Byers P.H.
      Genomics 23:480-485(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Skin.
    2. "Further characterization of proteins associated with elastic fiber microfibrils including the molecular cloning of MAGP-2 (MP25)."
      Gibson M.A., Hatzinikolas G., Kumaratilake J.S., Sandberg L.B., Nicholl J.K., Sutherland G.R., Cleary E.G.
      J. Biol. Chem. 271:1096-1103(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.

    Entry informationi

    Entry nameiFBN1_BOVIN
    AccessioniPrimary (citable) accession number: P98133
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3