Fbn1
entrez
14118
canonical
uniprot
Q61554
canonical
ensembl
ENSMUSG00000027204
resolver
ensp
ENSMUSP00000028633
resolver
ensp
ENSMUSP00000099524
resolver
enst
ENSMUST00000028633
resolver
enst
ENSMUST00000103234
resolver
genesymbol
Fbn1
resolver
genesymbol_syn
Fbn-1
resolver
uniprot
A2AQ53
resolver
uniprot
Q60826
resolver
uniprot_entry
FBN1_MOUSE
resolver
uniprot_sec
A2AQ53
resolver
uniprot_sec
Q60826
resolver
amino_acid_sequence
MRRGGLLEVALAFALLLESYTSHGADANLEAGSLKETRANRAKRRGGGGHDALKGPNVCGSRYNAYCCPGWKTLPGGNQCIVPICRHSCGDGFCSRPNMCTCPSGQISPSCGSRSIQHCSIRCMNGGSCSDDHCLCQKGYIGTHCGQPVCESGCLNGGRCVAPNRCACTYGFTGPQCERDYRTGPCFTVVSNQMCQGQLSGIVCTKTLCCATVGRAWGHPCEMCPAQPHPCRRGFIPNIRTGACQDVDECQAIPGMCQGGNCINTVGSFECKCPAGHKFNEVSQKCEDIDECSTIPGVCDGGECTNTVSSYFCKCPPGFYTSPDGTRCVDVRPGYCYTALANGRCSNQLPQSITKMQCCCDLGRCWSPGVTVAPEMCPIRSTEDFNKLCSVPLVIPGRPEYPPPPIGPLPPVQPVPPGYPPGPVIPAPRPPPEYPYPSPSREPPRVLPFNVTDYCQLVRYLCQNGRCIPTPGSYRCECNKGFQLDIRGECIDVDECEKNPCTGGECINNQGSYTCHCRAGYQSTLTRTECRDIDECLQNGRICNNGRCINTDGSFHCVCNAGFHVTRDGKNCEDMDECSIRNMCLNGMCINEDGSFKCICKPGFQLASDGRYCKDINECETPGICMNGRCVNTDGSYRCECFPGLAVGLDGRVCVDTHMRSTCYGGYRRGQCVKPLFGAVTKSECCCASTEYAFGEPCQPCPAQNSAEYQALCSSGPGMTSAGTDINECALDPDICPNGICENLRGTYKCICNSGYEVDITGKNCVDINECVLNSLLCDNGQCRNTPGSFVCTCPKGFVYKPDLKTCEDIDECESSPCINGVCKNSPGSFICECSPESTLDPTKTICIETIKGTCWQTVIDGRCEININGATLKSECCSSLGAAWGSPCTICQLDPICGKGFSRIKGTQCEDINECEVFPGVCKNGLCVNSRGSFKCECPNGMTLDATGRICLDIRLETCFLKYDDEECTLPIAGRHRMDACCCSVGAAWGTEECEECPLRNSREYEELCPRGPGFATKDITNGKPFFKDINECKMIPSLCTHGKCRNTIGSFKCRCDSGFALDSEERNCTDIDECRISPDLCGRGQCVNTPGDFECKCDEGYESGFMMMKNCMDIDECQRDPLLCRGGICHNTEGSYRCECPPGHQLSPNISACIDINECELSANLCPHGRCVNLIGKYQCACNPGYHPTHDRLFCVDIDECSIMNGGCETFCTNSDGSYECSCQPGFALMPDQRSCTDIDECEDNPNICDGGQCTNIPGEYRCLCYDGFMASEDMKTCVDVNECDLNPNICLSGTCENTKGSFICHCDMGYSGKKGKTGCTDINECEIGAHNCGRHAVCTNTAGSFKCSCSPGWIGDGIKCTDLDECSNGTHMCSQHADCKNTMGSYRCLCKDGYTGDGFTCTDLDECSENLNLCGNGQCLNAPGGYRCECDMGFVPSADGKACEDIDECSLPNICVFGTCHNLPGLFRCECEIGYELDRSGGNCTDVNECLDPTTCISGNCVNTPGSYTCDCPPDFELNPTRVGCVDTRSGNCYLDIRPRGDNGDTACSNEIGVGVSKASCCCSLGKAWGTPCELCPSVNTSEYKILCPGGEGFRPNPITVILEDIDECQELPGLCQGGKCINTFGSFQCRCPTGYYLNEDTRVCDDVNECETPGICGPGTCYNTVGNYTCICPPDYMQVNGGNNCMDMRRSLCYRNYYADNQTCDGELLFNMTKKMCCCSYNIGRAWNKPCEQCPIPSTDEFATLCGSQRPGFVIDIYTGLPVDIDECREIPGVCENGVCINMVGSFRCECPVGFFYNDKLLVCEDIDECQNGPVCQRNAECINTAGSYRCDCKPGYRLTSTGQCNDRNECQEIPNICSHGQCIDTVGSFYCLCHTGFKTNVDQTMCLDINECERDACGNGTCRNTIGSFNCRCNHGFILSHNNDCIDVDECATGNGNLCRNGQCVNTVGSFQCRCNEGYEVAPDGRTCVDINECVLDPGKCAPGTCQNLDGSYRCICPPGYSLQNDKCEDIDECVEEPEICALGTCSNTEGSFKCLCPEGFSLSSTGRRCQDLRMSYCYAKFEGGKCSSPKSRNHSKQECCCALKGEGWGDPCELCPTEPDEAFRQICPFGSGIIVGPDDSAVDMDECKEPDVCRHGQCINTDGSYRCECPFGYILEGNECVDTDECSVGNPCGNGTCKNVIGGFECTCEEGFEPGPMMTCEDINECAQNPLLCAFRCVNTYGSYECKCPVGYVLREDRRMCKDEDECAEGKHDCTEKQMECKNLIGTYMCICGPGYQRRPDGEGCIDENECQTKPGICENGRCLNTLGSYTCECNDGFTASPTQDECLDNREGYCFSEVLQNMCQIGSSNRNPVTKSECCCDGGRGWGPHCEICPFEGTVAYKKLCPHGRGFMTNGADIDECKVIHDVCRNGECVNDRGSYHCICKTGYTPDITGTACVDLNECNQAPKPCNFICKNTEGSYQCSCPKGYILQEDGRSCKDLDECATKQHNCQFLCVNTIGGFTCKCPPGFTQHHTACIDNNECTSDINLCGSKGVCQNTPGSFTCECQRGFSLDQSGASCEDVDECEGNHRCQHGCQNIIGGYRCSCPQGYLQHYQWNQCVDENECLSAHVCGGASCHNTLGSYKCMCPTGFQYEQFSGGCQDINECGSSQAPCSYGCSNTEGGYLCGCPPGYFRIGQGHCVSGMGMGRGGPEPPASSEMDDNSLSPEACYECKINGYPKRGRKRRSTNETDASDIQDGSEMEANVSLASWDVEKPASFAFNISHVNNKVRILELLPALTTLMNHNRYLIESGNEDGFFKINQKEGVSYLHFTKKKPVAGTYSLQISSTPLYKKKELNQLEDRYDKDYLSGELGDNLKMKIQILLH
uniprot
proteins
function
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. 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 (By similarity). Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively (PubMed:20855508). 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. Binds heparin and this interaction plays an important role in the assembly of microfibrils (By similarity). {ECO:0000250|UniProtKB:P35555, ECO:0000269|PubMed:20855508, ECO:0000269|PubMed:24039232}.; FUNCTION: [Asprosin]: Adipokine secreted by white adipose tissue that plays an important regulatory role in the glucose metabolism of liver, muscle and pancreas (PubMed:30997682, PubMed:31230984). Hormone that targets the liver in response to fasting to increase plasma glucose levels (PubMed:31230984). Binds the olfactory receptor Olfr734 at the surface of hepatocytes and promotes hepatocyte glucose release by activating the protein kinase A activity in the liver, resulting in rapid glucose release into the circulation (PubMed:31230984). May act as a regulator of adaptive thermogenesis by inhibiting browning and energy consumption, while increasing lipid deposition in white adipose tissue (PubMed:33705351). Also acts as an orexigenic hormone that increases appetite: crosses the blood brain barrier and exerts effects on the hypothalamus (PubMed:29106398). In the arcuate nucleus of the hypothalamus, asprosin directly activates orexigenic AgRP neurons and indirectly inhibits anorexigenic POMC neurons, resulting in appetite stimulation (PubMed:29106398, PubMed:32337066). Activates orexigenic AgRP neurons via binding to the olfactory receptor Olfr734 (PubMed:32337066). May also play a role in sperm motility in testis via interaction with Olfr734 receptor (PubMed:31798959). {ECO:0000269|PubMed:29106398, ECO:0000269|PubMed:30997682, ECO:0000269|PubMed:31230984, ECO:0000269|PubMed:31798959, ECO:0000269|PubMed:32337066, ECO:0000269|PubMed:33705351}.
uniprot
proteins
mass_dalton
312298
uniprot
proteins
post_translational_modification
PTM: Cleavage of N- and C-terminus by furin is required for incorporation into the extracellular matrix and assembly into microfibrils. The C-terminus, which corresponds to the Asprosin chain, was initially thought to constitute a propeptide. Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin, an essential step for incorporation of Fibrillin-1 into the nascent microfibrils. {ECO:0000250|UniProtKB:P35555}.; PTM: [Fibrillin-1]: Forms intermolecular disulfide bonds either with other fibrillin-1 molecules or with other components of the microfibrils. {ECO:0000250|UniProtKB:P35555}.; PTM: O-glycosylated on serine residues by POGLUT2 and POGLUT3 which is necessary for efficient protein secretion. {ECO:0000250|UniProtKB:P35555}.
uniprot
proteins
protein_family
Fibrillin family
uniprot
proteins
pubmed
16407178
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19940141
uniprot
proteins
pubmed
20855508
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24039232
uniprot
proteins
pubmed
27087445
uniprot
proteins
pubmed
29106398
uniprot
proteins
pubmed
30997682
uniprot
proteins
pubmed
31230984
uniprot
proteins
pubmed
31798959
uniprot
proteins
pubmed
32337066
uniprot
proteins
pubmed
33705351
uniprot
proteins
pubmed
33904407
uniprot
proteins
pubmed
7829516
uniprot
proteins
sequence_length
2873
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P35555}. Note=Fibrillin-1 and Asprosin chains are still linked together during the secretion from cells, but are subsequently separated by furin. {ECO:0000250|UniProtKB:P35555}.; SUBCELLULAR LOCATION: [Fibrillin-1]: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:24039232}.; SUBCELLULAR LOCATION: [Asprosin]: Secreted {ECO:0000250|UniProtKB:P35555}. Note=Secreted by white adipose tissue and circulates in the plasma. {ECO:0000250|UniProtKB:P35555}.
uniprot
proteins