Uniprot ID:P35555	Protein name: Fibrillin-1 [Cleaved into: Asprosin]	Gene : FBN1 FBN
Protein Family:Fibrillin family	Squence Length : 2871

Sequnce	>P35555 2872 MRRGRLLEIALGFTVLLASYTSHGADANLEAGNVKETRASRAKRRGGGGHDALKGPNVCGSRYNAYCCPGWKTLPGGNQCIVPICRHSCGDGFCSRPNMCTCPSGQIAPSCGSRSIQHCNIRCMNGGSCSDDHCLCQKGYIGTHCGQPVCESGCLNGGRCVAPNRCACTYGFTGPQCERDYRTGPCFTVISNQMCQGQLSGIVCTKTLCCATVGRAWGHPCEMCPAQPHPCRRGFIPNIRTGACQDVDECQAIPGLCQGGNCINTVGSFECKCPAGHKLNEVSQKCEDIDECSTIPGICEGGECTNTVSSYFCKCPPGFYTSPDGTRCIDVRPGYCYTALTNGRCSNQLPQSITKMQCCCDAGRCWSPGVTVAPEMCPIRATEDFNKLCSVPMVIPGRPEYPPPPLGPIPPVLPVPPGFPPGPQIPVPRPPVEYLYPSREPPRVLPVNVTDYCQLVRYLCQNGRCIPTPGSCRCECNKGFQLDLRGECIDVDECEKNPCAGGECINNQGSYTCQCRAGYQSTLTRTECRDIDECLQNGRICNNGRCINTDGSFHCVCNAGFHVTRDGKNCEDMDECSIRNMCLNGMCINEDGSFKCICKPGFQLASDGRYCKDINECETPGICMNGRCVNTDGSYRCECFPGLAVGLDGRVCVDTHMRSTCYGGYKRGQCIKPLFGAVTKSECCCASTEYAFGEPCQPCPAQNSAEYQALCSSGPGMTSAGSDINECALDPDICPNGICENLRGTYKCICNSGYEVDSTGKNCVDINECVLNSLLCDNGQCRNTPGSFVCTCPKGFIYKPDLKTCEDIDECESSPCINGVCKNSPGSFICECSSESTLDPTKTICIETIKGTCWQTVIDGRCEININGATLKSQCCSSLGAAWGSPCTLCQVDPICGKGYSRIKGTQCEDIDECEVFPGVCKNGLCVNTRGSFKCQCPSGMTLDATGRICLDIRLETCFLRYEDEECTLPIAGRHRMDACCCSVGAAWGTEECEECPMRNTPEYEELCPRGPGFATKEITNGKPFFKDINECKMIPSLCTHGKCRNTIGSFKCRCDSGFALDSEERNCTDIDECRISPDLCGRGQCVNTPGDFECKCDEGYESGFMMMKNCMDIDECQRDPLLCRGGVCHNTEGSYRCECPPGHQLSPNISACIDINECELSAHLCPNGRCVNLIGKYQCACNPGYHSTPDRLFCVDIDECSIMNGGCETFCTNSEGSYECSCQPGFALMPDQRSCTDIDECEDNPNICDGGQCTNIPGEYRCLCYDGFMASEDMKTCVDVNECDLNPNICLSGTCENTKGSFICHCDMGYSGKKGKTGCTDINECEIGAHNCGKHAVCTNTAGSFKCSCSPGWIGDGIKCTDLDECSNGTHMCSQHADCKNTMGSYRCLCKEGYTGDGFTCTDLDECSENLNLCGNGQCLNAPGGYRCECDMGFVPSADGKACEDIDECSLPNICVFGTCHNLPGLFRCECEIGYELDRSGGNCTDVNECLDPTTCISGNCVNTPGSYICDCPPDFELNPTRVGCVDTRSGNCYLDIRPRGDNGDTACSNEIGVGVSKASCCCSLGKAWGTPCEMCPAVNTSEYKILCPGGEGFRPNPITVILEDIDECQELPGLCQGGKCINTFGSFQCRCPTGYYLNEDTRVCDDVNECETPGICGPGTCYNTVGNYTCICPPDYMQVNGGNNCMDMRRSLCYRNYYADNQTCDGELLFNMTKKMCCCSYNIGRAWNKPCEQCPIPSTDEFATLCGSQRPGFVIDIYTGLPVDIDECREIPGVCENGVCINMVGSFRCECPVGFFYNDKLLVCEDIDECQNGPVCQRNAECINTAGSYRCDCKPGYRFTSTGQCNDRNECQEIPNICSHGQCIDTVGSFYCLCHTGFKTNDDQTMCLDINECERDACGNGTCRNTIGSFNCRCNHGFILSHNNDCIDVDECASGNGNLCRNGQCINTVGSFQCQCNEGYEVAPDGRTCVDINECLLEPRKCAPGTCQNLDGSYRCICPPGYSLQNEKCEDIDECVEEPEICALGTCSNTEGSFKCLCPEGFSLSSSGRRCQDLRMSYCYAKFEGGKCSSPKSRNHSKQECCCALKGEGWGDPCELCPTEPDEAFRQICPYGSGIIVGPDDSAVDMDECKEPDVCKHGQCINTDGSYRCECPFGYILAGNECVDTDECSVGNPCGNGTCKNVIGGFECTCEEGFEPGPMMTCEDINECAQNPLLCAFRCVNTYGSYECKCPVGYVLREDRRMCKDEDECEEGKHDCTEKQMECKNLIGTYMCICGPGYQRRPDGEGCVDENECQTKPGICENGRCLNTRGSYTCECNDGFTASPNQDECLDNREGYCFTEVLQNMCQIGSSNRNPVTKSECCCDGGRGWGPHCEICPFQGTVAFKKLCPHGRGFMTNGADIDECKVIHDVCRNGECVNDRGSYHCICKTGYTPDITGTSCVDLNECNQAPKPCNFICKNTEGSYQCSCPKGYILQEDGRSCKDLDECATKQHNCQFLCVNTIGGFTCKCPPGFTQHHTSCIDNNECTSDINLCGSKGICQNTPGSFTCECQRGFSLDQTGSSCEDVDECEGNHRCQHGCQNIIGGYRCSCPQGYLQHYQWNQCVDENECLSAHICGGASCHNTLGSYKCMCPAGFQYEQFSGGCQDINECGSAQAPCSYGCSNTEGGYLCGCPPGYFRIGQGHCVSGMGMGRGNPEPPVSGEMDDNSLSPEACYECKINGYPKRGRKRRSTNETDASNIEDQSETEANVSLASWDVEKTAIFAFNISHVSNKVRILELLPALTTLTNHNRYLIESGNEDGFFKINQKEGISYLHFTKKKPVAGTYSLQISSTPLYKKKELNQLEDKYDKDYLSGELGDNLKMKIQVLLH
Domains	DOMAIN 81 112 EGF-like 1 DOMAIN 115 146 EGF-like 2 DOMAIN 147 178 EGF-like 3 DOMAIN 184 236 TB 1 DOMAIN 246 287 EGF-like 4 calcium-binding DOMAIN 288 329 EGF-like 5 calcium-binding DOMAIN 334 389 TB 2 DOMAIN 449 489 EGF-like 6 DOMAIN 490 529 EGF-like 7 calcium-binding DOMAIN 530 571 EGF-like 8 calcium-binding DOMAIN 572 612 EGF-like 9 calcium-binding DOMAIN 613 653 EGF-like 10 calcium-binding DOMAIN 659 711 TB 3 DOMAIN 723 764 EGF-like 11 calcium-binding DOMAIN 765 806 EGF-like 12 calcium-binding DOMAIN 807 846 EGF-like 13 calcium-binding DOMAIN 851 902 TB 4 DOMAIN 910 951 EGF-like 14 calcium-binding DOMAIN 956 1008 TB 5 DOMAIN 1028 1069 EGF-like 15 calcium-binding DOMAIN 1070 1112 EGF-like 16 calcium-binding DOMAIN 1113 1154 EGF-like 17 calcium-binding DOMAIN 1155 1196 EGF-like 18 calcium-binding DOMAIN 1197 1237 EGF-like 19 calcium-binding DOMAIN 1238 1279 EGF-like 20 calcium-binding DOMAIN 1280 1321 EGF-like 21 calcium-binding DOMAIN 1322 1362 EGF-like 22 calcium-binding DOMAIN 1363 1403 EGF-like 23 calcium-binding DOMAIN 1404 1445 EGF-like 24 calcium-binding DOMAIN 1446 1486 EGF-like 25 calcium-binding DOMAIN 1487 1527 EGF-like 26 calcium-binding DOMAIN 1532 1589 TB 6 DOMAIN 1606 1647 EGF-like 27 calcium-binding DOMAIN 1648 1688 EGF-like 28 calcium-binding DOMAIN 1693 1748 TB 7 DOMAIN 1766 1807 EGF-like 29 calcium-binding DOMAIN 1808 1848 EGF-like 30 calcium-binding DOMAIN 1849 1890 EGF-like 31 calcium-binding DOMAIN 1891 1929 EGF-like 32 calcium-binding DOMAIN 1930 1972 EGF-like 33 calcium-binding DOMAIN 1973 2012 EGF-like 34 calcium-binding DOMAIN 2013 2054 EGF-like 35 calcium-binding DOMAIN 2059 2111 TB 8 DOMAIN 2127 2165 EGF-like 36 calcium-binding DOMAIN 2166 2205 EGF-like 37 calcium-binding DOMAIN 2206 2246 EGF-like 38 calcium-binding DOMAIN 2247 2290 EGF-like 39 calcium-binding DOMAIN 2291 2332 EGF-like 40 calcium-binding DOMAIN 2337 2390 TB 9 DOMAIN 2402 2443 EGF-like 41 calcium-binding DOMAIN 2444 2484 EGF-like 42 calcium-binding DOMAIN 2485 2523 EGF-like 43 calcium-binding DOMAIN 2524 2566 EGF-like 44 calcium-binding DOMAIN 2567 2606 EGF-like 45 calcium-binding DOMAIN 2607 2647 EGF-like 46 calcium-binding DOMAIN 2648 2687 EGF-like 47 calcium-binding
EGF-like sequence regions	81 - 112 PICRHSCGDGFCSRPNMCTCPSGQIAPSCGSR 115 - 146 QHCNIRCMNGGSCSDDHCLCQKGYIGTHCGQP 147 - 178 VCESGCLNGGRCVAPNRCACTYGFTGPQCERD 246 - 287 DECQAIPGLCQGGNCINTVGSFECKCPAGHKLNEVSQKCEDI 288 - 329 DECSTIPGICEGGECTNTVSSYFCKCPPGFYTSPDGTRCIDV 449 - 489 DYCQLVRYLCQNGRCIPTPGSCRCECNKGFQLDLRGECIDV 490 - 529 DECEKNPCAGGECINNQGSYTCQCRAGYQSTLTRTECRDI 530 - 571 DECLQNGRICNNGRCINTDGSFHCVCNAGFHVTRDGKNCEDM 572 - 612 DECSIRNMCLNGMCINEDGSFKCICKPGFQLASDGRYCKDI 613 - 653 NECETPGICMNGRCVNTDGSYRCECFPGLAVGLDGRVCVDT 723 - 764 NECALDPDICPNGICENLRGTYKCICNSGYEVDSTGKNCVDI 765 - 806 NECVLNSLLCDNGQCRNTPGSFVCTCPKGFIYKPDLKTCEDI 807 - 846 DECESSPCINGVCKNSPGSFICECSSESTLDPTKTICIET 910 - 951 DECEVFPGVCKNGLCVNTRGSFKCQCPSGMTLDATGRICLDI 1028 - 1069 NECKMIPSLCTHGKCRNTIGSFKCRCDSGFALDSEERNCTDI 1070 - 1112 DECRISPDLCGRGQCVNTPGDFECKCDEGYESGFMMMKNCMDI 1113 - 1154 DECQRDPLLCRGGVCHNTEGSYRCECPPGHQLSPNISACIDI 1155 - 1196 NECELSAHLCPNGRCVNLIGKYQCACNPGYHSTPDRLFCVDI 1197 - 1237 DECSIMNGGCETFCTNSEGSYECSCQPGFALMPDQRSCTDI 1238 - 1279 DECEDNPNICDGGQCTNIPGEYRCLCYDGFMASEDMKTCVDV 1280 - 1321 NECDLNPNICLSGTCENTKGSFICHCDMGYSGKKGKTGCTDI 1322 - 1362 NECEIGAHNCGKHAVCTNTAGSFKCSCSPGWIGDGIKCTDL 1363 - 1403 DECSNGTHMCSQHADCKNTMGSYRCLCKEGYTGDGFTCTDL 1404 - 1445 DECSENLNLCGNGQCLNAPGGYRCECDMGFVPSADGKACEDI 1446 - 1486 DECSLPNICVFGTCHNLPGLFRCECEIGYELDRSGGNCTDV 1487 - 1527 NECLDPTTCISGNCVNTPGSYICDCPPDFELNPTRVGCVDT 1606 - 1647 DECQELPGLCQGGKCINTFGSFQCRCPTGYYLNEDTRVCDDV 1648 - 1688 NECETPGICGPGTCYNTVGNYTCICPPDYMQVNGGNNCMDM 1766 - 1807 DECREIPGVCENGVCINMVGSFRCECPVGFFYNDKLLVCEDI 1808 - 1848 DECQNGPVCQRNAECINTAGSYRCDCKPGYRFTSTGQCNDR 1849 - 1890 NECQEIPNICSHGQCIDTVGSFYCLCHTGFKTNDDQTMCLDI 1891 - 1929 NECERDACGNGTCRNTIGSFNCRCNHGFILSHNNDCIDV 1930 - 1972 DECASGNGNLCRNGQCINTVGSFQCQCNEGYEVAPDGRTCVDI 1973 - 2012 NECLLEPRKCAPGTCQNLDGSYRCICPPGYSLQNEKCEDI 2013 - 2054 DECVEEPEICALGTCSNTEGSFKCLCPEGFSLSSSGRRCQDL 2127 - 2165 DECKEPDVCKHGQCINTDGSYRCECPFGYILAGNECVDT 2166 - 2205 DECSVGNPCGNGTCKNVIGGFECTCEEGFEPGPMMTCEDI 2206 - 2246 NECAQNPLLCAFRCVNTYGSYECKCPVGYVLREDRRMCKDE 2247 - 2290 DECEEGKHDCTEKQMECKNLIGTYMCICGPGYQRRPDGEGCVDE 2291 - 2332 NECQTKPGICENGRCLNTRGSYTCECNDGFTASPNQDECLDN 2402 - 2443 DECKVIHDVCRNGECVNDRGSYHCICKTGYTPDITGTSCVDL 2444 - 2484 NECNQAPKPCNFICKNTEGSYQCSCPKGYILQEDGRSCKDL 2485 - 2523 DECATKQHNCQFLCVNTIGGFTCKCPPGFTQHHTSCIDN 2524 - 2566 NECTSDINLCGSKGICQNTPGSFTCECQRGFSLDQTGSSCEDV 2567 - 2606 DECEGNHRCQHGCQNIIGGYRCSCPQGYLQHYQWNQCVDE 2607 - 2647 NECLSAHICGGASCHNTLGSYKCMCPAGFQYEQFSGGCQDI 2648 - 2687 NECGSAQAPCSYGCSNTEGGYLCGCPPGYFRIGQGHCVSG
Function	"Fibrillin-1: Structural component of the 10-12 nm diameter microfibrils of the extracellular matrix, which conveys both structural and regulatory properties to load-bearing connective tissues (PubMed:1860873, PubMed:15062093). Fibrillin-1-containing microfibrils provide long-term force bearing structural support. In tissues such as the lung, blood vessels and skin, microfibrils form the periphery of the elastic fiber, acting as a scaffold for the deposition of elastin. In addition, microfibrils can occur as elastin-independent networks in tissues such as the ciliary zonule, tendon, cornea and glomerulus where they provide tensile strength and have anchoring roles. Fibrillin-1 also plays a key role in tissue homeostasis through specific interactions with growth factors, such as the bone morphogenetic proteins (BMPs), growth and differentiation factors (GDFs) and latent transforming growth factor-beta-binding proteins (LTBPs), cell-surface integrins and other extracellular matrix protein and proteoglycan components (PubMed:27026396). Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (By similarity). Negatively regulates osteoclastogenesis by binding and sequestering an osteoclast differentiation and activation factor TNFSF11. This leads to disruption of TNFSF11-induced Ca(2+) signaling and impairment of TNFSF11-mediated nuclear translocation and activation of transcription factor NFATC1 which regulates genes important for osteoclast differentiation and function (PubMed:24039232). Mediates cell adhesion via its binding to cell surface receptors integrins ITGAV:ITGB3 and ITGA5:ITGB1 (PubMed:12807887, PubMed:17158881). Binds heparin and this interaction has an important role in the assembly of microfibrils (PubMed:11461921).; Asprosin: Hormone that targets the liver to increase plasma glucose levels. Secreted by white adipose tissue and circulates in the plasma. Acts in response to fasting and promotes blood glucose elevation by binding to the surface of hepatocytes. Promotes hepatocyte glucose release by activating the protein kinase A activity in the liver, resulting in rapid glucose release into the circulation"
Motifs	MOTIF 1541 1543 Cell attachment site
Mutation	"1542 1542 G->D: Loss of integrin-mediated cell adhesion 2728 2728 R->A: Abolishes furin cleavage site, leading to defects in protein processing at the C-terminus 2731 2731 R->K: Abolishes furin cleavage site, leading to defects in protein processing at the C-terminus 2732 2732 S->T: Defects in protein processing at the C-terminus"
Disease	"DISEASE: Marfan syndrome (MFS) [MIM:154700]: A hereditary disorder of connective tissue that affects the skeletal, ocular, and cardiovascular systems A wide variety of skeletal abnormalities occurs with Marfan syndrome, including scoliosis, chest wall deformity, tall stature, abnormal joint mobility Ectopia lentis occurs in most of the patients and is almost always bilateral The leading cause of premature death is progressive dilation of the aortic root and ascending aorta, causing aortic incompetence and dissection Neonatal Marfan syndrome is the most severe form resulting in death from cardiorespiratory failure in the first few years of life 68} Note=The disease is caused by mutations affecting the gene represented in this entry The majority of the more than thousand mutations in FBN1 currently known are point mutations, the rest are frameshifts and splice site mutations Marfan syndrome has been suggested in at least 2 historical figures, Abraham Lincoln and Paganini ; DISEASE: Ectopia lentis 1, isolated, autosomal dominant (ECTOL1) [MIM:129600]: An ocular abnormality characterized by partial or complete displacement of the lens from its space resulting from defective zonule formation Note=The disease is caused by mutations affecting the gene represented in this entry ; DISEASE: Weill-Marchesani syndrome 2 (WMS2) [MIM:608328]: A rare connective tissue disorder characterized by short stature, brachydactyly, joint stiffness, and eye abnormalities including microspherophakia, ectopia lentis, severe myopia and glaucoma Note=The disease is caused by mutations affecting the gene represented in this entry ; DISEASE: Overlap connective tissue disease (OCTD) [MIM:604308]: Heritable disorder of connective tissue characterized by involvement of the mitral valve, aorta, skeleton, and skin MASS syndrome is closely resembling both the Marfan syndrome and the Barlow syndrome However, no dislocation of the lenses or aneurysmal changes occur in the aorta, and the mitral valve prolapse is by no means invariable Note=The disease is caused by mutations affecting the gene represented in this entry ; DISEASE: Stiff skin syndrome (SSKS) [MIM:184900]: A syndrome characterized by hard, thick skin, usually over the entire body, which limits joint mobility and causes flexion contractures Other occasional findings include lipodystrophy and muscle weakness Note=The disease is caused by mutations affecting the gene represented in this entry ; DISEASE: Geleophysic dysplasia 2 (GPHYSD2) [MIM:614185]: An autosomal dominant disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening Radiologic features include delayed bone age, cone-shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies Affected individuals have characteristic facial features including a 'happy' face with full cheeks, shortened nose, hypertelorism, long and flat philtrum, and thin upper lip Other distinctive features include progressive cardiac valvular thickening often leading to an early death, toe walking, tracheal stenosis, respiratory insufficiency, and lysosomal-like storage vacuoles in various tissues Note=The disease is caused by mutations affecting the gene represented in this entry ; DISEASE: Acromicric dysplasia (ACMICD) [MIM:102370]: An autosomal dominant disorder characterized by severe short stature, short hands and feet, joint limitations, and skin thickening Radiologic features include delayed bone age, cone-shaped epiphyses, shortened long tubular bones, and ovoid vertebral bodies Affected individuals have distinct facial features, including round face, well-defined eyebrows, long eyelashes, bulbous nose with anteverted nostrils, long and prominent philtrum, and thick lips with a small mouth Other characteristic features include hoarse voice and pseudomuscular build, and there are distinct skeletal features as well, including an internal notch of the femoral head, internal notch of the second metacarpal, and external notch of the fifth metacarpal Note=The disease is caused by mutations affecting the gene represented in this entry ; DISEASE: Marfan lipodystrophy syndrome (MFLS) [MIM:616914]: A syndrome characterized by congenital lipodystrophy, a progeroid facial appearance due to lack of subcutaneous fat, and variable signs of Marfan syndrome Clinical features include premature birth with an accelerated linear growth disproportionate to the weight gain, ectopia lentis, aortic dilatation, dural ectasia, and arachnodactyly Mental and motor development are within normal limits Note=The disease is caused by mutations affecting the gene represented in this entry Asprosin: Mutations specifically affect Asprosin, a hormone peptide present at the C-terminus of Fibrillin-1 chain, which is cleaved from Fibrillin-1 following secretion (PubMed:27087445)"

P35555 Proteins EGF-like domain Repeats